HSP90 (C45G5) Rabbit mAb

HSP90 (C45G5) Rabbit mAb Suppliers list
Company Name: Shanghai Universal Biotech Co.,Ltd  
Tel: 15921930842 15921930842
Email: yh-wang@univ-bio.com
Products Intro: Product Name:HSP90 (C45G5) Rabbit mAb
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Company Name: Cell Signaling Technology Inc  
Tel: 21-80243558 86218024
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Products Intro: Product Name:HSP90 (C45G5) Rabbit mAb
Company Name: Shanghai Universal Biotech Co.,Ltd  
Tel: 021-38939000-9068
Email: dongh@univ-bio.com
Products Intro: Product Name:HSP90 (C45G5) Rabbit mAb
Company Name: Hangzhou Baixi Biotechnology Co., Ltd.  
Tel: 0571-86469640
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Products Intro: Product Name:HSP90 (C45G5) Rabbit mAb
Company Name: Zhengzhou Xuqian Biotechnology Co., Ltd.  
Tel: 13939040623
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Products Intro: Product Name:HSP90 (C45G5) Rabbit mAb
HSP90 (C45G5) Rabbit mAb Basic information
Source Reactivity Background References
Product Name:HSP90 (C45G5) Rabbit mAb
Synonyms:HSP90 (C45G5) Rabbit mAb
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MW:0
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Mol File:Mol File
HSP90 (C45G5) Rabbit mAb Structure
HSP90 (C45G5) Rabbit mAb Chemical Properties
Safety Information
MSDS Information
HSP90 (C45G5) Rabbit mAb Usage And Synthesis
SourceRabbit
ReactivityHuman;Mouse;Rat;Monkey
BackgroundHSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner. HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23. The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments. When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome. The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules. They also play a role in vesicle formation and protein trafficking.
References[1] Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
[2] Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
[3] Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
[4] Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
HSP90 (C45G5) Rabbit mAb Preparation Products And Raw materials
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