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Product listing: ATP2A1/SERCA1 (D54G12) Rabbit mAb, UniProt ID O14983 #12293 to Phospho-IP3 Receptor (Ser1756) (D10E3) Rabbit mAb, UniProt ID Q14643 #8548

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Sarcoplasmic and endoplasmic reticulum Ca2+ ATPases (SERCA) are members of a highly conserved family of Ca2+ pumps (1). SERCA pumps transport Ca2+ from the cytosol to the sarcoplasmic and endoplasmic reticulum lumen against a large concentration gradient (1). ATP2A1 (SERCA1) is a fast-twitch, skeletal muscle sarcoplasmic reticulum Ca2+ ATPase (2). Research studies have shown that mutations in the ATP2A1 gene cause an autosomal recessive muscle disorder known as Brody myopathy, which is characterized by muscle cramping and impaired muscle relaxation associated with exercise (1-3).

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

Application Methods: Western Blotting

Background: The ATP2A2 (SERCA2) calcium pump is one of several sarcoplasmic and endoplasmic reticulum Ca2+-ATPases responsible for regulating calcium transport across intracellular membranes (1). Multiple isoforms have been isolated, with ATP2A2a (SERCA2a) found predominantly in the sarcoplasmic reticulum of muscle cells and ATP2A2b (SERCA2b) more ubiquitously expressed in the endoplasmic reticulum of most cell types (2). An isoform containing a truncated carboxy region (ATP2A2c) is expressed in epithelial and hematopoietic cell lines and may be involved in monocyte differentiation (3). Post-translational modification of ATP2A2 (SERCA2), including phosphorylation and tyrosine nitration, modify Ca2+ -ATPase activity and calcium transport (4,5). Mutation in the corresponding ATP2A2 (SERCA2) gene results in Darier disease, a skin disorder characterized by the presence of dark, keratotic papules or rash found on the head and torso (6).

$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).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells and for immunofluorescent analysis in human and mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Calreticulin (D3E6) XP® Rabbit mAb #12238.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

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

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

Background: Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding, and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor channel (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but regulates proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Calretinin (29 kDa calbindin, calbindin 2) is a calcium-binding protein of the EF-hand family encoded by the CALB2 gene. It is differentially expressed from homologous family member calbindin-d28k in distinct neuronal populations of the retina, auditory system, and cerebellar granule cells (1, 2), and acts as a marker for specific neuronal subsets of the subthalamic nucleus and the substantia nigra (3). Calretinin has been shown to play an important role in modulating neuronal excitability and the induction of long-term potentiation (1). Research has shown that, pathologically, calretinin is a selective marker for epithelial mesothelioma, making it a diagnostic tool to differentiate from adenocarcinomas (4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Calumenin belongs to the CREC family of proteins that also contains reticulocalbin, ERC-55/TCBP-49/E6BP, Cab45, and crocalbin/CBP-50. These EF-hand proteins localize to the endoplasmic reticulum (ER) and are involved in the secretory pathway in mammalian cells (1). Calumenin exists as two isoforms corresponding to alternativly spliced variants of the CALU gene (2). Calumenin has been shown to localize to the ER via a carboxy terminal HDEF ER retention signal (3), and undergoes secretion after trafficking through the secretory pathway (4). Secreted calumenin plays a role in amyloidosis by interacting with serum amyloid P component (5). Calumenin is also a chaperone for mutants of the cystic fibrosis transmembrane conductance regulator (CFTR) (6). Researchers performing a proteomics analysis of endometrial cancer identified calumenin as a potential target for endometrial carcinoma (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The calcium signal-modulating cyclophilin ligand (CAMLG) is a multi-pass endoplasmic reticulum (ER) membrane protein that plays an important role in calcium-mediated signal transduction. The CAMLG protein was first identified in T lymphocytes as a cyclophilin B-binding protein that regulates calcium influx following T-cell receptor (TCR) activation (1). Research studies indicate that CAMLG overexpression activates the transcription factors NFAT and NF-IL2A and leads to increased IL-2 gene transcription, providing additional evidence that CAMLG plays an important role in TCR signal transduction. CAMLG negatively regulates the non-receptor protein kinase Lck, which is critical for the thymocyte selection process (2). Thymocytes deficient for CAMLG fail to undergo normal development, accumulate reactive oxygen species, and exhibit increased apoptosis in response to cytotoxic stimuli (3). The CAMLG protein also acts as a receptor of TRC40, an ATPase that targets newly synthesized proteins in the secretory pathway to the ER membrane. CAMLG interacts with the protein insertion receptor WRB to form the TRC40 receptor complex that is responsible for insertion of tail-anchored proteins into the ER membrane (4).

$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, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: CBARA1/MICU1 is a mitochondrial protein associated to the mitochondrial inner membrane that is comprised of two EF hand helix-loop-helix motifs. CBARA1/MICU1 is involved in mitochondrial calcium entry, metabolic coupling between cytosolic calcium transients, and activation of matrix dehydrogenases (1). Mitochondrial CBARA1/MICU1 is required to preserve normal mitochondrial calcium concentration below the equilibrium level by interacting with the uniporter pore-forming subunit MCU (2). CBARA1/MICU1 is important in pancreatic β-cell mitochondrial calcium uptake and sustained insulin secretion (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CFTR (ABC35, ABCC7, CBAVD, CF, dj760C5.1, MRP7, TNR-CFTR) is a member of the ATP-binding cassette (ABC) transporter superfamily. Mutations in ABC genes have been linked to many diseases. CFTR is a plasma membrane cyclic AMP activated chloride channel that is expressed in the epithelial cells of the lung and several other organs (1,2). It mediates the secretion of Cl- and also regulates several channels including the epithelial sodium channel (ENaC), K+ channels , ATP release mechanisms, anion exchangers, sodium bicarbonate transporters and aquaporin water channels (3,4,5,6,7,8 9,10). Mutations in the CFTR gene cause cystic fibrosis, a disease that is characterized by exocrine pancreatic insufficiency, increase in sweat gland NaCl, male infertility and airway disease (1,2,11). Intracellular trafficking regulates the number of CFTR molecules at the cell surface, which in part regulates Cl- secretion. Deletion of phenylalanine 508 (deltaF508) is the most common mutation in CF patients. This mutation results in retention in the ER, where ER quality control mechanisms target the deltaF508 mutant to the proteosome for degradation (12-14). Therefore, disruption of CFTR trafficking leads to disregulation of Cl- secretion at the plasma membrane of epithelial cells.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Choline kinase (ChoK) catalyzes the phosphorylation of choline, a key step in the biosynthesis of the membrane phospholipid phosphatidylcholine. At least three ChoK isoforms exist in mammalian cells, α-1, α-2, and β. The two α isoforms are transcribed from the same CHKA gene as splice variants, while the β isoform resides on a separate CHKB gene (reviewed in 1).Research studies indicate that ChoKα levels affect signaling through MAPK and Akt pathways (2,3). Investigators have shown that ChoKα plays a role in proliferation and carcinogenesis and is highly expressed/activated in human cancers (4-7). Additional research studies suggest ChoKα may be a potential target for cancer therapy (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins (G proteins) consist of α, β and γ subunits and mediate the effects of hormones, neurotransmitters, chemokines, and sensory stimuli. To date, over 20 known Gα subunits have been classified into four families, Gα(s), Gα(i/o), Gα(q) and Gα(12), based on structural and functional similarities (1,2). Phosphorylation of Tyr356 of Gα(q)/Gα(11) is essential for activation of the G protein, since phenylalanine substitution for Tyr356 changes the interaction of Gα with receptors and abolishes ligand-induced IP3 formation (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphatidylinositol lipids and phosphoinositides are important second messengers, their generation controlling many cellular events. Intracellular levels of these molecules are regulated by phosphoinositide kinases and phosphatases. One of the best characterized lipid kinases is phosphoinositide 3-kinase (PI3K), which is responsible for phosphorylation on the D-3 position of the inositide head group (1). This action of PI3K catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN, the well characterized partnering phosphatase, reverses this process by removing the phosphate from PI(3,4,5)P3 at the D-3 position to generate PI(4,5)P2 (1,2). Dephosphorylation on the D-5 position to generate PI(3,4)P2 occurs through the action of SHIP1 or SHIP2 (3), and dephosphorylation on the D-4 position to generate PI(3)P can occur through the action of inositol polyphosphate 4-phosphatase isoenzymes type I (INPP4a) and type II (INPP4b) (4,5). While INPP4a has been implicated in neuronal survival and megakaryocyte lineage determination (6,7), less is understood about INPP4b. It has been shown that two splice variants of INPP4b occur in mice, each showing distinct tissue distribution and subcellular localization (5,8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Phosphatidylinositol lipids and phosphoinositides are important second messengers, their generation controlling many cellular events. Intracellular levels of these molecules are regulated by phosphoinositide kinases and phosphatases. One of the best characterized lipid kinases is phosphoinositide 3-kinase (PI3K), which is responsible for phosphorylation on the D-3 position of the inositide head group (1). This action of PI3K catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN, the well characterized partnering phosphatase, reverses this process by removing the phosphate from PI(3,4,5)P3 at the D-3 position to generate PI(4,5)P2 (1,2). Dephosphorylation on the D-5 position to generate PI(3,4)P2 occurs through the action of SHIP1 or SHIP2 (3), and dephosphorylation on the D-4 position to generate PI(3)P can occur through the action of inositol polyphosphate 4-phosphatase isoenzymes type I (INPP4a) and type II (INPP4b) (4,5). While INPP4a has been implicated in neuronal survival and megakaryocyte lineage determination (6,7), less is understood about INPP4b. It has been shown that two splice variants of INPP4b occur in mice, each showing distinct tissue distribution and subcellular localization (5,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

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

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

Background: Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is a major PKC substrate expressed in many cell types. MARCKS has been implicated in cell motility, cell adhesion, phagocytosis, membrane traffic, and mitogenesis (1). PKC phosphorylates Ser159, 163, 167, and 170 of MARCKS in response to growth factors and oxidative stress. Phosphorylation at these sites regulates the calcium/calmodulin binding and filamentous (F)-actin cross-linking activities of MARCKS (2-4). Phosphorylation by PKC also results in translocation of MARCKS from the plasma membrane to the cytoplasm (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The mitochondrial calcium uniporter (MCU) is an inner membrane transport protein that is essential for the regulation of calcium uptake and the maintenance of mitochondrial calcium homeostasis (1). MCU is responsible for the rapid transport of calcium ions across the inner membrane and into the mitochondrial matrix, taking advantage of the membrane potential generated by the electron transport chain. Subsequent release of calcium from the matrix through antiporter proteins regulates a number of biological processes, including signal transduction, bioenergetics, and cell death and survival (2,3). The MCU protein contains a pair of transmembrane domains with both carboxy- and amino-terminal ends within the mitochondrial matrix (3). The surrounding uniporter complex contains a number of proteins that regulate calcium ion transport, including the mitochondrial calcium uniporter regulator 1 (MCUR1), mitochondrial calcium uptake proteins 1 and 2 (MICU1, MICU2), and the essential MCU regulator EMRE (3). MICU1 stabilizes the closed state of the transport complex and preserves the normal mitochondrial calcium concentration below the equilibrium level during resting conditions (4). The MCUR1 protein is an essential regulator of calcium uptake, with decreased ion transport in cells with reduced MCUR1 expression (2). EMRE is also essential for MCU transport function where it functions as bridge between MCU uniporter activity and the calcium-sensing MICU1/2 proteins (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: NCX1 (Na+/Ca2+ exchanger, isoform 1) belongs to a conserved family of sodium-calcium membrane antiporter proteins that play a fundamental role in regulating intracellular calcium levels (1). NCX1 facilitates transmembrane transport of Ca2+ ions in exchange for Na+ ions in response to electrochemical gradients (2). Due to its relatively low affinity for calcium, NCX1 most commonly functions to export Ca2+ under acute conditions of high intracellular Ca2+. Notably however, NCX1 is a reversible antiporter, and can thus facilate Ca2+ influx under specialized physiological circumstances (3). Research studies have shown that NCX1 is particularly important for regulating intracellular Ca2+ levels in excitatory cell types (e.g., neurons, cardiac muscle). For example, conditional knockout of NCX1 in mouse cardiac pacemaker cells identified a critical role for NCX1 in the initiation and maintenance of cardiac rhythm (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1 (NIPSNAP1) is a member of a highly conserved family of proteins whose functions include the regulation of channel activity, mitochondrial function and cognitive function.Interaction of NIPSNAP1 with the putative oncogene Ca2+-selective transient receptor potential vanilloid channel 6 (TRPV6) inhibits channel function at the cell membrane (1,2). In prostate cancer cells, alterations in chromatin structure that result in corresponding NIPSNAP1 gene inactivation have been implicated in the malignant phenotype (3).In mouse brain, NIPSNAP has been shown to interact with mitochondrial amyloid precursor protein (APP), which may facilitate the effect of APP on mitochondrial function. (4). NIPSNAP1 expression is also altered in the brains of phenylketonuria (PKU) mice, implying a role for NIPSNAP1 in PKU-related cognitive impairment (5). NIPSNAP1 has also been implicated in pain transmission through its interaction with the neuropeptide nocistatin (NST) in mouse spinal cord (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Enzymes of the phosphodiesterase (PDE) superfamily catalyze the hydrolysis of 3',5'-cyclic nucleotides into the corresponding nucleotide 5'-monophosphates. The PDE superfamily includes 11 subfamilies (PDE1-PDE11) in mammals (1). These enzymes function as important positive and negative regulators of cellular response, including regulation of insulin secretion, heart function, erectile function, and inflammation (2-5). The cAMP-specific phosphodiesterase 4B (PDE4B, DPDE4) is important for the inflammatory response to lipopolysaccharide in monocytes (6). PDE4B plays an important role in the hydrolysis and inactivation of the ubiquitous second messenger cAMP that regulates lymphocyte cell growth and apoptosis (7). Research studies indicate that PDE4B is also involved in psychiatric disorders, including schizophrenia, autism, and depression (8-10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).