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当前位置: 首页 > 产品中心 > exosome_research > Enzolifesciences/HSP27 monoclonal antibody (G3.1)/ADI-SPA-800-D/50µg
商品详细Enzolifesciences/HSP27 monoclonal antibody (G3.1)/ADI-SPA-800-D/50µg
Enzolifesciences/HSP27 monoclonal antibody (G3.1)/ADI-SPA-800-D/50µg
Enzolifesciences/HSP27 monoclonal antibody (G3.1)/ADI-SPA-800-D/50µg
商品编号: ADI-SPA-800-D
品牌: enzolifesciences
市场价: ¥4080.00
美元价: 2448.00
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:HspB1, Heat shock protein 27
 
Clone:G3.1
 
Host:Mouse
 
Isotype:IgG1
 
Immunogen:Native human Hsp27.
 
UniProt ID:P04792
 
GenBank ID:L39370
 
Species reactivity:Human, Mouse, Rat
Bovine, Fish, Monkey
 
Applications:ELISA, ICC, IHC (PS), IP, WB
Electron microscopy, in vitro Assay
 
Recommended Dilutions/Conditions:Western Blot (1:1,000, colorimetric)
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 ~27kDa by Western blot.
 
Purity Detail:Protein G affinity purified.
 
Formulation:Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background:Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
 
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