G0296
AntiGRK2 兔抗
affinity isolated antibody, buffered aqueous solution
别名:
Anti-β-ARK1, Anti-β-Adrenergic receptor kinase-1, Anti-ADRBK1, Anti-BARK1, Anti-G Protein-dependent receptor kinase 2
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~80 kDa
species reactivity
human
enhanced validation
recombinant expression
Learn more about Antibody Enhanced Validation
technique(s)
western blot: 0.5-1 μg/mL using HEK-293T cells expressing human GRK2 or Jurkat cell lysate
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ADRBK1(156)
General description
G protein-coupled receptor kinases (GRK2) belongs to the GRK family that includes seven known GRKs, termed as GRK1-7. It is also known as β-adrenergic receptor kinase-1 (β-ARK1) and ADRBK1. It regulates the activity of G protein-coupled receptors (GPCRs). GRKs facilitate the uncoupling of GPCRs from G proteins, and participate directly in receptor endocytosis and trafficking, and modulation of ERK/MAPK cascade by GPCRs. It phosphorylates the activated form of the β2-adrenergic receptor (β2-AR) and related GPCRs. The GRK2 activity is regulated by different mechanisms including phosphorylation by kinases such as PKC, Src, ERK1/2 and p38MAPK. Phosphorylated ERK inactivates GRK2 on Ser670 in a negative feedback mechanism.
Immunogen
Synthetic peptide corresponding to amino acids 674-689 located at the C-terminus of human GRK2/βARK1, conjugated to KLH. The immunizing sequence is specific to GRK2 (not found in human GRK1, and GRK3-7). It is identical in dog GRK2 and highly conserved (single amino acid substitution) in rat, mouse, and bovine GRK2/βARK1.
Application
Anti-GRK2 antibody is suitable for western blots of cortical synaptoneurosomes to study the β-arrestin-1 and ERK protein expression. It is also suitable for western blot at a concentration of 0.5-1μg/mL using HEK-293T cells expressing human GRK2 or Jurkat cell lysate.
Biochem/physiol Actions
G protein-coupled receptor kinase 2 (GRK2) is involved in the pathogenesis of chronic heart failure.
Physical form
0.01M 磷酸缓冲盐溶液，pH 7.4，含 15mM 叠氮化钠。
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Adrenal GRK2 upregulation mediates sympathetic overdrive in heart failure
Lymperopoulos A, et al.
Nature Medicine, 13(3), 315-315 (2007)
J A Pitcher et al.
Annual review of biochemistry, 67, 653-692 (1998-10-06)
G protein-coupled receptor kinases (GRKs) constitute a family of six mammalian serine/threonine protein kinases that phosphorylate agonist-bound, or activated, G protein-coupled receptors (GPCRs) as their primary substrates. GRK-mediated receptor phosphorylation rapidly initiates profound impairment of receptor signaling, or desensitization. This
Petronila Penela et al.
Cellular signalling, 15(11), 973-981 (2003-09-23)
G protein-coupled receptor kinases (GRKs) are key modulators of G protein-coupled receptor signalling. Increasing evidence points to the occurrence of complex mechanisms able to modulate the subcellular localization, activity and expression levels of GRKs, revealing new functional interactions of these
Ruxu Zhai et al.
International journal of molecular sciences, 23(5) (2022-03-11)
G-protein coupled receptor (GPCR) kinase 2 (GRK2) is upregulated in heart failure (HF) patients and mouse models of cardiac disease. GRK2 is a regulator of β-adrenergic receptors (βARs), a GPCR involved in ionotropic and chronotropic responses. We and others have
Xiu-Rong Ren et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(5), 1448-1453 (2005-01-27)
Signaling through beta-arrestins is a recently appreciated mechanism used by seven-transmembrane receptors. Because G protein-coupled receptor kinase (GRK) phosphorylation of such receptors is generally a prerequisite for beta-arrestin binding, we studied the roles of different GRKs in promoting beta-arrestin-mediated extracellular
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