Abcam, ab5442, Anti-Hsp70 antibody [2A4]

Size: 50µL
Mouse Monoclonal Hsp70 antibody. Suitable for IP, Flow Cyt, WB, IHC-P, ICC/IF and reacts with Human, Mouse, Saccharomyces cerevisiae samples. Cited in 23 publications. Immunogen corresponding to Recombinant Fragment Protein within Human HSPA1A.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:2A4,
Isotype:IgM,
Carrier free:No,
Reacts with:Mouse, Human, Saccharomyces cerevisiae,
Applications:IHC-P, ICC/IF, IP, WB, Flow CytSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human HSPA1A. The exact immunogen used to generate this antibody is proprietary information.P0DMV8,
Epitope:Epitope mapping with a panel of Hsp 70 deletion mutants suggests that the epitope recognized is located between amino acids 437-479 of human Hsp 70.,
Specificity:ab5442 detects several members of the heat shock protein 70 kDa (Hsp 70) gene family including Hsp 70, Hsc 70 and, following heat shock, Hsp 72 from yeast, Drosophila, fish, mouse, avian, amphibian and human samples. Immunofluorescence staining of Hsp 70 in heat shocked HeLa cells with ab5442 results in cytoplasmic staining.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-Preservative: 0.05% Sodium azideConstituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°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.