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ELISA Kit Calcium Ion Homeostasis

Also showing ELISA Kit ELISA Calcium Ion Homeostasis

$489
96 assays
1 Kit
The PathScan® Total Caveolin-1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Caveolin-1 protein. A Caveolin-1 Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Caveolin-1 protein is captured by the coated antibody. Following extensive washing, Caveolin-1 Mouse Detection mAb is added to detect the captured Caveolin-1 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 absorbance for the developed color is proportional to the quantity of total Caveolin-1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Background: The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

$489
96 assays
1 Kit
The PathScan® Total α-Synuclein Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels ofα-Synuclein protein. An α-Synuclein rabbit mAb has been coated onto the microwells. After incubation with cell lysates, the α-Synuclein protein is captured by the coated antibody. Following extensive washing, α-Synuclein mouse detection mAb is added to detect captured α-Synuclein protein. Anti-mouse, 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 α-Synuclein protein. Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Mouse, Rat

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$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® 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
PathScan® Phospho-c-Abl (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated Bcr-Abl and c-Abl proteins. A c-Abl rabbit antibody has been coated on the microwells. After incubation with cell lysates, Bcr-Abl and c-Abl protein (phospho and nonphospho) are captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse detection antibody is added to detect captured tyrosine-phosphorylated Bcr-Abl and c-Abl 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 tyrosine-phosphorylated Bcr-Abl and c-Abl protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The c-Abl proto-oncogene encodes a nonreceptor protein tyrosine kinase that is ubiquitously expressed and highly conserved in metazoan evolution. c-Abl protein is distributed in both the nucleus and the cytoplasm of cells. It is implicated in regulating cell proliferation, differentiation, apoptosis, cell adhesion, and stress responses (1-3). c-Abl kinase activity is increased in vivo by diverse physiological stimuli including integrin activation; PDGF stimulation; and binding to c-Jun, Nck, and RFX1 (2,4). The in vivo mechanism for regulation of c-Abl kinase activity is not completely understood. Tyr245 is located in the linker region between the SH2 and catalytic domains. This positioning is conserved among Abl family members. Phosphorylation at Tyr245 is involved in the activation of c-Abl kinase (5). In addition, phosphorylation at Tyr412, which is located in the kinase activation loop of c-Abl, is required for kinase activity (6).

$489
96 assays
1 Kit
PathScan® Phospho-c-Abl (Tyr412) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated Bcr-Abl and c-Abl proteins. A c-Abl Mouse mAb has been coated on the microwells. After incubation with cell lysates, Bcr-Abl and c-Abl protein (phospho and nonphospho) are captured by the coated antibody. Following extensive washing, a Phospho-c-Abl (Tyr412) Rabbit Detection Antibody is added to detect phospho-Bcr-Abl and phospho-c-Abl 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 the developed color is proportional to the quantity of Bcr-Abl or c-Abl protein phosphorylated at Tyr412.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The c-Abl proto-oncogene encodes a nonreceptor protein tyrosine kinase that is ubiquitously expressed and highly conserved in metazoan evolution. c-Abl protein is distributed in both the nucleus and the cytoplasm of cells. It is implicated in regulating cell proliferation, differentiation, apoptosis, cell adhesion, and stress responses (1-3). c-Abl kinase activity is increased in vivo by diverse physiological stimuli including integrin activation; PDGF stimulation; and binding to c-Jun, Nck, and RFX1 (2,4). The in vivo mechanism for regulation of c-Abl kinase activity is not completely understood. Tyr245 is located in the linker region between the SH2 and catalytic domains. This positioning is conserved among Abl family members. Phosphorylation at Tyr245 is involved in the activation of c-Abl kinase (5). In addition, phosphorylation at Tyr412, which is located in the kinase activation loop of c-Abl, is required for kinase activity (6).

$489
96 assays
1 Kit
The PathScan® Phospho-PDGF Receptor α/β (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of PDGF receptor α/β when tyrosine phosphorylated. A PDGF Receptor α/β Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, PDGF Receptor α/β (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Biotinylated Phospho-Tyrosine Mouse Detection Antibody is added to detect tyrosine phosphorylation of the captured PDGF receptor α/β protein. HRP-linked Strepavidin 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 PDGF receptor α/β phosphorylated on tyrosine.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

$489
96 assays
1 Kit
The PathScan® Phospho-Lck (Tyr505) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Lck (Tyr505). A phospho-Lck rabbit antibody has been coated onto the microwells. After incubation with cell lysates, phospho-Lck (Tyr505) is captured by the coated antibody. Following extensive washing, a Lck mouse detection mAb is added to detect the captured phospho-Lck (Tyr505). 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-Lck (Tyr505).
REACTIVITY
Human

Background: Lck belongs to the Src-like non-receptor tyrosine kinase family with the typical Src family kinase structure: a unique amino terminal domain (Src homology 4 domain, SH4) followed by an SH3 domain, an SH2 domain, a kinase domain (SH1), and a carboxy-terminal negative regulatory domain (1). Lck activity is controlled by the interactions of SH2 and SH3 domains as well as tyrosine phosphorylation status of the activation loop (2,3). Lck is recruited to the T cell receptor (TCR) complex upon stimulation and activates downstream tyrosine kinases to initiate T cell signaling (4). Lck is also found to be involved in the regulation of mitochondrial apoptosis pathways and may be responsible for some anticancer drug induced apoptosis (5,6).

$489
96 assays
1 Kit
CST's PathScan® Total Bad Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Bad protein. A Bad Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Bad protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Bad Mouse mAb is added to detect the captured Bad 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 absorbance for this developed color is proportional to the quantity of total Bad protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

$489
96 assays
1 Kit
CST's PathScan® Phospho-Bad (Ser112) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Bad (Ser112) protein. A Bad rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Bad protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a phospho-Bad (Ser112) mouse mAb is added to detect the captured phospho-Bad 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 absorbance for this developed color is proportional to the quantity of phospho-Bad (Ser112) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

$499
96 assays
1 Kit
The FastScan™ Phospho-Bad (Ser112) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Bad when phosphorylated at Ser112. 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-Bad (Ser112) 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-Bad (Ser112). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

$499
96 assays
1 Kit
The FastScan™ Phospho-Bad (Ser136) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Bad when phosphorylated at Ser136. 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-Bad (Ser136) 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-Bad (Ser136). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).