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Merck
CN

C9243

Sigma-Aldrich

Anti-CHIP (C-terminal) 兔抗

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

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别名:
Anti-CHIP, carboxy terminus of Hsp70p-interacting protein, Anti-HSPABP2, Anti-NY-CO-7, Anti-STUB1, Anti-UBOX1
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

形式

buffered aqueous solution

分子量

antigen ~35 kDa

种属反应性

human, mouse, rat

浓度

~1 mg/mL

技术

western blot: 1-2 μg/test using HEK-293T cells lysate and mouse brain extract (S2 fraction)

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 ... STUB1(10273)
mouse ... Stub1(56424)
rat ... Stub1(287155)

一般描述

CHIP (carboxy terminus of Hsp70-interacting protein, also known as STIP1-homology and U-box containing protein 1, STUB1, HSPABP2, NY-CO-7, SDCCAG7, UBOX1), is a dual-function chaperone/E3 ubiquitin ligase. CHIP has 3 functional domains: a N-terminal tetratricopeptide repeat (TPR), a U-box at its C-terminus, and a highly charged internal region. It is located on human chromosome 16p13.3.

应用

Anti-CHIP (C-terminal) antibody produced in rabbit has been used in western blotting and histology to stain testes and ovary sections.
Anti-CHIP (C-terminal) antibody produced in rabbit is suitable for immunoblotting at a working concentration of 1-2 μg/mL using HEK-293T cells lysate and mouse brain extract (S2 fraction).

生化/生理作用

CHIP (carboxy terminus of Hsp70-interacting protein) plays a crucial role in regulating protein quality control at multiple levels. It ubiquitinates Hsp70, a cytosolic chaperone and enhances refolding of stress damaged proteins. Additionally, it has E3 ubiquitin ligase activity and triggers proteasome degradation of irreversibly damaged proteins to prevent cellular toxicity. The ubiquitination, aggregation and degradation of several proteins involved in neurodegenerative disorders including tau, huntingtin, Cu/Zn SOD1, ataxin-1, and α-synuclein are regulated by CHIP and Hsp70. The aggregation and toxicity of polyglutamine (polyQ) expanded proteins is suppressed by CHIP. It also regulates stress-dependent apoptosis.

外形

0.01M 磷酸缓冲盐溶液,pH 7.4,含 15mM 叠氮化钠。

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.

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

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Yasaman Pakdaman et al.
International journal of molecular sciences, 22(11) (2021-06-03)
Variants in STUB1 cause both autosomal recessive (SCAR16) and dominant (SCA48) spinocerebellar ataxia. Reports from 18 STUB1 variants causing SCA48 show that the clinical picture includes later-onset ataxia with a cerebellar cognitive affective syndrome and varying clinical overlap with SCAR16.
Bridget F Donnelly et al.
The Journal of biological chemistry, 288(18), 13124-13135 (2013-03-14)
The thiazide-sensitive NaCl cotransporter (NCC) is the primary mediator of salt reabsorption in the distal convoluted tubule and is a key determinant of the blood pressure set point. Given its complex topology, NCC is inefficiently processed and prone to endoplasmic
Cloning and characterization of carboxyl terminus of heat shock cognate 70-interacting protein gene from the silkworm, Bombyx mori
Ohsawa T, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 201, 29-36 (2016)
Regulation of autophagic flux by CHIP
Guo D, et al.
Neuroscience Bulletin, 31(4), 469-479 (2015)
Victor M Miller et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 25(40), 9152-9161 (2005-10-07)
Huntington's disease (HD) and other polyglutamine (polyQ) neurodegenerative diseases are characterized by neuronal accumulation of the disease protein, suggesting that the cellular ability to handle abnormal proteins is compromised. As both a cochaperone and ubiquitin ligase, the C-terminal Hsp70 (heat

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