Abcam, ab113187, Recombinant mouse Hsp70 protein

Size: 50µg
Recombinant mouse Hsp70 protein is a Mouse Full Length protein, in the 1 to 641 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:>85% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:FuncS, SDS-PAGE, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:ATPase activity assay (positive) but there is not quantification of activity,
Accession:Q61696,
Animal free:No,
Carrier free:No,
Species:Mouse,
Storage buffer:Constituents: PBS, 0.15% Glutathione

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.
Hsp70 also known as Heat Shock Protein 70 or HSPA1B is a molecular chaperone with a mass of approximately 70 kDa. It plays a mechanical role by assisting in the proper folding of nascent polypeptide chains and the refolding of misfolded proteins. Researchers often detect Hsp70 using Western blot and immunohistochemistry (IHC) techniques. Hsp70 is widely expressed in many tissues particularly during stress conditions like heat shock where its expression level increases significantly.
Biological function summary
Hsp70 operates by stabilizing intermediate states of folding proteins preventing aggregation and facilitating the correct folding process. It often forms a complex with co-chaperones such as Hsp40 and nucleotide exchange factors. This complex is essential for the protein's activity and function. Additionally Hsp70 participates in protein degradation pathways by guiding misfolded proteins to the proteasome for degradation maintaining cellular homeostasis.
Pathways
This molecular chaperone plays significant roles in the heat shock response and unfolded protein response pathways. Hsp70 interacts closely with proteins such as Hsp90 and co-chaperones which together help protect cells from stress-induced damage. The protein also participates in the JAK/STAT signaling pathway influencing cell proliferation and apoptosis. These interactions suggest an integral role in maintaining cellular integrity during stress conditions.
Overexpression of Hsp70 has been associated with various cancers and neurodegenerative diseases. In cancer Hsp70 helps tumor cells survive the hostile tumor microenvironment partly by interacting with anti-apoptotic proteins such as Bcl-2. In neurodegenerative disorders such as Alzheimer's disease Hsp70 associates with amyloid-beta peptides potentially mitigating their aggregation toxicity. These interactions highlight Hsp70's importance in both protective and pathological cellular processes.