Abcam, ab47455, Anti-Hsp70 antibody [C92F3A-5]

Size: 100µL
Mouse Monoclonal Hsp70 antibody. Suitable for Flow Cyt, WB, IHC-P and reacts with Human, Mouse, Rat samples. Cited in 47 publications. Immunogen corresponding to Recombinant Fragment Protein within Human HSPA1A aa 400-550.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:C92F3A-5,
Isotype:IgG1,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, 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 aa 400-550. The exact immunogen used to generate this antibody is proprietary information.P0DMV8,
Epitope:The mapped epitope is in the region of amino acid residues 436-503.,
Specificity:Detects a 70kDa protein corresponding to the molecular mass of Hsp70 of SDS PAGE immunoblots. There is no cross-reactivity to Hsc70 (Hsp73).

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Storage buffer-Preservative: 0.1% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 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.