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| Product Data | |
| Description | Recombinant protein of human heat shock 70kDa protein 6 (HSP70B') (HSPA6) |
| Species | Human |
| Expression Host | HEK293T |
| Expression cDNA Clone or AA Sequence | Recombinant protein was produced with TrueORF clone, RC207795. Click on the TrueORF clone link to view cDNA and protein sequences. |
| Tag | C-Myc/DDK |
| Predicted MW | 70.8 kDa |
| Concentration | >50 ug/mL as determined by microplate BCA method |
| Purity | > 80% as determined by SDS-PAGE and Coomassie blue staining |
| Buffer | 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol |
| Reference Data | |
| Locus ID | 3310 |
| Refseq Size | 2664 |
| Cytogenetics | 1q23.3 |
| Refseq ORF | 1929 |
| Synonyms | heat shock 70kD protein 6 (HSP70B'); heat shock 70kDa protein 6 (HSP70B'); HSP70B' |
| Summary | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). [UniProtKB/Swiss-Prot Function] |
| Protein Pathways | Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Spliceosome |
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