Reactivity | HuSpecies Glossary |
Applications | Enzyme Activity |
Format | Carrier-Free |
Details of Functionality | Reaction conditions will need to be optimized for each specific application. We recommend an initial HSP70/HSPA1A concentration of 2-3 μM for in vitro use. IMPORTANT: HSP40/DNAJB1 (Catalog # AP-110), or another suitable co-chaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A. |
Source | E. coli-derived human HSP70/HSPA1A protein Met1 - Asp641 |
Accession # | |
Protein/Peptide Type | Recombinant Proteins |
Gene | HSPA1A |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain. |
Dilutions |
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Theoretical MW | 70 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a solution in HEPES, NaCl, DTT. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain. |
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 (1). HSP70/HSPA1A promotes the proper folding of nascent polypeptides and assists in the refolding of denatured proteins (2). 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 (3,4). HSP70/HSPA1A can be regulated post-translationally via multiple mechanisms, including phosphorylation, ubiquitination, and methylation (5-8). For example, unmethylated HSP70/HSPA1A localizes to the cytoplasm, but following methylation on Lys561 it is found only in the nucleus (8). Pathologically, HSP70/HSPA1A has been implicated in the promotion of multiple cancer types (8-10). Conversely, it is thought to protect against several neurodegenerative diseases that are caused by the accumulation of misfolded proteins (11,12).
Diseases for HSP70/HSPA1A (AP-100)Discover more about diseases related to HSP70/HSPA1A (AP-100).
| Pathways for HSP70/HSPA1A (AP-100)View related products by pathway.
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PTMs for HSP70/HSPA1A (AP-100)Learn more about PTMs related to HSP70/HSPA1A (AP-100).
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Gene Symbol | HSPA1A |
Uniprot |