商品编号


AG-40T-0273-C050



品牌


Adipogen



公司


Adipogen



公司分类


Proteins



Size

50 ?g

商品信息


More Information



Product Details



Synonyms

Heat Shock Protein 90 α; HSP86; HSP90A; HSP90AA1; HSP90N; HSPC1; HSPCA; HSPN; LAP2; Lipopolysaccharide-associated Protein 2; Renal Carcinoma Antigen NY-REN-38



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Human HSP90α (Accession Nr. P07900).



Crossreactivity

Human



Formulation

Liquid. In 50mM Hepes pH 7.5, 50mM KCl, 1mM TCEP.



Other Product Data


Use:
This protein works in conjunction with the co-chaperone p23/PTGES3. Both proteins are required for enzymatic activity in various
in vitro
protein refolding assays. Typical enzyme concentration for use
in vitro
is dependent on specific application. We recommend an initial p23/PTGES3 concentration of 2-?3μM, and HSP90α/HSP90AA1 concentration equimolar (or above) to p23/PTGES3.



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

DRY ICE



Short Term Storage

-20°C



Long Term Storage

-80°C



Handling Advice

Aliquot to avoid freeze/thaw cycles.



Use/St
ABI
lity

Stable for at least 6 months after receipt when stored at -80°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





Members of the HSP90 family are essential chaperones found in all organisms from bacteria to humans. HSP90 complexes often interact with proteins in their native conformation and help to maintain/st
ABI
lize ligand-bound states. In this capacity, HSP90 plays a central role in function and turnover of many proteins involved in processes such as signal transduction, cell cycle control and Cancer. HSP70 family members and HSP90 complexes frequently act in tandem, with the former participating in the folding of the client proteins and HSP90 st
ABI
lizing them in a way favorable for interaction with ligands. HSP90 forms complexes with an array of co-chaperones that both regulate its interaction with client proteins and stimulate its ATPase activity. By binding to different co-chaperones HSP90 acquires specificity for different families of client proteins. Many of the HSP90-client proteins are involved in tumor cell growth and HSP90 inhibitors are important as potential anticancer drugs. Inhibition of HSP90 also prevents the formation of protein aggregates in models of Parkinson disease, Huntington disease, and others.