Abcam, ab92433, Recombinant human HSPA2 protein

Size: 50µg
Recombinant human HSPA2 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:FuncS, WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:ATPase activity: Positive,
Accession:P54652,
Animal free:No,
Carrier free:No,
Species:Human

Product details:
Endotoxin: >500 EU/mg as determined by LAL gel clot assay

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HSPA2 also known as Heat Shock Protein Family A (Hsp70) Member 2 serves as a molecular chaperone. It assists in the folding of nascent polypeptides and protection of proteins under stress. The protein has a mass of approximately 70 kilodaltons (kDa). You can find HSPA2 expressed in various tissues including the testes which suggests a role in sperm maturation and fertilization. Its expression is also notable in other tissues under stress conditions.
Biological function summary
This chaperone protein plays a role in spermatogenesis by ensuring the proper folding and functioning of sperm proteins. HSPA2 is not part of a larger protein complex but acts in coordination with co-chaperones to exert its functions. Its activities contribute to sperm development and viability impacting male fertility. HSPA2 also provides cellular protection in response to different stress stimuli such as increased temperature and toxic substances.
Pathways
HSPA2 participates in the protein folding pathway and stress response pathway. Its precise chaperone action is important for maintaining protein homeostasis; thereby it influences cellular health. In the stress response pathway HSPA2 interacts with other heat shock proteins such as HSP90AA1 coordinating to mitigate damage from cytotoxic stressors. This interaction helps to stabilize and refold misfolded proteins while facilitating their repair or degradation.
HSPA2's role in fertility and cell protection connects it to infertility and cancer. Research indicates abnormalities in HSPA2 function are associated with male infertility due to improper protein folding critical for sperm function. Similarly alterations in HSPA2 expression link to cancer progression where its regulation could impact cell survival and proliferation. Within these diseases HSPA2 interacts with proteins like tumor suppressors p53 highlighting its complex involvement in cellular responses.