Recombinant Human Heat shock-related 70 kDa protein 2 (HSPA2)

Uniprot Id

P54652

Target Species

Human

Target Name

HSPA2

Target Full Name

Heat shock-related 70 kDa protein 2

Target 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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.

Target Subcellular Location

Cytoplasm, cytoskeleton, spindle.

Target Protein Families

Heat shock protein 70 family

Target Synonyms

70kDa; Hcp70.2; Heat shock 70 kDa protein 2; Heat shock protein 2; Heat shock protein 70.2; Heat shock related 70 kDa protein 2; Heat shock-related 70 kDa protein 2; Heat-shock protein, 70-KD, 2; Heat-shock protein, 70-KD, 3; HSP70 2; HSP70 3; Hsp70-2; HSP70-3; HSP70.2; HSP70A2; HSP72; HSP72_HUMAN; HSPA2; Hspt70; Hst70; MGC58299; MGC7795; MGC93458; OTTHUMP00000180664 ; Testis-specific heat shock protein-related

Target Background

Enables disordered domain specific binding activity; enzyme binding activity; and unfolded protein binding activity. Involved in negative regulation of inclusion body assembly and protein refolding. Located in cytosol.