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Recombinant human HSPA6 protein

Cat:P06598

Summary:

【Derived From】: E.coli
【Endotoxin】: Not measured
【Amino Acid】: 294-644aa
【Purity】: ≥85% by SDS-PAGE.
【Name】: HSPA6
【Full Name】: heat shock 70kDa protein 6 (HSP70B')
【Uniprot】: P17066
【Gene ID】: 3310
【Species Reactivity】: Human (Pig)
【Mol Mass】: 38.8kDa
【Application】: Immunology research
【Purification】: NI-NTA affinity purification
【Bioactive】: N0
【Tag】: With a 6×His tag at the N/C-terminus.
【Concentration】: 1mg/ml by SDS-PAGE.

Store:

【Reconstitution】: Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.)
【Storage】: Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks, stored at < -20℃ for 1 year.
【Formulation】: Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0.

Background:

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).

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