HSPA2
HSPA2 (heat shock protein family A (Hsp70) member 2, also called heat shock-related 70 kDa protein 2) is a member of the heat shock protein 70 family. It acts as a molecular chaperone in protein quality control and plays a role in spermatogenesis. Browse Assay Genie's current range of HSPA2 research reagents below, or read on for the biology behind the target.
HSPA2 is a molecular chaperone implicated in a wide variety of cellular processes. These include protection of the proteome from stress, folding and transport of newly synthesised polypeptides, activation of proteolysis of misfolded proteins, and the formation and dissociation of protein complexes. It has a pivotal role in the protein quality control system, ensuring correct folding, re-folding of misfolded proteins and control of the targeting of proteins for subsequent degradation.
The chaperone works through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. Its affinity for polypeptides depends on its nucleotide-bound state. In the ATP-bound form it has low affinity for substrate proteins. After ATP is hydrolysed to ADP, a conformational change increases substrate affinity. Repeated rounds of hydrolysis and nucleotide exchange permit cycles of substrate binding and release. Consistent with this, NCBI Gene annotates the HSPA2 protein with unfolded protein binding and enzyme binding activity, and with involvement in protein refolding and negative regulation of inclusion body assembly. It is located in the cytosol and, according to UniProt, associates with the spindle in the cytoskeleton.
HSPA2 also plays a role in spermatogenesis. In association with SHCBP1L, it may participate in maintaining spindle integrity during meiosis in male germ cells. The HSPA2 gene is a member of the HGNC group of heat shock 70 kDa proteins, and the protein belongs to the heat shock protein 70 family. Earlier names for the gene were heat shock 70kD protein 2 and heat shock 70kDa protein 2. Mouse and rat orthologs are both named Hspa2.
HSPA2 helps ensure correct folding, re-folding of misfolded proteins and targeting of proteins for degradation, making it a useful subject for proteostasis studies.
Its substrate affinity changes with ATP binding, hydrolysis and ADP release, mediated by co-chaperones, which makes it a model for Hsp70 mechanism studies.
HSPA2 plays a role in spermatogenesis and may help maintain spindle integrity during male germ cell meiosis with SHCBP1L.
As a chaperone implicated in protecting the proteome from stress, HSPA2 is relevant to studies of how cells handle misfolded proteins.
HSPA2 is a molecular chaperone that supports protein quality control. It helps fold newly synthesised polypeptides, re-fold misfolded proteins and direct proteins towards degradation, using cycles of ATP binding, hydrolysis and ADP release. It also plays a role in spermatogenesis.
UniProt lists the protein as heat shock-related 70 kDa protein 2, and HGNC names the gene heat shock protein family A (Hsp70) member 2. Previous names were heat shock 70kD protein 2 and heat shock 70kDa protein 2. No alternative gene symbols are recorded.
Yes. Mouse and rat both have an ortholog named Hspa2, so the target can be studied in common rodent models. Check the datasheet of any product for its validated reactivity.
Other Hsp70 family chaperones that work in protein folding and quality control, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P54652; product specifications from Assay Genie datasheets.