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Product listing: Vimentin (D21H3) XP® Rabbit mAb (Alexa Fluor® 555 Conjugate), UniProt ID P08670 #9855 to WAPL (D9J1U) Rabbit mAb, UniProt ID Q7Z5K2 #77428

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vimentin (D21H3) XP® Rabbit mAb #5741.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$260
100 µg
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: VCP-interacting membrane protein (VIMP, selenoprotein S) is a putative reductase and endoplasmic reticulum (ER)-resident protein involved in the ER-associated degradation (ERAD) pathway (1,2). Research studies indicate that VIMP may play a protective role against inflammation and reduce ER-stress (3). The VIMP protein is a single-pass, transmembrane protein that recruits the cytosolic p97/VCP AAA-ATPase and its cofactors, UFD1 and NPL4, to the ER membrane (4). An ER membrane complex containing Derlin-1 and VIMP forms a critical node in the ERAD machinery and links substrate recognition in the ER lumen with the retrotranslocation function of the p97/VCP AAA-ATPase in the cytosol (1,4). Polymorphisms in the corresponding VIMP gene are associated with spontaneous preterm births and cardiovascular disease risk (5,6) while other studies do not support a correspondence between VIMP polymorphisms and inflammatory disorders (7).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Vinculin (E1E9V) XP® Rabbit mAb #13901.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development (1-4). Three structural vinculin domains include an amino-terminal head, a short, flexible proline-rich region and a carboxy-terminal tail (1). In the inactive state, the head and tail domains of vinculin interact to form a closed confirmation. The open and active form of vinculin translocates to focal adhesions where it is thought to be involved in anchoring F-actin to the membrane and regulation of cell migration (2). Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC-α and Tyr100 and Tyr1065 by Src kinases weakens the head-tail interaction (5,6). This change in vinculin allows the binding of a number of other proteins, including talin, α-actinin and paxillin, which disrupts the head-tail interaction and initiates the conformational change from the inactive to active state (2,4). Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth (7,8). This is supported by a demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Western Blotting

Background: Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development (1-4). Three structural vinculin domains include an amino-terminal head, a short, flexible proline-rich region and a carboxy-terminal tail (1). In the inactive state, the head and tail domains of vinculin interact to form a closed confirmation. The open and active form of vinculin translocates to focal adhesions where it is thought to be involved in anchoring F-actin to the membrane and regulation of cell migration (2). Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC-α and Tyr100 and Tyr1065 by Src kinases weakens the head-tail interaction (5,6). This change in vinculin allows the binding of a number of other proteins, including talin, α-actinin and paxillin, which disrupts the head-tail interaction and initiates the conformational change from the inactive to active state (2,4). Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth (7,8). This is supported by a demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: Vasoactive intestinal polypeptide (VIP) is a neuropeptide synthesized as a precursor that is processed to an active mature peptide of 28 residues (1). VIP is produced by neurons, endocrine, and immune cells and is expressed in many tissues, in agreement with its various biological functions (2). VIP acts through activation of two receptors belonging to the G protein-coupled receptor family, VPAC1 and VPAC2 (2) and elicits several effects such as vasodilation, regulation of smooth muscle cell contractility, and blood flow in the gastrointestinal track (3,4). In addition, VIP is involved in the regulation of T cell differentiation (6), and in immunosuppression (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Vasoactive intestinal polypeptide (VIP) is a neuropeptide synthesized as a precursor that is processed to an active mature peptide of 28 residues (1). VIP is produced by neurons, endocrine, and immune cells and is expressed in many tissues, in agreement with its various biological functions (2). VIP acts through activation of two receptors belonging to the G protein-coupled receptor family, VPAC1 and VPAC2 (2) and elicits several effects such as vasodilation, regulation of smooth muscle cell contractility, and blood flow in the gastrointestinal track (3,4). In addition, VIP is involved in the regulation of T cell differentiation (6), and in immunosuppression (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The antiviral protein viperin (RSAD2) is induced by viral infection, lipopolysaccharides (LPS), polyriboinosinic polyribocytidylic acid [poly(I:C)], and interferons (1,2). Viperin protein localizes to the ER and redistributes to the Golgi and then to lipid droplets following viral infection (1,3). Viruses are known to use lipid droplets for replication, and the localization of the antiviral viperin protein to these lipid droplets is likely part of a cellular mechanism to inhibit these pathogens (4). Research studies indicate that induction of viperin by HIV in human macrophages inhibits virus production, and that siRNA targeting viperin reduced the inhibition of HIV replication observed in poly(I:C) treated astrocytes (5,6). Additional research suggests that human cytomegalovirus (HCMV) co-opts viperin protein function, resulting in an interaction between viperin and the viral protein vMIA. This association leads to relocalization of viperin to mitochondria, resulting in disruption of ATP generation and the actin cytoskeleton, and increased viral infection (7). The viperin protein also contributes to innate immune signaling by recruiting IRAK1 ant TRAF6 to lipid droplets, which results in activation of IRF7 and induction of type I interferon (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Visinin-like Protein 1, also called VILIP-1 and VSNL1, is a calcium-sensing protein in the central nervous system. Visinin-like Protein 1 exhibits a widespread distribution with high expression in the CNS, and lower expression levels in some peripheral tissues (1). Visinin-like Protein 1 responds to increased intracellular calcium concentration by translocating from the cytoplasm to membranes through calcium-dependent myristoylation at its N-terminus that allows interaction with membranes (2). This change in localization has been proposed to facilitate the activation of compartment-specific signal transduction for the selective activation of downstream signaling cascades (3,4). In Alzheimer’s disease, Visinin-like Protein 1 expression is decreased in the brain, including a reduced number of Visinin-like Protein 1 immunoreactive neurons (5); however, the presence of the protein is increased in the CSF (6), suggesting that it is released from neurons during insults.

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VISTA (D1L2G™) XP® Rabbit mAb #64953.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VISTA (D1L2G™) XP® Rabbit mAb #64953.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VISTA (D1L2G™) XP® Rabbit mAb #64953.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VISTA (D5L5T) XP® Rabbit mAb #54979.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VISTA (D5L5T) XP® Rabbit mAb #54979.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: VISTA (V-Domain Ig Suppressor of T Cell Activation) is a negative checkpoint control protein that regulates T cell activation and immune responses. VISTA, which contains a single Ig-like V-type domain, a transmembrane domain, and an intracellular domain, has sequence similarity to both the B7 and CD28 family members. Although primarily expressed by myeloid cells, VISTA is also expressed by CD4+, CD8+, and FoxP3+ T-cells. Thus, VISTA is described as both a ligand and a receptor (1-3). Blocking VISTA induces T-cell activation and proliferation, and potentiates disease severity in the EAE model (1). Furthermore, genetic deletion of VISTA in mice leads to spontaneous T-cell activation and chronic inflammation (4,5). In mouse models of cancer, neutralization of VISTA enhances T-cell proliferation and effector function and increases tumor infiltration, suggesting VISTA blockade could be an effective strategy for tumor immunotherapy (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Although originally identified based on their roles in calcium and bone homeostasis, the vitamin D3 receptor (VDR/NR1I1) and its ligand 1-α, 25-dihydroxycholecalciferol [1α, 25(OH)2D3] are now recognized to exert biological effects in almost every tissue of the human body. Targets for vitamin D signaling include the central nervous system, skin, immune system, endocrine glands, kidney, and colon. At the cellular level, vitamin D signaling affects proliferation, differentiation, and apoptosis of both normal and transformed cells. Within the steroid receptor gene family, VDR belongs to the NR1I subfamily that also includes NR1I2/PXR and NR1I3/CAR. The human VDR gene is composed of 11 exons that encode six domains (A-F) of the full length VDR protein, which includes an N-terminal dual zinc finger DNA binding domain, a C-terminal ligand-binding activity domain, and an extensive unstructured region that links the two functional domains together (1). Upon 1α, 25(OH)2D3 binding to the hormone ligand-binding domain, VDR is stabilized by the phosphorylation of Ser51 in the DNA-binding domain by PKC (2), and Ser208 in the hinge region by casein kinase II (3). VDR associates with the retinoic acid receptor (RXR) through dimerization domains. The 1α, 25(OH)2D3-VDR-RXR complex binds to the vitamin D response elements (VDREs) in the promoters of target genes through the DNA-binding domain. Ligand-induced conformation changes in VDR results in the dissociation of the co-repressor, silencing-mediator for retinoid and thyroid hormone receptors (SMRT), and allows interaction of the VDR activation function (AF2) transactivation domain with transcriptional coactivators (1).Studies have shown that variable VDR expression is associated with different forms or stages of cancer and likely results from tissue-type variation in 1α, 25(OH)2D3 signaling. In the case of colon cancer, research indicates that VDR expression is relatively higher in hyperplastic colon polyps and during early tumorigenesis but diminishes in later stage, poorly differentiated tumors. Multiple studies suggest that 1α, 25(OH)2D3 may be an attractive target for development as a therapeutic anticancer agent (4,5) .

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Mitochondria are membrane-bound subcellular organelles critical to many functions in eukaryotic cells (1). Several mechanisms have been found to play a role in mitochondria quality control (2). A recent study identified mitochondria-associated protein degradation as one such mechanism (1,2). The study showed that VMS1 (VCP/Cdc48-associated mitochondrial stress-responsive) interacts with VCP/Cdc48 and Npl4, two components in the endoplasmic reticulum-associated protein degradation pathway, and mediates the degradation of damaged mitochondrial proteins under stress conditions (1). Defective VMS1 compromises mitochondrial functions and cell viability (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The HIV-1 viral protein R (Vpr)-binding protein (VPRBP, DCAF1) is a substrate-specific adaptor for the CUL4-based ubiquitin ligase complex that consists of CUL4A, RBX1, and DDB1 (1). VPRBP protein structure contains a central LIS1 homology (LisH) motif responsible for dimerization, and two carboxy-terminal WD-40 motifs involved in Vpr and DDB1 binding (2-4). Research studies demonstrate that VPRBP plays a role in hepatic lipid metabolism by promoting the ubiquitin-dependent proteasomal degradation of the TR4 nuclear receptor, which is involved in lipid homeostasis (5). The VPRBP protein plays a role in mammalian germ cell development through regulation of TET methylcytosine dioxygenase activation (6). Additional studies show that VPRBP exhibits kinase activity and phosphorylates histone H2A at Ser120, which blocks tumor suppressor gene transcription (7). The tumor suppressor Merlin/NF2 inhibits tumorigenesis through interaction with and suppression of the CUL4A-RBX1-DDB1-VPRBP complex (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Retromer is a heteropentameric protein complex that consists of two protein compounds, a sortin-nexin dimer and a trimeric VPS26-VPS29-VPS35 protein subcomplex. The retromer complex associates with endosomes at their cytosolic side to mediate retrograde transport of transmembrane proteins from endosomes to the trans-Golgi network (1-3). Vacuolar protein sorting-associated protein 29 (VPS29) is considered a cryptic metallophosphoesterase, as it contains a conserved metallophosphoesterase-fold that includes a phenylalanine in place of an essential histidine residue within the active site (4). While VPS29 is capable of binding metal ions, it does so with low affinity and exhibits no enzymatic activity. Instead, VPS29 serves as a scaffold protein that interacts with the carboxy-terminal region of VPS35 and is essential for association of the retromer with other endosomal transport proteins (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The vaccinia-related kinase (VRK) proteins are a new group of Ser/Thr kinases in the human kinome. This mammalian kinase family comprises three members, VRK1, VRK2, and VRK3 (1-3). The VRK1 has autophosphorylation activity and phosphorylates several transcription factors, including p53 (4), ATF2 (5), and c-Jun (6). VRK2 is associated with the endoplasmic reticulum (7). VRK3 suppresses Erk activity through direct interaction and activation of the MAP kinase phosphatase VHR (8). Further functional and structural analysis of VRK proteins will elucidate important new aspects of cell regulation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Vesicle transport through interaction with t-SNAREs homolog 1 (Vti1) has two protein members, Vti1a and Vti1b. Human Vti1 was first identified as a homolog of the yeast v-SNARE Vti1p and was able to functionally rescue the phenotype of Vti1p-deficient yeast (1). The mammalian proteins Vti1a and Vti1b exhibit distinct but overlapping localization. Vti1a and Vti1b are both localized in the trans-Golgi network, with Vti1a also found in the Golgi apparatus and Vti1b in endosomes (2). Vti1 proteins have been implicated in a number of protein-protein interactions with partners such as VAMP4, syntaxin 6, syntaxin 8, syntaxin 16, and synaptobrevin (2-4).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: VWF (Von Willebrand factor) is a multimeric plasma glycoprotein that promotes adhesion of platelets to sites of vascular injury (1). Mature circulating VWF is made up of disulfide-bonded multimers that are in a complex with factor VIII (2). VWF is stored in secretory Weibel-Palade bodies in endothelial cells (3,4). It is synthesized as a large precursor protein and undergoes extensive posttranslational modifications including dimerization in the endoplasmic reticulum followed by cleavage of the pro-peptide and multimerization in the Golgi apparatus (3,4). VWF is important in hemostasis, and genetic defects in the structure and modification of VWF can cause von Willebrand disease (VWD), the most common congenital bleeding disorder in humans (5).  Alternatively, increased levels of VWF have been shown to be involved in acute coronary thrombosis and are a clinical risk marker for atherosclerosis (6). VWF has also been shown to have a role in inflammation, functioning as an adhesive site for a variety of leukocyte subsets (7). Through siRNA experiments and the use VWF-deficient mice, it has also been shown that VWF regulates angiogenesis (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The cohesin protein complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). WAPL, also wings apart-like or WAPAL, is a chromatin-associated protein that binds to the cohesin protein complex and regulates its function and its interaction with chromatin (3,4). WAPL, through its interaction with cohesin, is important in the regulation of chromosome structure, cell cycle progression and appropriate chromosome segregation (5,6). Depletion of WAPL leads to segregation errors and DNA damage, and in p53 deficient cells leads to aneuploidy (6).