生物源
rabbit
品質等級
共軛
unconjugated
抗體表格
affinity isolated antibody
抗體產品種類
primary antibodies
無性繁殖
polyclonal
形狀
buffered aqueous solution
分子量
antigen ~36 kDa
物種活性
human, mouse, bovine, rat
技術
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 1:500-1:1,000 using total rat brain homogenate
UniProt登錄號
運輸包裝
dry ice
儲存溫度
−20°C
基因資訊
human ... PPP1CC(5501)
mouse ... Ppp1cc(19047)
rat ... Ppp1cc(24669)
一般說明
Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. PP1 isoforms catalyze a wide range of protein dephosphorylation reactions in a tightly regulated manner and is expressed abundantly in the brain. PP1 has broad functions covering glycogen metabolism, protein synthesis, cell cycle and growth and muscle contractility. PP1 forms exclusive complexes with >50 regulatory subunits that allows for restricted subcellular location and thereby distinct cellular functions. There are 3 isoforms of PP1 (α, β and γ1) with 90% homology. PP1γ1 is expressed in brain and has been reported to be crucial for cell proliferation in lung carcinoma cells, A549. .
The antibody specifically recognizes protein phosphatase 1γ1 isoform.
The antibody specifically recognizes protein phosphatase 1γ1 isoform.
免疫原
synthetic peptide (TPPRGMITKQAKK) corresponding to the C-terminus of the protein phosphatase 1γ1 catalytic subunit (amino acid residues 311-323).
應用
Anti-Serine/Threonine Protein Phosphatase 1γ1 antibody may be used for detection by immunoblotting in total rat brain homogenate at a working dilution of 1:500-1:1000. It is suitable for immunoprecipitation and protein microarray applications.
外觀
Solution in phosphate buffered saline with 0.08% sodium azide.
免責聲明
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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The Journal of biological chemistry, 275(3), 1846-1854 (2000-01-15)
In lower eukaryotic organisms, the loss of serine/threonine protein phosphatase type 1 (PP1) results in growth arrest after the onset of mitosis. In humans, four highly homologous isoforms of PP1 (PP1alpha, PP1delta, PP1gamma1, and PP1gamma2) have been identified. Determining the
The Journal of comparative neurology, 413(3), 373-384 (1999-09-29)
Protein phosphatase 1 (PP1) is a gene family with a number of important functions in brain. Association with a wide variety of regulatory/targeting subunits is thought to be instrumental in directing the phosphatase to specific subcellular locations and substrates. By
Journal of cell science, 115(Pt 2), 241-256 (2002-02-13)
Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits. Most of these target
Trends in biochemical sciences, 35(8), 450-458 (2010-04-20)
Protein Ser/Thr phosphatase-1 (PP1) catalyzes the majority of eukaryotic protein dephosphorylation reactions in a highly regulated and selective manner. Recent studies have identified an unusually diversified PP1 interactome with the properties of a regulatory toolkit. PP1-interacting proteins (PIPs) function as
Protein phosphatases: recent progress.
Advances in second messenger and phosphoprotein research, 23, 1-121 (1991-01-01)
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