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ELISA Kit Cell-Cell Adhesion

$489
96 assays
1 Kit
CST's PathScan® Total Beta-Catenin Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Beta-catenin protein. A Beta-Catenin Ab has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-Beta-catenin proteins are captured by the coated antibody. Following extensive washing, Beta-Catenin rabbit mAb is added to detect both the captured phospho- and nonphospho-Beta-catenin protein. Anti-Rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total Beta-catenin protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$489
96 assays
1 Kit
PathScan® Total Tyro3 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Tyro3 protein. A Tyro3 Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Tyro3 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Tyro3 Mouse Detection mAb is added to detect the captured Tyro3 proteins. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total tyro3 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Tyro3 is a receptor tyrosine kinase belonging to the TAM subfamily (Tyro3, Axl and Mer). All three members have similar domain structure composed of an extracellular region with 2 Ig-like domains, followed by 2 FNII-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase domain (1). The natural ligand for Tyro3, as well as Axl and Mer, is Gas6 (growth arrest-specific gene 6) (1,2). Expression pattern and target knockout data indicate an important role of Tyro3 in apoptotic cell phagocytosis of dendritic cells and macrophages (3), NK cell differentiation (4), reproductive neuron survival and migration (5), osteoclast stimulation (6,7), as well as cortical and hippocampal neuron function (8). Both MAPK and PI3K pathways have been suggested as downstream targets of Tyro3 activation (7,8). Tyro3 has also been shown to be correlated to melanoma tumorigenesis, likely through its reglulatory role in the expression of oncogenic microphthalmia-associated transcription factor (MITF) (9).

$489
96 assays
1 Kit
PathScan® Phospho-Tyro3 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated Mer protein. A Tyro3 Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Tyro3 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Phospho-Tyrosine Mouse Detection mAb is added to detect the captured phospho-Tyro3 proteins. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of Tyro3 protein phosphorylated on tyrosine residues.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Tyro3 is a receptor tyrosine kinase belonging to the TAM subfamily (Tyro3, Axl and Mer). All three members have similar domain structure composed of an extracellular region with 2 Ig-like domains, followed by 2 FNII-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase domain (1). The natural ligand for Tyro3, as well as Axl and Mer, is Gas6 (growth arrest-specific gene 6) (1,2). Expression pattern and target knockout data indicate an important role of Tyro3 in apoptotic cell phagocytosis of dendritic cells and macrophages (3), NK cell differentiation (4), reproductive neuron survival and migration (5), osteoclast stimulation (6,7), as well as cortical and hippocampal neuron function (8). Both MAPK and PI3K pathways have been suggested as downstream targets of Tyro3 activation (7,8). Tyro3 has also been shown to be correlated to melanoma tumorigenesis, likely through its reglulatory role in the expression of oncogenic microphthalmia-associated transcription factor (MITF) (9).

$499
96 assays
1 Kit
The FastScan™ Phospho-Zap-70 (Tyr319) ELISA Kit (Human Preferred) is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Zap-70 (Tyr319). To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with phospho-Zap-70 (Tyr319) in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of phospho-Zap-70 (Tyr319). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$489
96 assays
1 Kit
The PathScan® Total Sox2 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Sox2. A Sox2 Mouse Antibody has been coated onto the microwells. After incubation with cell lysates, Sox2 protein is captured by the coated antibody. Following extensive washing, a Sox2 Rabbit Detection Antibody is added to detect the captured Sox2 protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of Sox2.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Embryonic stem cells (ESC) derived from the inner cell mass of the blastocyst are unique in their pluripotent capacity and potential for self-renewal (1). Research studies demonstrate that a set of transcription factors that includes Oct-4, Sox2, and Nanog forms a transcriptional network that maintains cells in a pluripotent state (2,3). Chromatin immunoprecipitation experiments show that Sox2 and Oct-4 bind to thousands of gene regulatory sites, many of which regulate cell pluripotency and early embryonic development (4,5). siRNA knockdown of either Sox2 or Oct-4 results in loss of pluripotency (6). Induced overexpression of Oct-4 and Sox2, along with additional transcription factors Klf4 and c-Myc, can reprogram both mouse and human somatic cells to a pluripotent state (7,8). Additional evidence demonstrates that Sox2 is also present in adult multipotent progenitors that give rise to some adult epithelial tissues, including several glands, the glandular stomach, testes, and cervix. Sox2 is thought to regulate target gene expression important for survival and regeneration of these tissues (9).

$489
96 assays
1 Kit
The PathScan® Total CD31 (PECAM-1) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of CD31 (PECAM-1) protein. A CD31 (PECAM-1) mouse mAb has been coated onto the microwells. After incubation with cell lysates, the CD31 (PECAM-1) proteins are captured by the coated antibody. Following extensive washing, a CD31 (PECAM-1) biotinylated detection mAb is added to detect captured CD31 (PECAM-1) proteins. HRP-linked Streptavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of CD31 (PECAM-1) protein.Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Human

Background: CD31 (Platelet Endothelial Cell Adhesion Molecule-1: PECAM-1), a member of the Ig superfamily of cell adhesion molecules, is expressed by circulating platelets, monocytes, neutrophils, some T cells, and endothelial cells and modulates cell adhesion, endothelial cell migration, and angiogenesis (1). CD31 is phosphorylated on Tyr686 at the cytoplasmic carboxy-terminal tail upon various stimuli (e.g. mechanical or oxidative stress), presumably by Src family members (2). The tyrosine phosphorylation mediates associations with a number of SH2 domain-containing binding partners such as PI3 kinase, SHIP, PLCγ, and SHP-2. Thus, CD31 serves as a scaffold for various signaling molecules (3).

$489
96 assays
1 Kit
CST's PathScan® Phospho-MEK1 (Ser217/221) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-MEK1 (Ser217/221) protein. MEK1 Mouse mAb has been coated onto the microwells. After incubation with cell lysates, total MEK1 protein (phospho- and nonphospho-) is captured by the coated antibody. Following extensive washing, a Phospho-MEK1/2 Antibody is added to detect the captured phospho-MEK1 protein. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-MEK1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$499
96 assays
1 Kit
The FastScan™ Total EGF Receptor ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of EGF Receptor. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with EGF Receptor in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of EGF Receptor. Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$489
96 assays
1 Kit
CST's PathScan® Total MEK1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total MEK1 protein. A MEK1 mouse mAb has been coated onto the microwells. After incubation with cell lysates, total MEK1 protein (phospho- and nonphospho-) is captured by the coated antibody. Following extensive washing, MEK1/2 Antibody is added to detect the captured MEK1 protein. HRP-linked, anti-rabbit antibody #7074 is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total MEK1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$489
96 assays
1 Kit
CST's PathScan® Phospho-PTEN (Ser380) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-PTEN (Ser380) protein. A PTEN Mouse mAb has been coated onto the microwells. After incubation with cell lysates, PTEN protein (phospho and non-phospho) is captured by the coated antibody. Following extensive washing, Phospho-PTEN (Ser380) Antibody is added to detect the captured phospho-PTEN (Ser380) protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for this developed color is proportional to the quantity of phospho-PTEN (Ser380) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$489
96 assays
1 Kit
The PathScan® Phospho-VEGFR-2 (Tyr1175) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-VEGFR-2 (Tyr1175) protein. A VEGFR-2 Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both nonphospho- and phospho-VEGFR-2 proteins are captured by the coated antibody. Following extensive washing, a phospho-VEGFR-2 Rabbit mAb is added to detect the captured phospho-VEGFR-2 protein. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-VEGFR-2 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Vascular endothelial growth factor receptor 2 (VEGFR2, KDR, Flk-1) is a major receptor for VEGF-induced signaling in endothelial cells. Upon ligand binding, VEGFR2 undergoes autophosphorylation and becomes activated (1). Major autophosphorylation sites of VEGFR2 are located in the kinase insert domain (Tyr951/996) and in the tyrosine kinase catalytic domain (Tyr1054/1059) (2). Activation of the receptor leads to rapid recruitment of adaptor proteins, including Shc, GRB2, PI3 kinase, NCK, and the protein tyrosine phosphatases SHP-1 and SHP-2 (3). Phosphorylation at Tyr1212 provides a docking site for GRB2 binding and phospho-Tyr1175 binds the p85 subunit of PI3 kinase and PLCγ, as well as Shb (1,4,5). Signaling from VEGFR2 is necessary for the execution of VEGF-stimulated proliferation, chemotaxis and sprouting, as well as survival of cultured endothelial cells in vitro and angiogenesis in vivo (6-8).

$489
96 assays
1 Kit
The PathScan® Total PTEN Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenously expressed PTEN. A PTEN rabbit antibody has been coated onto the microwells. After incubation with cell lysates, PTEN is captured by the coated antibody. Following extensive washing, a PTEN mouse detection antibody is added to detect the captured PTEN. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate (TMB) is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of PTEN.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$499
96 assays
1 Kit
The FastScan™ Phospho-EGF Receptor (Tyr1068) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of EGF Receptor when phosphorylated at Tyr1068. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with phospho-EGF Receptor (Tyr1068) in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of phospho-EGF Receptor (Tyr1068). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$489
96 assays
1 Kit
CST's PathScan® Total VEGFR-2 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total VEGFR-2 protein. A VEGFR-2 Mouse mAb (7335-1D6*) has been coated onto the microwells. After incubation with cell lysates, Both nonphospho- and phospho-VEGFR-2 proteins are captured by the coated antibody. Following extensive washing, a VEGFR-2 Rabbit mAb (7340-55B11*) is added to detect the captured VEGFR-2 protein. HRP-linked anti-rabbit antibody (#7074*) is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total VEGFR-2 protein.* Antibodies in this kit are custom formulations specific to the kit.
REACTIVITY
Human

Background: Vascular endothelial growth factor receptor 2 (VEGFR2, KDR, Flk-1) is a major receptor for VEGF-induced signaling in endothelial cells. Upon ligand binding, VEGFR2 undergoes autophosphorylation and becomes activated (1). Major autophosphorylation sites of VEGFR2 are located in the kinase insert domain (Tyr951/996) and in the tyrosine kinase catalytic domain (Tyr1054/1059) (2). Activation of the receptor leads to rapid recruitment of adaptor proteins, including Shc, GRB2, PI3 kinase, NCK, and the protein tyrosine phosphatases SHP-1 and SHP-2 (3). Phosphorylation at Tyr1212 provides a docking site for GRB2 binding and phospho-Tyr1175 binds the p85 subunit of PI3 kinase and PLCγ, as well as Shb (1,4,5). Signaling from VEGFR2 is necessary for the execution of VEGF-stimulated proliferation, chemotaxis and sprouting, as well as survival of cultured endothelial cells in vitro and angiogenesis in vivo (6-8).

$489
96 assays
1 Kit
The PathScan® Total MUC1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of MUC1 protein. A MUC1 mouse mAb has been coated onto the microwells. After incubation with cell lysates, the MUC1 proteins are captured by the coated antibody. Following extensive washing, a MUC1 rabbit detection mAb is added to detect captured MUC proteins. Anti-rabbit, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of MUC1 protein.Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Human

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$489
96 assays
1 Kit
The PathScan® Phospho-Src (Tyr416) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Src (Tyr416). A phospho-Src rabbit antibody has been coated onto the microwells. After incubation with cell lysates, phospho-Src (Tyr416) is captured by the coated antibody. Following extensive washing, a Src mouse detection antibody is added to detect the captured phospho-Src (Tyr416). Anti-mouse, HRP-linked antibody is then used to recognize the bound detection antibody. The HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-Src (Tyr416).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Dog, Human

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$499
96 assays
1 Kit
The FastScan™ Total E-Cadherin ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of E-cadherin. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with E-cadherin in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of E-cadherin. Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$489
96 assays
1 Kit
CST's PathScan® Phospho-EGF Receptor (Tyr1068) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-EGF Receptor (Tyr1068) protein with a chemiluminescent readout. Chemiluminescent ELISAs often have a wider dynamic range and higher sensitivity than conventional chromogenic detection. This chemiluminescent ELISA, which is offered in low volume microplates, shows increased signal and sensitivity while using a smaller sample size. An EGF Receptor Mouse mAb has been coated onto the microwells. After incubation with cell lysates, EGF receptor proteins (phospho and nonphospho) are captured by the coated antibody. Following extensive washing, Phospho-EGF Receptor (Tyr1068) Rabbit mAb is added to detect the captured phospho-EGF Receptor protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. Chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of Phospho-EGF Receptor (Tyr1068).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$489
96 assays
1 Kit
CST's PathScan® Total EGF Receptor Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total EGF Receptor protein. An EGF Receptor Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-EGF Receptor proteins are captured by the coated antibody. Following extensive washing, EGF Receptor Rabbit Antibody is added to detect both the captured phospho- and nonphospho-EGF Receptor protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total EGF Receptor protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$489
96 assays
1 Kit
The PathScan® Total DDR1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total DDR1 protein. A DDR1 rabbit antibody has been coated on the microwells. After incubation with cell lysates, DDR1 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a DDR1 mouse mAb is added to detect captured DDR1 protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of total DDR1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The discoidin domain receptors (DDRs) are receptor tyrosine kinases with a discoidin homology repeat in their extracellular domains, activated by binding to extracellular matrix collagens. So far, two mammalian DDRs have been identified: DDR1 and DDR2 (1). They are widely expressed in human tissues and may have roles in smooth muscle cell-mediated collagen remodeling (2). Research studies have implicated aberrant expression and signaling of DDRs in human diseases related to increased matrix degradation and remodeling, such as cardiovascular disease, liver fibrosis, and tumor invasion (1).