protein

HSPA2 Protein, Human (His)

HY-P701385

10 μg;50 μg

160;450 USD

HSPA2 Protein, Human (His)

proteins

E. coli

10 μg;50 μg

160;450 USD

The HSPA2 protein is a molecular chaperone that protects the proteome, aids in protein folding and transport, activates proteolysis, and regulates protein complex formation. It ensures accurate protein folding and degradation, with substrate affinity related to its nucleotide status. HSPA2 Protein, Human (His) is the recombinant human-derived HSPA2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of HSPA2 Protein, Human (His) is 638 a.a., .

Human

HSPA2 protein, a molecular chaperone, engages in diverse cellular processes critical for proteome integrity. Its functions encompass safeguarding the proteome from stress, assisting in the folding and transport of newly synthesized polypeptides, activating the proteolysis of misfolded proteins, and orchestrating the formation and dissolution of protein complexes. As a key player in the protein quality control system, HSPA2 ensures the accurate folding of proteins, refolding of misfolded counterparts, and the targeted degradation of proteins. The regulation of substrate protein affinity is intricately linked to its nucleotide-bound state. In the ATP-bound state, HSPA2 exhibits low substrate protein affinity, but upon ATP hydrolysis to ADP, it undergoes a conformational change, enhancing its affinity for substrate proteins. This dynamic process involves repeated cycles of ATP hydrolysis and nucleotide exchange, allowing for successive substrate binding and release. Beyond its general cellular functions, HSPA2 plays a crucial role in spermatogenesis and may contribute to spindle integrity maintenance during meiosis in male germ cells when associated with SHCBP1L. Notably, it interacts with FKBP6 and ZNF541, highlighting its involvement in various cellular pathways and protein interactions. Additionally, HSPA2 forms part of the CatSper complex and shows preferential binding to GTP-bound RABL2, further expanding its functional repertoire.

HSPA2; Heat shock-related 70 kDa protein 2; Heat shock 70 kDa protein 2

Greater than 90% as determined by reducing SDS-PAGE.

Supplied as a 0.22 μm filtered solution of 50 mM HEPES, 200 mM NaCl, 20% glycerol, 1 mM DTT, pH 7.5.

Shipping with dry ice