HSP70 (human) (rec.)
AG-40T-0272-C05050 µgCHF 463.00
AG-40T-0272-C100100 µgCHF 577.00
|Synonyms||Heat Shock Protein 70; HSP70-1A; HSPA1A|
|Sequence||Human HSP70 (Accession Nr. AAD21816 ).|
|Formulation||Liquid. In 50mM HEPES, pH 8, 100mM NaCl, 5mM DTT.|
|Other Product Data||
Use: An initial protein concentration of 2-3μM for in vitro use.
IMPORTANT: HSP40/DNAJB1, or another suitable cochaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A. Reaction conditions will need to be optimized for each specific application.
|Declaration||Manufactured by Boston Biochem|
|Shipping and Handling|
|Short Term Storage||-20°C|
|Long Term Storage||-80°C|
|Handling Advice||Aliquot to avoid freeze/thaw cycles.|
|Use/Stability||Stable for at least 1 year after receipt when stored at -80°C.|
|Product Specification Sheet|
Heat Shock 70kDa Protein (HSP70), also known as Heat Shock 70kDa Protein 1A (HSPA1A), is a 641 amino acid (aa) member of the HSP70 family of molecular chaperones with a predicted molecular weight of 70 kDa. Human HSP70/HSPA1A shares 95% and 97% aa sequence identity with the mouse and rat orthologs, respectively. It has an N-terminal nucleotide-binding domain, which contains ATPase activity, and a C-terminal substrate-binding domain. HSP70/HSPA1A promotes the proper folding of nascent polypeptides and assists in the refolding of denatured proteins. However, if either of these processes proceeds too slowly or fails, HSP70/HSPA1A can interact with the HSP40 co-chaperone protein and the CHIP/STUB1 ubiquitin ligase (E3) to promote ubiquitination and degradation of the nascent polypeptide or denatured protein. HSP70/HSPA1A can be regulated post-translationally via multiple mechanisms, including phosphorylation, ubiquitination, and methylation. For example, unmethylated HSP70/HSPA1A localizes to the cytoplasm, but following methylation on Lys561 it is found only in the nucleus. Pathologically, HSP70/HSPA1A has been implicated in the promotion of multiple cancer types. Conversely, it is thought to protect against several neurodegenerative diseases that are caused by the accumulation of misfolded proteins.