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Description: Spectrin is an actin binding protein that is a major component of the plasma membrane skeleton. Spectrins function as membrane organizers and stabilizers by forming dimers, tetramers and higher polymers. Spectrin alpha and spectrin beta are present in erythrocytes, whereas spectrin alphaII (fodrin alpha) and spectrin betaI (fodrin beta) are present in other somatic cells. SPTBN2/Spectrin betaIII is highly homologous to both spectrin betaI and spectrin betaII. SPTBN2 is highly expressed in brain, kidney, pancreas and liver, and at lower levels in lung and placenta.
Catalog Number: 76194-656
Supplier: Prosci


Description: 4-{2-[3-(4,4,5,5-Tetramethyl[1,3,2]dioxaborolan-2-yl)phenoxy]ethyl}morpholine ≥97%
Catalog Number: 102836-260
Supplier: Matrix Scientific


Description: cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. PKA beta (catalytic subunit) is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK.
Catalog Number: 10339-186
Supplier: Bioss


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
Catalog Number: 10350-356
Supplier: Bioss


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
Catalog Number: 10352-750
Supplier: Bioss


Description: Human Chemokine (C-X-C motif) Ligand 4 (CXCL4) is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 contains several heparin-binding sites at the C-terminal region and binds heparin with high affinity. The active CXCL4 protein is a tetramer. Human and mouse CXCL4 share 64% sequence identity. CXCL4 is chemotactic for neutrophils, fibroblasts and monocytes and plays a critical role in inflammation and wound repair. CXCL4 functions via a splice variant of the chemokine receptor CXCR3, known as CXCR3B. The major physiologic role of CXCL4 appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. In contrast to other CXC chemokines, CXCL4 lacks chemotactic activity for polymorphonuclear granulocytes.
Catalog Number: 75791-428
Supplier: Prosci


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
Catalog Number: 10350-358
Supplier: Bioss


Description: cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Several alternatively spliced transcript variants encoding distinct isoforms have been observed.
Catalog Number: 10394-472
Supplier: Bioss


Description: Spectrin is an actin binding protein that is a major component of the plasma membrane skeleton. Spectrins function as membrane organizers and stabilizers by forming dimers, tetramers and higher polymers. Spectrin alpha and spectrin beta are present in erythrocytes, whereas spectrin alphaII (fodrin alpha) and spectrin betaI (fodrin beta) are present in other somatic cells. SPTBN2/Spectrin betaIII is highly homologous to both spectrin betaI and spectrin betaII. SPTBN2 is highly expressed in brain, kidney, pancreas and liver, and at lower levels in lung and placenta.
Catalog Number: 76194-670
Supplier: Prosci


Description: Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency. [provided by RefSeq].
Catalog Number: 76012-298
Supplier: Prosci


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene.
Catalog Number: 76085-114
Supplier: Bioss


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]
Catalog Number: 10350-360
Supplier: Bioss


Description: ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene.
Catalog Number: 76085-112
Supplier: Bioss


Description: PRKACA and PRKACB are members of the Ser/Thr protein kinase family and are a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.PKA alpha + beta (catalytic subunits) (phospho Thr198).
Catalog Number: 76084-788
Supplier: Bioss


Description: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms. This enzyme is required for embryonic development since TH knockout mice die before or at birth. Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH. Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels.
Catalog Number: 10071-934
Supplier: Prosci


Description: Voltage-gated K+ channels in the plasma membrane control the repolarization and the frequency of action potentials in neurons, muscles and other excitable cells. The KV gene family encodes more than 30 proteins that comprise the subunits of the K+ channels, and they vary in their gating and permeation properties, subcellular distribution and expression patterns. Functional KV channels assemble as tetramers consisting of pore-forming å subunits (KV), which include the KV1, KV2, KV3 and KV4 proteins, and accessory or KV-subunits that modify the gating properties of the coexpressed KV subunits. KV∫, also known as KCNAB1 (potassium voltage-gated channel, shaker-related subfamily, beta member 1), is a 419 amino acid accessory K+ channel protein that exists as three alternatively spliced isoforms and regulates the activity of the pore-forming å subunit. It is expressed in brain, with highest levels detected in caudate nucleus, hippocampus and thalamus.
Catalog Number: 10671-194
Supplier: Bioss


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