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Merck
CN

S5188

Sigma-Aldrich

Anti-SGK antibody produced in rabbit

buffered aqueous solution, IgG fraction of antiserum

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别名:
Anti-SGK
MDL编号:
UNSPSC代码:
12352203
NACRES:
NA.44

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

IgG fraction of antiserum

抗体产品类型

primary antibodies

克隆

polyclonal

形式

buffered aqueous solution

分子量

antigen 50 kDa

种属反应性

human

技术

indirect immunofluorescence: 1:2,000 using 3% paraformaldehyde-fixed, 0.5% Triton X-100 treated human epidermal carcinoma A431cell line
microarray: suitable
western blot: 1:2,000 using whole cell extract of the human epidermal carcinoma A431 cell line

UniProt登记号

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... SGK1(6446)

一般描述

Anti-SGK is developed in rabbit using a synthetic peptide corresponding to the C-terminus of human SGK conjugated to KLH (keyhole limpet hemocyanin). SGK is localized to the perinuclear or cytoplasmic compartment as a hypophosphorylated protein.
SGK (serum and glucocorticoid-regulated protein kinase) is a 50 kDa member of Ser/Thr kinase family. Sequence of sgk is well conserved across species, the human and rat SGK amino acid sequences are 96-98% identical.

应用

Anti-SGK antibody produced in rabbit has been used in :
  • immunoprecipitation
  • western blotting
  • immunofluorescence

生化/生理作用

SGK (serum and glucocorticoid-regulated protein kinase) plays an important role in signal transduction activated by mineral corticoids. It is also regulated at the transcription level by stimuli including glucocorticoid, serum, follicle stimulating hormone as well as changes in cell volume. SGK levels are strongly affected by osmotic changes. SGK is strongly and rapidly stimulated in kidney cells in response to aldosterone and stimulates epithelial Na+ channels, suggesting a central role of SGK in the regulation of sodium transport and homeostasis. SGK transcription is markedly increased in diabetic nephropathy, in response to excessive extracellular glucose concentrations. The localization of SGK in the cell is regulated by hormones or serum. For cell cycle progression, the shuttling of SGK between nucleus and cytoplasm is required.

外形

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

免责声明

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.

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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cell cycle and hormonal control of nuclear-cytoplasmic localization of the serum-and glucocorticoid-inducible protein kinase, sgk, in mammary tumor cells a novel convergence point of anti-proliferative and proliferative cell signaling pathways
Buse P, et al.
The Journal of biological chemistry, 274(11), 7253-7263 (1999)
Joseph R Shaw et al.
Aquatic toxicology (Amsterdam, Netherlands), 98(2), 157-164 (2010-03-09)
Seawater acclimation in killifish, Fundulus heteroclitus, is mediated in part by a rapid (1h) translocation of CFTR Cl(-) channels from an intracellular pool to the plasma membrane in gill and increased CFTR-mediated Cl(-) secretion. This effect is mediated by serum
Differential ubiquitylation of the mineralocorticoid receptor is regulated by phosphorylation
Faresse N, et al.
Faseb Journal, 26(10), 4373-4382 (2012)
A Náray-Fejes-Tóth et al.
Kidney international, 57(4), 1290-1294 (2000-04-12)
The sgk, an aldosterone-induced gene in mineralocorticoid target cells, regulates the epithelial sodium channel. Aldosterone increases sodium reabsorption in tight epithelia. The early phase of this stimulatory effect is thought to involve activation of apical sodium channels. To identify immediate-early
Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume
Waldegger S, et al.
Proceedings of the National Academy of Sciences of the USA, 94(9), 4440-4445 (1997)

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