Anti-HSPA2, clone 4A4

0.5mg/ml if reconstituted with 0.2ml sterile DI water. HSPA2 (heat shock 70kDa protein 2) is also known as HEAT-SHOCK PROTEIN, 70-KD, 2, HSP70-2, HEAT-SHOCK PROTEIN, 70-KD, 3 or HSP70-3. Analysis of the sequence indicated that HSPA2 is the human homolog of the murine Hsp70-2 gene, with 91.7% identity in the nucleotide coding sequence and 98.2% in the corresponding amino acid sequence. HSPA2 has less amino acid homology to the other members of the human HSP70 gene family. HSPA2 is constitutively expressed in most tissues, with very high levels in testis and skeletal muscle. The HSPA2 gene is located on chromosome 14q22-q24. Immunohistochemical analysis detected weak expression of HSPA2 in spermatocytes and stronger expression in spermatids and in the tail of mature sperm. HSPA2 may be critical to sperm maturation through its role as a protein chaperone. Protein function: 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). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells. [The UniProt Consortium]