Recombinant Human HSPA6 protein (His tag N-Terminus)
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Recombinant Human HSPA6 protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
HSP70B', HSPA6, HSP70B, Heat shock 70 kDa protein 6, Heat shock 70 kDa protein B', Heat shock protein family A member 6
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human HSPA6 protein (His tag N-Terminus) (AB89366)
15% SDS-PAGE showing ab89366 at approximately 73.2kDa (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Heat Shock 70kDa Protein 6 acts as a molecular chaperone and facilitates the stabilization and proper folding of unfolded or misfolded proteins under stress conditions. It operates independently and does not appear to form part of a larger protein complex unlike some other heat shock proteins. HSPA6 helps cells recover from stress damage by transporting proteins across cellular membranes and aiding in the assembly of multiprotein complexes. This function is important for maintaining cellular integrity especially during and after exposure to stressors.
Pathways
Heat Shock 70kDa Protein 6 plays a role in the cellular stress response pathway. It synergistically collaborates with other heat shock proteins like HSP70 and HSP90 which are important in protein folding and protection against stress-induced damage. Additionally HSPA6 interacts within the unfolded protein response pathway a critical mechanism in the endoplasmic reticulum to manage stress. This relationship with other heat shock proteins and pathways allows cells to maintain function and resilience under stress.
Specifications
Form
Liquid
Additional notes
ab89366 is purified using conventional chromatography techniques.
General info
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).
Sequence similarities
Belongs to the heat shock protein 70 family.
Target data
Complementary Products
Product promise
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