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Product listing: EPAC2 (5B1) Mouse mAb, UniProt ID Q9EQZ6 #4156 to Keratin 17/19 (D4G2) XP® Rabbit mAb, UniProt ID P08727 #12434

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$305
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 EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
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 EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Epithelial Protein Lost in Neoplasm (EPLIN) is an actin-binding protein that regulates actin filament dynamics and cross-linking (1). Alpha and beta isoforms are generated from alternate promoters, with the EPLIN-β isoform representing the full-length protein and the EPLIN-α isoform lacking the amino-terminal 160 amino acids (2). Increased expression of EPLIN protein results in more abundant and larger actin stress fibers due to stabilizing of cross-links and inhibition of actin depolymerization. EPLIN protein inhibits Rac1-promoted membrane ruffling and Arp2/3-associated actin filament branching (1).Research studies demonstrate reduced EPLIN-α expression in tumor tissues, and correlate this reduction with increased invasiveness and poor clinical outcomes (3). The EPLIN protein is an important negative regulator of the epithelial-mesenchymal transition (EMT)(4). While EMT is a critical process during normal embryonic development, dysregulation in transformed cells is a key step in the transition to metastasis (5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin)

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Fer is a nonreceptor protein-tyrosine kinase of the Fes/Fps family. Like many other cytoplasmic tyrosine kinases, Fer contains a long amino-terminal domain, a central SH2 domain, and a carboxy-terminal kinase domain. Its amino-terminal domain is responsible for protein oligomerization as well as interaction with cytoskeletal proteins. Fer is ubiquitously expressed in a wide variety of cell and tissue types, and is localized to both cytoplasm and nucleus (1). Tyrosine kinase activity of Fer can be stimulated by growth factors and cytokines (2,3). After activation, Fer can further activate various downstream signaling components including Stat3 (3). Fer plays an important role in regulation of cell movement, oncogenesis and inflammation (4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fibrillarin is a 2'-O-methyltransferase located in fibrillar regions and Cajal bodies of the nucleolus, where RNA transcription and pre-RNA processing take place (1,2). Fibrillarin associates with several other structural proteins as well as box C/D snoRNA to form a complex that functions in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. This complex catalyzes site-specific 2'-O-ribose methylation of targeted nucleotides within the rRNA sequence (3,4). The sequence, structure, and function of fibrillarin are highly conserved and fibrillarin gene expression is essential for early embryonic development (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

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

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

Background: Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology domain (PHB) (1). Flotillin members are ubiquitously expressed and located in noncaveolar microdomains (lipid rafts) on the plasma membrane where they support signal transduction and regulate lipid raft motility and localization (2-5). Two flotillin members have been described, flotillin-1 and flotillin-2. In addition to its colocalization with lipid rafts on the plasma membrane, flotillin-1 also has been found in compartments of the endocytic and autophagosomal pathways, such as recycling/late endosomes, the Golgi complex, and the nucleus (6,7). Flotillin-2 is mainly localized to the plasma membrane and is prevalent in cell-cell contact sites. However, overexpressed flotillin-2 has also been found in the late endosome (4,8,9). Both flotillin-1 and flotillin-2 are commonly used as lipid raft-associated markers.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology domain (PHB) (1). Flotillin members are ubiquitously expressed and located in noncaveolar microdomains (lipid rafts) on the plasma membrane where they support signal transduction and regulate lipid raft motility and localization (2-5). Two flotillin members have been described, flotillin-1 and flotillin-2. In addition to its colocalization with lipid rafts on the plasma membrane, flotillin-1 also has been found in compartments of the endocytic and autophagosomal pathways, such as recycling/late endosomes, the Golgi complex, and the nucleus (6,7). Flotillin-2 is mainly localized to the plasma membrane and is prevalent in cell-cell contact sites. However, overexpressed flotillin-2 has also been found in the late endosome (4,8,9). Both flotillin-1 and flotillin-2 are commonly used as lipid raft-associated markers.

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

Application Methods: Western Blotting

Background: Rho family small GTPases regulate processes such as cell migration, adhesion, proliferation, and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of GDP for GTP. GEF-H1 is a Rho GEF that localizes to microtubules and regulates Rho activity in response to microtubule destabilization (1). Loss of interaction between GEF-H1 and microtubules leads to activation of Rho (2). Phosphorylation of GEF-H1 at Ser886 (Ser885 in mouse), a site located in the 14-3-3 binding motif, has been implicated in recruitment of 14-3-3 and GEF-H1 to microtubules (3), and in the regulation of RhoA activity in response to mitotic kinases during cytokinesis (4).GEF-H1 has also been shown to localize to tight junctions and modulate polarized cell permeability (5,6). GEF-H1 is inactivated by binding to cingulin at epithelial tight junctions, inactivating RhoA and leading to G1/S arrest (6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Gelsolin (actin-depolymerizing factor, ADF, AGEL, Brevin) is an 83 kDa protein that shares structural and functional homology to villin and adseverin/scinderin (1,2). Gelsolin plays an important role in actin filament assembly by capping and severing actin proteins in a Ca2+-dependent manner (3,4). Gelsolin is important for cellular events (e.g., membrane ruffling, chemotaxis, ciliogenesis) that require cytoskeletal remodeling (3). Accordingly, cells from gelsolin knockout mice exhibit motility defects, including a failure to ruffle in response to growth factor stimulation (5,6). In humans, defects in gelsolin have been linked to amyloidosis type 5 (AMYL5), a hereditary disease characterized by cranial neuropathy, which appears to result from gelsolin amyloid deposition (7).

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

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

Background: The Golgi apparatus functions in the modification, organization, and transport of proteins and membranes targeted to other parts of the cell, such as the plasma membrane, lysosomes, and endosomes. This regulated transport is important for appropriate protein localization, secretion, and signal transduction. Members of the Golgin family of proteins, including GM130, Giantin, p115, and GRASP65, are defined by their presence in the Golgi matrix and by their long coiled coil domains. Golgin function, which is regulated in part by small GTPases of the Rab and Arl families, includes establishing and maintaining Golgi structure and transport (reviewed in 1). The Golgi cisternae are stacked and linked laterally to form a ribbon. GRASP65 and GM130 are required for membrane fusion events that mediate ribbon formation during Golgi assembly. These lateral fusion events allow for uniform distribution of Golgi enzymes (2). GM130 and Giantin interact with the transport factor p115 to facilitate endoplasmic reticulum (ER)-Golgi transport (3). GM130 is also involved in the transport of the Ether-a-go-go-Related (hERG) potassium ion channel. Inappropriate hERG localization may be an underlying cause in Long QT syndrome, a hereditary and potentially fatal cardiac arrhythmia (4). Further, GM130 was implicated in signal transduction regulating invasion, migration, and cell polarization via its interaction with and activation of serine/threonine kinases YSK1 and Mst4 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Golgi-associated protein golgin A1 (GOLGA1, golgin-97) was first isolated as a Golgi complex autoantigen associated with the autoimmune disorder Sjogren's syndrome (1). The golgin-97 protein contains a carboxy-terminal GRIP domain and is a commonly used trans-Golgi network (TGN) marker. All four known mammalian GRIP domain-containing proteins (golgin-97, golgin-245, GCC88 and GCC185) are found in the TGN, share extensive alpha-helical structure, and form homodimers (2). While all four golgin proteins localize to the TGN, they exhibit different membrane-binding abilities and are found in distinct TGN regions (3). Golgin-97 and golgin-245 are targeted to the trans-Golgi network through an interaction between their GRIP domains and the Arl1 protein switch II region (4). Overexpression studies and siRNA assays with GRIP domain-containing proteins suggest that these proteins help to maintain trans-Golgi network integrity and function by controlling localization of TGN resident proteins (5). By using a Shiga toxin B fragment (STxB)-based in vitro transport assay and an E-cadherin transport model system, golgin-97 and its effector Arl1-GTP were shown to play a role in trans-Golgi endosomal trafficking (6,7). Research studies also suggest that golgin-97 may play a role in poxvirus morphogenesis and maturation (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Golgi-associated protein golgin A1 (GOLGA1, golgin-97) was first isolated as a Golgi complex autoantigen associated with the autoimmune disorder Sjogren's syndrome (1). The golgin-97 protein contains a carboxy-terminal GRIP domain and is a commonly used trans-Golgi network (TGN) marker. All four known mammalian GRIP domain-containing proteins (golgin-97, golgin-245, GCC88 and GCC185) are found in the TGN, share extensive alpha-helical structure, and form homodimers (2). While all four golgin proteins localize to the TGN, they exhibit different membrane-binding abilities and are found in distinct TGN regions (3). Golgin-97 and golgin-245 are targeted to the trans-Golgi network through an interaction between their GRIP domains and the Arl1 protein switch II region (4). Overexpression studies and siRNA assays with GRIP domain-containing proteins suggest that these proteins help to maintain trans-Golgi network integrity and function by controlling localization of TGN resident proteins (5). By using a Shiga toxin B fragment (STxB)-based in vitro transport assay and an E-cadherin transport model system, golgin-97 and its effector Arl1-GTP were shown to play a role in trans-Golgi endosomal trafficking (6,7). Research studies also suggest that golgin-97 may play a role in poxvirus morphogenesis and maturation (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Human enhancer of filamentation protein 1 (HEF1), also known as neural precursor cell expressed developmentally down-regulated protein 9 (NEDD9), is part of the Cas family of proteins, which include HEF1/NEDD9, p130Cas and Efs (1). HEF1 is a predominantly cytoplasmic protein, localizing to focal adhesions during interphase, and centrosomes and other parts of the mitotic apparatus during G2/M phase of the cell cycle (2). HEF1 is a docking protein that plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion, motility, growth and apoptosis (1). Phosphorylation of HEF1 is induced by a number of factors, including FAK, TGF-β, PDGFR, Abl, and BCR-ABL, which leads to coordinate binding of multiple downstream effector proteins via 15 known SH2 domain-binding sites (1). HEF1 is a key regulator of cancer metastasis. It is required for the invasive activity of glioblastomas (3), is linked to the promotion of metastasis in melanoma (4), and is found to be up-regulated in lung cancer metastasis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

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

Application Methods: Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlaping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).Several αV subfamily members, including αVβ3, αVβ5, αVβ1, are highly expressed in active endothelial cells and cancer cells (3-6) where they play a critical role in angiogenesis and tumor metastasis (7-9). Therefore, interest has focused on αV integrin as a key therapeutic target in the treatment of cancer (10-12).

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

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

Background: IQGAPs are scaffolding proteins involved in mediating cytoskeletal function. They contain multiple protein interaction domains and bind to a growing number of molecules including actin, myosin light chain, calmodulin, E-cadherin, and β-catenin (reviewed in 1). Through their GAP-related domains, they bind the small GTPases Rac1 and cdc42. IQGAPs lack GAP activity, however, and regulate small GTPases by stabilizing their GTP-bound (active) forms (2,3). Research studies have shown that the function and distribution of the IQGAP proteins widely vary. IQGAP1 is ubiquitously expressed and has been found to interact with APC (4) and the CLIP170 complex (5) in response to small GTPases, promoting cell polarization and migration. Additional research studies have suggested that IQGAP1 could play a part in the invasiveness of some cancers (6-8). IQGAP2, which is about 60% identical to IQGAP1, is expressed primarily in liver (3), but lower levels have been detected in the prostate, kidney, thyroid, stomach, and testis (9,10). Research studies have shown that IQGAP2 displays tumor suppressor properties (11). Less is known about the function of IQGAP3, but this protein is present in the lung, brain, small intestine, and testis (9) and is only expressed in proliferating cells (12), suggesting a role in cell growth and division.

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

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

Background: IQGAPs are scaffolding proteins involved in mediating cytoskeletal function. They contain multiple protein interaction domains and bind to a growing number of molecules including actin, myosin light chain, calmodulin, E-cadherin, and β-catenin (reviewed in 1). Through their GAP-related domains, they bind the small GTPases Rac1 and cdc42. IQGAPs lack GAP activity, however, and regulate small GTPases by stabilizing their GTP-bound (active) forms (2,3). Research studies have shown that the function and distribution of the IQGAP proteins widely vary. IQGAP1 is ubiquitously expressed and has been found to interact with APC (4) and the CLIP170 complex (5) in response to small GTPases, promoting cell polarization and migration. Additional research studies have suggested that IQGAP1 could play a part in the invasiveness of some cancers (6-8). IQGAP2, which is about 60% identical to IQGAP1, is expressed primarily in liver (3), but lower levels have been detected in the prostate, kidney, thyroid, stomach, and testis (9,10). Research studies have shown that IQGAP2 displays tumor suppressor properties (11). Less is known about the function of IQGAP3, but this protein is present in the lung, brain, small intestine, and testis (9) and is only expressed in proliferating cells (12), suggesting a role in cell growth and division.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: IQGAPs are scaffolding proteins involved in mediating cytoskeletal function. They contain multiple protein interaction domains and bind to a growing number of molecules including actin, myosin light chain, calmodulin, E-cadherin, and β-catenin (reviewed in 1). Through their GAP-related domains, they bind the small GTPases Rac1 and cdc42. IQGAPs lack GAP activity, however, and regulate small GTPases by stabilizing their GTP-bound (active) forms (2,3). Research studies have shown that the function and distribution of the IQGAP proteins widely vary. IQGAP1 is ubiquitously expressed and has been found to interact with APC (4) and the CLIP170 complex (5) in response to small GTPases, promoting cell polarization and migration. Additional research studies have suggested that IQGAP1 could play a part in the invasiveness of some cancers (6-8). IQGAP2, which is about 60% identical to IQGAP1, is expressed primarily in liver (3), but lower levels have been detected in the prostate, kidney, thyroid, stomach, and testis (9,10). Research studies have shown that IQGAP2 displays tumor suppressor properties (11). Less is known about the function of IQGAP3, but this protein is present in the lung, brain, small intestine, and testis (9) and is only expressed in proliferating cells (12), suggesting a role in cell growth and division.

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

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

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

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

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

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).