The b2-adrenergic receptor (b2AR) is a G-protein coupled receptor that transmits extracellular signals to the intracellular environment. b2AR couples to G-proteins Gs and Gi sending modest inotropic signals via Gs and cardioprotective signals via Gi. This antibody is a polyclonal, anti-peptide antibody (IgG) to an extracellular, N-terminal sequence peculiar to b2AR (residues 15-30, mouse sequence).
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43kDa Dystrophin-associated glycoprotein; (43-DAG, DG, b-DAG, b -DG, DAG1) β-dystroglycan is a component of the dystrophin glycoprotein complex (DGC), a membrane-spanning complex that links the interior cytoskeleton to the extracellular matrix in muscle and other tissues (Winder 2001). It is a transmembrane protein (single TM domain) of 34.9kDa molecular weight, and pI 8.85, which displays an apparent molecular weight of 43kDa by SDS-PAGE due to asparagine-linked glycosylation and a high proportion of proline residues in the cytoplasmic domain. The dystroglycan complex is a subcomplex within the DGC comprising alpha and beta-subunits. Dystroglycan is of importance in cell signalling, cell polarity, cell adhesion and movement. β-dystroglycan binds to dystrophin (in muscle cells) and utrophin (in non-muscle cells), but dissociates from these proteins when phosphorylated on Tyr-892 allowing its association with SH2 containing proteins such as Src and other cytolinker proteins such as plectin.
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Cytoplasmic Ca2+ binds to calmodulin and activates the phosphatase calcineurin (Cn) a 60 kDa protein, and CaM kinase II (CaMKII). One action of Cn is to dephosphorylate cytoplasmic NFAT (nuclear factor of activated T cells), inducing its translocation to the nucleus where it activates antiapoptotic and hypertrophic target genes. The phosphorylation of Cn at Phospho Ser-197 site has been observed in cultured neonatal rat ventricular myocytes (NRVMs) over-expressing constitutively active CAMKII. This appears to inhibit C activity which in turn prevents the dephosphorylation of NFAT and prevents activation of NFAT regulated genes.
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Ca2+/calmodulin-dependent kinase II (CaMKII) is a ubiquitous, multifunctional serine/threonine kinase involved in translating Ca2+- transient signals into cellular responses. Four separate CaMKII genes are expressed in man (α, β, δ, γ) with isoforms within each gene. CaMKII δ and γ are abundant in the heart. CaMKII is activated by Ca2+/CaM binding, and becomes activated for prolonged periods of time following autophosphorylation of Thr-286 or Thr-287 (equivalent residues in different isoforms). Prolonged activation of CaMKII is associated with a variety of vascular and cardiac diseases including stroke, atrial fibrillation cardiac arrhythmia & sudden death, cardiac apoptosis, and heart failure.
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The L-type Ca2+ channel (LTCC, or Cav1.2 or dihydropyridine receptor) is a voltage gated Ca2+ channel of the plasma membrane in brain and heart, which is responsible for the influx of Ca2+ to initiate neurotransmitter release (in neurones) or muscle contraction (in cardiac muscle). The channel is controlled by a number of chemical influences including phosphorylation on Ser-1928 by PKA which enhances ion channel activity. Ser-1928 from rabbit, is conserved across all mammalian species and is thought to be phosphorylated in response to elevated cAMP in these species.
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The extracellular-regulated kinases - Erk1 and Erk2 are widely expressed protein kinases which are activated by mitogen-activated protein kinase 1 and 2 (MEK1/2) via phosphorylation of the TEY motif in the activation loop. Erk1/2 may become autophosporylated at position Thr-188 and this is a marker of cardiac hypertrophy.
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Phospholamban (PLB/PLN) is a small transmembrane protein which plays an important role in controlling the activity of the sarcoplasmic reticulum ATPase (SERCA2a) of cardiac muscle during calcium sequestration. Phospholamban is phosphorylated on separate amino acid residues by cAMP-dependent, and cGMP-dependent (Ser-16) and Ca2+/CaM-dependent (Thr-17) protein kinases in response to β-adrenergic stimulation. Akt has also been shown to phosphorylate Thr-17. The result is an increased calcium pump activity which reduces the time course of the calcium transient, increases the calcium load in the sarcoplasmic reticulum, and consequently, produces a larger calcium transient at the next action potential. However, alteration in this homeostatic interaction has been shown to result in heart failure.
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Ryanodine Receptor (RyR2)
The Ryanodine Receptor (RyR2) is a Ca2+ channel of cardiac muscle that plays a central role in EC coupling. The binding of Ca2+ to ryanodine receptor 2 RyR2 opens the channel and Ca2+ stored in the SR moves through the channel into the cytosol to initiate muscle contraction. Abnormal structure and function of ryanodine receptors has been reported in failing hearts, with Ser-2809 phosphorylation appearing elevated in clinical situations which may contribute to the abnormal Ca2+ handling characteristics of cardiac muscle in these conditions. Serine-2809 can be phosphorylated by PKA or CaMKII, which is coincident with significant change in RyR2 channel function typified by an increased open probability, the abrogation of the inhibitory effects of CaM and Mg2+, dissociation of regulatory factors, expression of subconductance states and the expression of channel activity at diastolic Ca2+ concentrations. This antibody recognises Dephosphorylated Ser-2808 (human sequence) or Ser-2809 from rabbit.
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SERCA, or sarco/endoplasmic reticulum Ca2+-ATPase, or SR Ca2+-ATPase, is a calcium ATPase-type P-ATPase, resides in the sarcoplasmic reticulum (SR) within muscle cells. It is a Ca2+ ATPase that transfers Ca2+ from the cytosol of the cell to the lumen of the SR at the expense of ATP hydrolysis during muscle relaxation. There are 3 major domains on the cytoplasmic face of SERCA: the phosphorylation and nucleotide-binding domains, which form the catalytic site, and the actuator domain, which is involved in the transmission of major conformational changes. The SR has a much higher concentration of Ca2+(10,000x) inside when compared to the intracellular Ca2+ concentration. The rate at which SERCA moves Ca2+ across the SR membrane can be controlled by phospholamban (PLB/PLN) under β-adrenergic stimulation. When PLB is associated with SERCA, the rate of Ca2+ movement is reduced, upon dissociation of PLB Ca2+ movement increases. There are 3 major paralogs, SERCA1-3, which are expressed at various levels in different cell types: ATP2A1 - SERCA1, ATP2A2 - SERCA2, ATP2A3 - SERCA3.
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