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当前位置: 首页 > 产品中心 > Specialty_ELISA_kits > Enzolifesciences/TRAP1 polyclonal antibody/ADI-SPA-970-0200/200µg
商品详细Enzolifesciences/TRAP1 polyclonal antibody/ADI-SPA-970-0200/200µg
Enzolifesciences/TRAP1 polyclonal antibody/ADI-SPA-970-0200/200µg
Enzolifesciences/TRAP1 polyclonal antibody/ADI-SPA-970-0200/200µg
商品编号: ADI-SPA-970-0200
品牌: enzolifesciences
市场价: ¥6600.00
美元价: 3960.00
产地: 美国(厂家直采)
公司:
产品分类: 特色ELISA试剂盒
公司分类: Specialty_ELISA_kits
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:HSP75, Mitochondrial HSP90, MtHSP90, TNF receptor-associated protein 1
 
Host:Rabbit
 
Immunogen:Recombinant human TRAP1.
 
UniProt ID:Q12931
 
Species reactivity:Human, Mouse, Rat
Bovine
 
Applications:WB
 
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 ~72kDa by Western blot.
 
Purity Detail:Protein A 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: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. It includes cytoplasmic (Hsp90-alpha/beta), ER (Grp94) and mitochondrial (TRAP1) localized members. Hsp90 is structurally composed of an N-terminal ATP binding domain, a medial substrate-binding region, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones to stabilize a multitude of client protein substrates. TRAP1 (aka Hsp75) was originally identified as a chaperone binding partner for retinoblastoma protein. TRAP1 was later found by immunofluorescence to be localized to the mitochondria. TRAP1 is significantly more active as an ATPase due in part to the lack of regulatory elements in the C-terminus, but retains the ability to dimerize. However, it does not form stable complexes with typical cochaperones of Hsp90 like p23 and HOP4. TRAP1 has been identified as a protective element for cell survival, and has been suggested as a target for anti-cancer therapeutics.
 
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