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Merck
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主要文件

SAB4504332

Sigma-Aldrich

Anti-phospho-Akt (pThr308) antibody produced in rabbit

affinity isolated antibody

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About This Item

UNSPSC代码:
12352203
NACRES:
NA.41

生物来源

rabbit

质量水平

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

表单

buffered aqueous solution

分子量

antigen 55 kDa

种属反应性

mouse, rat, human

浓度

~1 mg/mL

技术

ELISA: 1:10000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI登记号

UniProt登记号

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

phosphorylation (pThr308)

基因信息

一般描述

The AKT/protein kinase B gene has three homologues, namely PKBα (Akt1), PKBβ (Akt2), and PKBγ (Akt3), which are localized to human chromosome 14q32, 19q13, and 1q44, respectively. The members of AKT family contain an amino-terminal pleckstrin homology (PH) domain, a short α-helical linker, and a carboxyl-terminal kinase domain. The AKT1 and AKT2 genes are expressed highly in insulin-responsive tissues, such as brown fat.

免疫原

The antiserum was produced against synthesized peptide derived from human Akt around the phosphorylation site of Thr308.

Immunogen Range: 276-325

应用

Anti-phospho-Akt (pThr308) antibody produced in rabbit has been used in immunoblotting.

生化/生理作用

AKT is activated in a multistep process that involves its translocation across the membrane and its phosphorylation. The 3′-phosphorylated phosphoinositides, 3,4,5-trisphosphate (PI-3,4,5-P3) and PI-3,4,-P2 produced by PI3K bind to the PH (pleckstrin homology) domain and this binding facilitates the localization of AKT kinases to the plasma membrane. Once localized, PDK1 (3-phosphoinositide-dependent kinase) phosphorylates Thr-308/309 residue on the AKT molecule, which is essential for its activation. Another residue, Ser- 473/474 on AKT, is also phosphorylated by PDK2. This phosphorylation, although not necessary, increases the activity of AKT. It plays a role in cell survival by regulating the effect of growth factors. AKT may facilitate phosphorylation and inactivation of glycogen synthase kinase-3 by insulin. In adipocytes, it may be involved in the activation of glucose transporter translocation. It is involved in the regulation of several proteins that are involved in cellular processes, such as metabolism, apoptosis, and proliferation. Variations in PI3K-AKT signaling have been observed in several types of cancer, such as human gastric cancer, prostate and breast cancers.

特点和优势

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

外形

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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.

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储存分类代码

12 - Non Combustible Liquids

WGK

nwg

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Lee D Spate et al.
Molecular reproduction and development, 82(4), 315-320 (2015-03-18)
The application of embryo-related technology is dependent on in vitro culture systems. Unfortunately, most culture media are suboptimal and result in developmentally compromised embryos. Since embryo development is partially dependent upon Warburg Effect-like metabolism, our goal was to test the
PI3K-Akt pathway: Its functions and alterations in human cancer
Osaki, M
Apoptosis, 9, 667-676 (2004)
PS48 can replace bovine serum albumin in pig embryo culture medium, and improve in vitro embryo development by phosphorylating AKT
Spate LD
Molecular Reproduction and Development, 82, 315?320-315?320 (2015)
Protein kinase B/Akt mediates effects of insulin on hepatic insulin-like growth factor-binding protein-1 gene expression through a conserved insulin response sequence.
Cichy, S
The Journal of Biological Chemistry, 273, 6482-6487 (1998)
J Matthew Kuczmarski et al.
Experimental physiology, 103(4), 545-558 (2018-01-10)
What is the central question of this study? Translocation of nNOSμ initiates catabolic signalling via FoxO3a and skeletal muscle atrophy during mechanical unloading. Recent evidence suggests that unloading-induced muscle atrophy and FoxO3a activation are redox sensitive. Will a mimetic of

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