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当前位置: 首页 > 产品中心 > exosome_research > Enzolifesciences/HSP90α monoclonal antibody (K41009) (PE conjugate)/ADI-SPA-839PE-0050/50µg
商品详细Enzolifesciences/HSP90α monoclonal antibody (K41009) (PE conjugate)/ADI-SPA-839PE-0050/50µg
Enzolifesciences/HSP90α monoclonal antibody (K41009) (PE conjugate)/ADI-SPA-839PE-0050/50µg
Enzolifesciences/HSP90α monoclonal antibody (K41009) (PE conjugate)/ADI-SPA-839PE-0050/50µg
商品编号: ADI-SPA-839PE-0050
品牌: enzolifesciences
市场价: ¥4520.00
美元价: 2712.00
产地: 美国(厂家直采)
公司:
产品分类: 外泌体研究
公司分类: exosome_research
联系Q Q: 3392242852
电话号码: 4000-520-616
电子邮箱: info@ebiomall.com
商品介绍

Product Specification:

Alternative Name:HSP86, Heat shock protein 90α
 
Clone:K41009
 
Host:Mouse
 
Isotype:IgG2a
 
Immunogen:Recombinant human Hsp90α.
 
UniProt ID:P07900
 
Species reactivity:Human, Mouse, Rat
Rabbit
 
Recommended Dilutions/Conditions:Flow Cytometry (1:100)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Detects a band of ~90kDa by Western blot.
 
Purity Detail:Protein G-affinity purified.
 
Formulation:Liquid. In PBS, pH 7.2, containing 0.09% sodium azide.
 
Handling:Avoid freeze/thaw cycles. Protect from light.
 
Shipping:Blue Ice Not Frozen
 
Long Term Storage:+4°C
 
Scientific Background:The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
 
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