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Product listing: TIF1β (4E1) Mouse mAb, UniProt ID Q13263 #5868 to TNFRSF8/CD30 (E4L4I) XP® Rabbit mAb, UniProt ID P28908 #54535

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: TIF1β is a member of the TIF1 (transcriptional intermediary factor 1) family, a group of transcriptional regulators that play key roles in development and differentiation. Members of this family are characterized by the presence of two conserved motifs – an N-terminal RING-B box-coiled-coil motif and a C-terminal PHD finger and bromodomain unit (1,2). TIF1β is a corepressor for KRAB (Kruppel associated box) domain containing zinc finger proteins. The KRAB domain containing zinc finger proteins are a large group of transcription factors that are vertebrate-specific, varied in their expression patterns between species, and thought to regulate gene transcription programs that control speciation (3,4).TIF1β has been shown to be essential for early embryonic development and spermatogenesis (6,5). It functions to either activate or repress transcription in response to environmental or developmental signals by chromatin remodeling and histone modification. The recruitment and association of TIF1β with heterochromatin protein (HP1) is essential for transcriptional repression, and for progression through differentiation of F9 embryonic carcinoma cells (6,7). TIF1β also plays a role in the DNA damage response. Phosphorylation of TIF1β on Ser842 occurs in an ATM-dependent manner in response to genotoxic stress and is thought to be essential for chromatin relaxation, which is in turn required for the DNA damage response (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: TIF1β is a member of the TIF1 (transcriptional intermediary factor 1) family, a group of transcriptional regulators that play key roles in development and differentiation. Members of this family are characterized by the presence of two conserved motifs – an N-terminal RING-B box-coiled-coil motif and a C-terminal PHD finger and bromodomain unit (1,2). TIF1β is a corepressor for KRAB (Kruppel associated box) domain containing zinc finger proteins. The KRAB domain containing zinc finger proteins are a large group of transcription factors that are vertebrate-specific, varied in their expression patterns between species, and thought to regulate gene transcription programs that control speciation (3,4).TIF1β has been shown to be essential for early embryonic development and spermatogenesis (6,5). It functions to either activate or repress transcription in response to environmental or developmental signals by chromatin remodeling and histone modification. The recruitment and association of TIF1β with heterochromatin protein (HP1) is essential for transcriptional repression, and for progression through differentiation of F9 embryonic carcinoma cells (6,7). TIF1β also plays a role in the DNA damage response. Phosphorylation of TIF1β on Ser842 occurs in an ATM-dependent manner in response to genotoxic stress and is thought to be essential for chromatin relaxation, which is in turn required for the DNA damage response (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein regulates the cellular response to multiple stresses, including DNA damage and oxidative stress. Activation of p53 can lead to cell cycle arrest and DNA repair, or apoptosis (1). Activated p53 transcription factor regulates the expression of multiple genes that regulate cell metabolism and the cell cycle. One p53-inducible gene is C12orf5, which encodes for a fructose-2,6-bisphosphatase known as TIGAR. TP53-inducible glycolysis and apoptosis regulator (TIGAR) protects cells from oxidative stress as it negatively regulates glycolysis and reduces the production of reactive oxygen species (ROS) in cells (2,3). Research studies demonstrate that knockdown of TIGAR expression induces autophagy and apoptosis (4,5), and its expression protects cells from ROS-related cell death (6,7). Additional studies show that TIGAR promotes cell cycle arrest and supports dephosphorylation of the retinoblastoma (Rb) protein (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: T-cell immunoreceptor with Ig and ITIM domains (TIGIT), also known as VSIG9, VSTM3, and WUCAM, is a member of the poliovirus receptor family of immunoglobulin proteins (1-3). TIGIT is expressed at low levels on subsets of T cells and NK cells, and is upregulated at the protein level following activation of these cells (1-4). TIGIT marks exhausted T cells in the tumor microenvironment (5) and during human immunodeficiency virus (HIV) infection (6). Research has shown TIGIT interacts with several receptors expressed on antigen presenting cells, such as dendritic cells and macrophages, as well as tumor cells and cells of the microenvironment. TIGIT binds with high affinity to PVR/CD155, and with low affinity to Nectin-2/CD112 and Nectin-3/CD113 (2,4,7). Upon binding to its ligands, TIGIT suppresses T cell activation, and inhibits T and NK cell cytotoxicity. This inhibition can be blocked using monoclonal antibodies directed at the ITIM domain of TIGIT, resulting in rejuvenated antigen-specific CD8+ T cell responses in tumors and during HIV infection (5,6,8). Three potential isoforms of TIGIT have been computationally mapped (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-1 (HAVCR1 (hepatitis A virus cellular receptor 1), KIM-1 (kidney injury molecule-1) was originally identified as a receptor for hepatitis A virus (1). TIM-1 also acts as a costimulatory receptor on T cells and following activation, associates with the TCR complex to upregulate signaling and cytokine production (2-5). Another TIM family member, TIM-4, is expressed by antigen presenting cells and is a ligand for TIM-1 (6). TIM-1 expressed by Th1 and Th17 cells was also recently shown to interact with P-selectin to mediate T cell trafficking during inflammation and autoimmune disease (7). NKT cells also express TIM-1, and engagement of TIM-1 on NKT cells leads to increased production of IL-4, but decreased production of IFN-gamma (8). TIM-1 is also a receptor for phosphatidylserine exposed by cells undergoing apoptosis. Detection of phosphatidylserine by TIM-1 expressed on NKT cells results in activation, proliferation, and cytokine production (9). Expression of TIM-1 on regulatory B cells is required for optimal production of IL-10. Mice lacking the TIM-1 mucin domain have decreased production of IL-10 by regulatory B cells, hyperactive T cells, increased levels of inflammatory cytokines, and enhanced severity of autoimmune disease (10,11). In addition, TIM-1 polymorphisms are associated with susceptibility to atopic diseases including asthma (12,13). Finally, expression of TIM-1 is increased in renal tubular epithelial cells following kidney injury (14).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation (1-3 ). TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer (4,5), and tumor-infiltrating T cells that coexpress PD-1 and TIM-3 exhibit the most severe exhausted phenotype (5). Tumor-infiltrating dendritic cells (DCs) also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells (6). Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer (7). In addition, blockade of TIM-3 in mouse models of autoimmunity enhanced the severity of disease (1). Finally, binding of Galectin-9 to TIM-3 expressed by Th1 cells induces T cell death (8).

$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 TIM-3 (D5D5R™) XP® Rabbit mAb #45208.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation (1-3 ). TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer (4,5), and tumor-infiltrating T cells that coexpress PD-1 and TIM-3 exhibit the most severe exhausted phenotype (5). Tumor-infiltrating dendritic cells (DCs) also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells (6). Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer (7). In addition, blockade of TIM-3 in mouse models of autoimmunity enhanced the severity of disease (1). Finally, binding of Galectin-9 to TIM-3 expressed by Th1 cells induces T cell death (8).

$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 TIM-3 (D5D5R™) XP® Rabbit mAb #45208.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation (1-3 ). TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer (4,5), and tumor-infiltrating T cells that coexpress PD-1 and TIM-3 exhibit the most severe exhausted phenotype (5). Tumor-infiltrating dendritic cells (DCs) also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells (6). Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer (7). In addition, blockade of TIM-3 in mouse models of autoimmunity enhanced the severity of disease (1). Finally, binding of Galectin-9 to TIM-3 expressed by Th1 cells induces T cell death (8).

$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 TIM-3 (D5D5R™) XP® Rabbit mAb #45208.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation (1-3 ). TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer (4,5), and tumor-infiltrating T cells that coexpress PD-1 and TIM-3 exhibit the most severe exhausted phenotype (5). Tumor-infiltrating dendritic cells (DCs) also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells (6). Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer (7). In addition, blockade of TIM-3 in mouse models of autoimmunity enhanced the severity of disease (1). Finally, binding of Galectin-9 to TIM-3 expressed by Th1 cells induces T cell death (8).

$145
20 µl
$426
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation (1-3 ). TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer (4,5), and tumor-infiltrating T cells that coexpress PD-1 and TIM-3 exhibit the most severe exhausted phenotype (5). Tumor-infiltrating dendritic cells (DCs) also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells (6). Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer (7). In addition, blockade of TIM-3 in mouse models of autoimmunity enhanced the severity of disease (1). Finally, binding of Galectin-9 to TIM-3 expressed by Th1 cells induces T cell death (8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-4 is expressed by dendritic cells and macrophages (1). Like TIM-1, TIM-4 is a receptor for phosphatidylserine (2). Interaction of TIM-4 with phosphatidylserine exposed by cells undergoing apoptosis leads to uptake of apoptotic cells (2,3). In this way, TIM-4 regulates adaptive immunity by removing apoptotic antigen-specific T cells following clearance of infection. Peritoneal macrophages from mice deficient in TIM-4 fail to effectively clear apoptotic cells leading to hyperactive T and B cells and autoimmunity (4). In addition, TIM-4 expressed by tumor-associated macrophages and dendritic cells leads to autophagy-mediated degradation of dying tumor cells, resulting in reduced antigen presentation and T cell responses (5). TIM-4 was also identified as a ligand for TIM-1, and interaction between these proteins regulates T cell proliferation (1). Finally, TIM-4 is expressed by a subset of proinflammatory B cells that produce IFN-γ and promote Th1 cell differentiation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: TIMPs are members of the family of tissue inhibitor of matrix metalloproteinases (MMPs) that includes TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding to their catalytic zinc cofactor and resultant inhibition of proteinase function (1,2). In addition to MMP inhibition, TIMPs have also been shown to interact with various membrane receptors on the cell surface. Some of these interactions include: TIMP1 with CD63, TIMP2 with α3β1 integrin, and TIMP3 with VEGFR2, all of which result in distinct cellular effects (3). TIMPs are involved in a wide variety of biological functions, such as tumor angiogenesis and progression (4,5), wound healing, and vascular remodeling (6,7). Mutations in TIMP3 are associated with Sorsby's fundus dystrophy (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: TIMPs are members of the family of tissue inhibitor of matrix metalloproteinases (MMPs) that includes TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding to their catalytic zinc cofactor and resultant inhibition of proteinase function (1,2). In addition to MMP inhibition, TIMPs have also been shown to interact with various membrane receptors on the cell surface. Some of these interactions include: TIMP1 with CD63, TIMP2 with α3β1 integrin, and TIMP3 with VEGFR2, all of which result in distinct cellular effects (3). TIMPs are involved in a wide variety of biological functions, such as tumor angiogenesis and progression (4,5), wound healing, and vascular remodeling (6,7). Mutations in TIMP3 are associated with Sorsby's fundus dystrophy (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: TIMPs are members of the family of tissue inhibitor of matrix metalloproteinases (MMPs) that includes TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding to their catalytic zinc cofactor and resultant inhibition of proteinase function (1,2). In addition to MMP inhibition, TIMPs have also been shown to interact with various membrane receptors on the cell surface. Some of these interactions include: TIMP1 with CD63, TIMP2 with α3β1 integrin, and TIMP3 with VEGFR2, all of which result in distinct cellular effects (3). TIMPs are involved in a wide variety of biological functions, such as tumor angiogenesis and progression (4,5), wound healing, and vascular remodeling (6,7). Mutations in TIMP3 are associated with Sorsby's fundus dystrophy (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Vacuole membrane protein 1 (VMP1, TMEM49) is a transmembrane protein localized to intracellular vacuoles that was originally described as a protein promoting vacuole formation in acinar cells associated with acute pancreatitis (1). Over-expression of VMP1 promotes vacuole formation and subsequent cell death (1). Additional research studies demonstrated that VMP1 expression might be induced by starvation or the mTOR inhibitor rapamycin, which triggers autophagy (2). VMP1 is targeted along with LC3 to autophagosome membranes (2). Knockdown of VMP1 can inhibit autophagosome formation (2). VMP1 interacts with beclin-1, a key autophagy protein that activates the class III PI3 kinase Vps34 (3). VMP1 functions in the degradation and clearance of zymogen-containing vacuoles during experimentally induced pancreatitis (4). During vacuole degradation and clearance, VMP1 interacts with the ubiquitin protease USP9X, suggesting a possible functional link between the molecular machinery of autophagy and the ubiquitin pathway. Orthologs of VMP1 from C. elegans (known as EPG-3), Drosophila (known as TANGO-5), and Dictyostelium, have been shown to play a role in membrane trafficking, organelle organization, and autophagy (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Vacuole membrane protein 1 (VMP1, TMEM49) is a transmembrane protein localized to intracellular vacuoles that was originally described as a protein promoting vacuole formation in acinar cells associated with acute pancreatitis (1). Over-expression of VMP1 promotes vacuole formation and subsequent cell death (1). Additional research studies demonstrated that VMP1 expression might be induced by starvation or the mTOR inhibitor rapamycin, which triggers autophagy (2). VMP1 is targeted along with LC3 to autophagosome membranes (2). Knockdown of VMP1 can inhibit autophagosome formation (2). VMP1 interacts with beclin-1, a key autophagy protein that activates the class III PI3 kinase Vps34 (3). VMP1 functions in the degradation and clearance of zymogen-containing vacuoles during experimentally induced pancreatitis (4). During vacuole degradation and clearance, VMP1 interacts with the ubiquitin protease USP9X, suggesting a possible functional link between the molecular machinery of autophagy and the ubiquitin pathway. Orthologs of VMP1 from C. elegans (known as EPG-3), Drosophila (known as TANGO-5), and Dictyostelium, have been shown to play a role in membrane trafficking, organelle organization, and autophagy (5-7).

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

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

Background: Tropomodulin-1 (TMOD1) belongs to a conserved family of cytoskeletal proteins (TMOD1-4) that play an important role in modulating actin cytoskeleton dynamics. TMOD proteins function as actin capping proteins, which stabilize actin filaments by inhibiting both elongation and depolymerization (1). While many proteins have been identified that cap the rapidly growing barbed end of actin filaments, TMODs are the only proteins thus far identified that cap the slowly growing pointed end (2). A research study in triple-negative breast cancer cells identified TMOD1 as a target of NF-κB signaling, and showed that increased TMOD1 expression was associated with enhanced tumor growth in a mouse xenograft model (3). Molecular expression of TMOD1 was also identified as part of a unique gene expression signature that could discriminate ALK-negative anaplastic large-cell lymphoma from other malignancy subtypes (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNF-α is an important cytokine produced by numerous cell types including neutrophils, activated lymphoctyes, macrophages and NK cells. It plays a critical role in inflammatory responses and in apoptosis (1). TNF-α exists as a membrane-anchored and soluble form, both of which show biological activity. Response to TNF-α is mediated through two receptors, TNF-R1, which is widely expressed, and TNF-R2, which is expressed mainly in immune and endothelial cells (2). Antagonists to TNF-α have been validated as therapeutic targets for rheumatoid arthritis and other immune disorders (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: TNF-α is an important cytokine produced by numerous cell types including neutrophils, activated lymphoctyes, macrophages and NK cells. It plays a critical role in inflammatory responses and in apoptosis (1). TNF-α exists as a membrane-anchored and soluble form, both of which show biological activity. Response to TNF-α is mediated through two receptors, TNF-R1, which is widely expressed, and TNF-R2, which is expressed mainly in immune and endothelial cells (2). Antagonists to TNF-α have been validated as therapeutic targets for rheumatoid arthritis and other immune disorders (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk1/2, p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk1/2, p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk1/2, p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).

$305
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 TNFRSF17/BCMA (E6D7B) Rabbit mAb #88183.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: B cell maturation antigen (BCMA/TNFRSF17/CD269) is a transmembrane glycoprotein and member of the TNFR superfamily (1). BCMA expression is largely restricted to the B-cell lineage. Pro-survival signaling through this receptor plays a pivotal role in humoral immunity by regulating B-cell maturation and plasma cell differentiation upon binding its ligands, BAFF and APRIL (2-6). BCMA is expressed in a number B-cell malignancies and has garnered much attention as a novel therapeutic target for the treatment of multiple myeloma due to its selective and elevated expression on the cell surface of malignant plasma cells (7-10).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) 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 TNFRSF17/BCMA (E6D7B) Rabbit mAb #88183.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: B cell maturation antigen (BCMA/TNFRSF17/CD269) is a transmembrane glycoprotein and member of the TNFR superfamily (1). BCMA expression is largely restricted to the B-cell lineage. Pro-survival signaling through this receptor plays a pivotal role in humoral immunity by regulating B-cell maturation and plasma cell differentiation upon binding its ligands, BAFF and APRIL (2-6). BCMA is expressed in a number B-cell malignancies and has garnered much attention as a novel therapeutic target for the treatment of multiple myeloma due to its selective and elevated expression on the cell surface of malignant plasma cells (7-10).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B cell maturation antigen (BCMA/TNFRSF17/CD269) is a transmembrane glycoprotein and member of the TNFR superfamily (1). BCMA expression is largely restricted to the B-cell lineage. Pro-survival signaling through this receptor plays a pivotal role in humoral immunity by regulating B-cell maturation and plasma cell differentiation upon binding its ligands, BAFF and APRIL (2-6). BCMA is expressed in a number B-cell malignancies and has garnered much attention as a novel therapeutic target for the treatment of multiple myeloma due to its selective and elevated expression on the cell surface of malignant plasma cells (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNFRSF8/CD30 is a type-I transmembrane glycoprotein that is a member of the TNFR superfamily. CD30 is synthesized as a precursor protein that undergoes extensive posttranslational modification before becoming embedded in the plasma membrane as a 120-kDa transmembrane protein (1,2). The expression of CD30 is upregulated in activated T-cells and may trigger costimulatory signaling pathways upon its engagement (3,4). While its expression is normally restricted to subsets of activated T-cells and B-cells, CD30 expression is robustly upregulated in hematologic malignancies, such as Hodgkin’s lymphoma (HL), anaplastic large cell lymphoma (ALCL), and adult T-cell leukemia, thus making it an attractive target for therapeutic intervention (5,6). Research studies have suggested that in certain disease contexts, CD30 recruits TRAF2 and TRAF5 adaptor proteins to drive NF-kappa B activation, aberrant cell growth, and cytokine production (7-9). CD30 signaling is also regulated by TACE-dependent proteolytic cleavage of its ectodomain, which results in reduced CD30L-dependent activation of CD30+ cells (10, 11).

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

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

Background: TNFRSF8/CD30 is a type-I transmembrane glycoprotein that is a member of the TNFR superfamily. CD30 is synthesized as a precursor protein that undergoes extensive posttranslational modification before becoming embedded in the plasma membrane as a 120-kDa transmembrane protein (1,2). The expression of CD30 is upregulated in activated T-cells and may trigger costimulatory signaling pathways upon its engagement (3,4). While its expression is normally restricted to subsets of activated T-cells and B-cells, CD30 expression is robustly upregulated in hematologic malignancies, such as Hodgkin’s lymphoma (HL), anaplastic large cell lymphoma (ALCL), and adult T-cell leukemia, thus making it an attractive target for therapeutic intervention (5,6). Research studies have suggested that in certain disease contexts, CD30 recruits TRAF2 and TRAF5 adaptor proteins to drive NF-kappa B activation, aberrant cell growth, and cytokine production (7-9). CD30 signaling is also regulated by TACE-dependent proteolytic cleavage of its ectodomain, which results in reduced CD30L-dependent activation of CD30+ cells (10, 11).