anti-HSP70, mAb (16A12)

CHF 315.00
In stock
YIF-LF-MA0101100 µlCHF 315.00
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Product Details
Synonyms HSPA1; HSPA1A; HSP70.1/HSP70.2; HSP70-1/HSP70-2; Heat Shock 70 kDa Protein 1/2; Heat Shock 70 kDa Protein 1A/1B
Product Type Monoclonal Antibody
Clone 16A12
Isotype Mouse IgG2b λ
Immunogen/Antigen Recombinant human HSP70 protein purified E. coli.

Western Blot (1:2,000)
Immunoprecipitation (1~2 μl)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG2b Isotype Control

Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

The Heat shock protein 70 (HSP70) family was found in many intracellular compartments. Members of this protein occur in chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variety of biological stresses, including heat stress, in every organism. HSP70 serves a variety of roles: 1) It acts as molecular chaperones facilitating the assembly of multi-protein complexes, 2) It participates in the translocation of polypeptides across cell membranes and to the nucleus 3) It aids in the proper folding of nascent polypeptide chains. HSP70 is mitochondrial import machinery and plays key roles in the cytosolic endoplasmic reticulum. Recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response. In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.

Product References

1) Multhoff G, et al. (2002) Int J Hyperthermia. 18(6):576-85. (General)
2) Martin J, et al.(1992) Science 258(5084):995-8. (General)
3) Hatayama T, et al.(1992) J Biochem 111(4):484-90. (General)
4) Haas IG. (1995) FEBS Lett. (1995) 369(1):72-5. (General)

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