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Monoclonal Antibody Detection of Calcium Ion

Also showing Monoclonal Antibody Western Blotting Detection of Calcium Ion

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calmodulin is a ubiquitously expressed small protein mediating many cellular effects such as short-term and long-term memory, nerve growth, inflammation, apoptosis, muscle contraction and intracellular movement (1). Upon binding of four Ca2+ ions, calmodulin undergoes conformational changes, allowing this complex to bind to and activate many enzymes including protein kinases, protein phosphatases, ion channels, Ca2+ pumps, nitric oxide synthase, inositol triphosphate kinase, and cyclic nucleotide phosphodiesterase (2,3). Since calmodulin binds Ca2+ in a cooperative fashion, small changes in cytosolic Ca2+ levels lead to large changes in the level of active calmodulin and its target proteins (4).

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

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

Background: Ca2+ is a key second messenger in many intracellular signaling pathways. Ca2+ signals control many cellular functions ranging from short-term responses such as contraction and secretion to longer-term regulation of cell growth and proliferation (1,2). Stromal interaction molecules (STIMs) function as Ca2+ sensors that detect changes in Ca2+ content in intracellular Ca2+ stores (3). STIM1 is conserved, ubiquitously expressed, and functions as an endoplasmic reticulum (ER) Ca2+ sensor that migrates from the ER Ca2+ store to the plasma membrane where it activates calcium-release-activated calcium (CRAC) channels when the ER Ca2+ store is low (4). STIM1 is a potential tumor suppressor; defects in STIM1 may cause rhabdomyosarcoma and rhabdoid tumors (5). STIM1 can either homodimerize or form heterodimers with STIM2. STIM2 possesses a high sequence identity to STIM1 and can function as an inhibitor of STIM1-mediated plasma membrane store-operated Ca2+ entry (6). However, further investigation is required to elucidate the true physiological function of STIM2.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CaSR, the extracellular Calcium-Sensing Receptor, is a widely expressed G-protein coupled receptor (GPCR) involved in calcium homeostasis. CaSR operates as a sensor in parathyroid and kidney, and alterations in its activity have been shown to cause thyroid disease in humans (1). Activation of the receptor in response to extracellular calcium or other ligands causes activation of phospholipase C (PLC), release of IP3 and release of calcium from intracellular stores (2). Proinflammatory cytokines IL-1β and TNF-α increase CaSR gene expression in human thyroid and kidney cells through activation of the NF-κB pathway, and this pathway may be involved in hypocalcemia often seen in critically ill patients (3). Elevated calcium concentration and CaSR expression have been linked to proliferation and metastasis of skeletal metastatic prostate cancer cell lines (4). In intestinal epithelial cells, CaSR is involved in regulation of cyclic nucleotide metabolism and the fluid secretion that results in life-threatening fluid loss in response to intestinal pathogens (5). The interaction of CaSR with the actin-binding protein filamin may provide scaffolding for the organization of signaling pathways converging on the cytoskeleton, including CaSR-mediated MAPK pathway activation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Synaptotagmin 1 (SYT1) is an integral membrane protein found in synaptic vesicles thought to play a role in vesicle trafficking and exocytosis (1). Individual SYT1 proteins are composed of an amino-terminal transmembrane region, a central linker region and a pair of carboxy-terminal C2 domains responsible for binding Ca2+ (2). The C2 domains appear to be functionally distinct, with the C2A domain responsible for regulating synaptic vesicle fusion in a calcium-dependent manner during exocytosis while the C2B domain allows for interaction between adjacent SYT1 proteins (3). Because synaptotagmin 1 binds calcium and is found in synaptic vesicles, this integral membrane protein is thought to act as a calcium sensor in fast synaptic vesicle exocytosis. Evidence suggests possible roles in vesicle-mediated endocytosis and glucose-induced insulin secretion as well (4,5). SYT1 binds several different SNARE proteins during calcium-mediated vesicle endocytosis and an association between SYT1 and the SNARE protein SNAP-25 is thought to be a key element in vesicle-mediated exocytosis (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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).

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

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

Background: Calcitonin gene-related peptide (CGRP) is a peptide of 37 amino acids that belongs to the calcitonin (CT) family of peptide hormones. The calcitonin gene (CALCA) encodes a number of tissue-specific peptides through alternative splicing of mRNA transcripts and precursor protein cleavage (1). Both calcitonin and α-CGRP are produced from the CALCA gene, while a second gene (CALCB) encodes the related β-CGRP protein (2). α-CGRP and β-CGRP share similar activities and differ by three or fewer residues depending on the species (3). The CGRP peptide activates a heterotrimeric receptor complex that consists of the seven transmembrane-spanning calcitonin receptor-like receptor, the single transmembrane-spanning RAMP1 protein, and an intracellular receptor component protein (4,5). CGRP is expressed in the central and peripheral nervous system in mammals, where it exhibits several important physiologic roles. Research studies demonstrate that CGRP is a potent vasodilatator (6) and a modulator of acetylcholine receptor function at neuromuscular junctions (7). Additional studies indicate that CGRP peptide is involved in feeding (8) and inflammatory pain (9). CGRP peptide also plays a key role in the physiology of migraine attacks. Specifically, CGRP peptide levels increase during acute migraine attacks, which can be ameliorated through treatment with CGRP antagonists (10).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).