H5147
Monoclonal Anti-Heat Shock Protein 70 antibody produced in mouse
clone BRM-22, ascites fluid
Synonym(s):
HSP70 Antibody - Monoclonal Anti-Heat Shock Protein 70 antibody produced in mouse, Hsp70 Antibody
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About This Item
Recommended Products
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
BRM-22, monoclonal
mol wt
antigen 70 kDa
species reactivity
bovine, chicken, guinea pig, plant, Drosophila, rat, human, nematode, rabbit, hamster
technique(s)
electron microscopy: suitable
immunohistochemistry (frozen sections): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1:5,000 using bovine brain extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HSPA1A(3303) , HSPA1B(3304)
rat ... Hspa1a(24472) , Hspa1b(294254)
General description
A variety of environmental disruptions, such as a sudden increase in temperature, induce cells to rapidly synthesize a group of polypeptides known as heat shock (stress) proteins. Eukaryotic cells contain a multigene family that encodes several closely related 70 kD stress proteins (the HSP70 family) that differ in their intracellular location and regulation.These include four proteins: the constitutive (or cognate) HSP73, the stress-inducible HSP72 and the glucose regulated proteins grp78 (or BiP) and grp75.
Monoclonal Anti-Heat Shock Protein 70 (mouse IgG1 isotype) is derived from the BRM-22 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with purified bovine brain HSP70. Heat shock protein family A (Hsp70) member 1A (HSPA1A), is encoded by the gene mapped to human chromosome 6p21.33. It is widely expressed in all tissues. The encoded protein is characterized with an N-terminal ATPase domain of 45 kDa and a C-terminal substrate binding domain of 25 kDa.
Specificity
By immunoblotting, the antibody localizes both the constitutive (HSP73) and inducible (HSP72) forms of HSP70. The antibody recognizes HSP70 from brain and other tissue. Immunofluorescent staining demonstrates a rapid and reversible accumulation of the HSP70 protein within the nucleus of heat-shocked (42 °C, 1 hour) human fibroblasts.
Immunogen
HSP70 isolated from bovine brain
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunoprecipitation (1 paper)
Western Blotting (4 papers)
Immunoprecipitation (1 paper)
Western Blotting (4 papers)
Monoclonal Anti-Heat Shock Protein 70 antibody produced in mouse has been used in:
- enzyme-linked immunosorbent assay (ELISA)
- immunoblot
- dot blot
- immunocytochemistry
The antibody titer of at least 1:5,000 was determined by immunoblotting using bovine brain extract.
Biochem/physiol Actions
Members of the HSP70 family play a major role in the folding, unfolding and translocation of polypeptides as well as in the assembly and disassembly of oligomeric protein complexes. In addition, several possible roles have been attributed to the HSP70 family of proteins, in the immune response. It has been shown that alcoholic liver disease is associated with intracytoplasmic accumulation of HSP70. HSP72 was found to increase dramatically in the brains of Alzheimer′s disease patient, and was localized exclusively in neuritic plaques and neurofibrillary tangles. HSP70 concentrates in nuclei during heat shock and returns to the cytoplasm when the shock is removed.
Other Notes
This product can be found as purified product that was produced using cell culture hybridoma product.
SAB4200714 Anti-Heat Shock Protein 70 (HSP70) antibody, Mouse monoclonal
clone BRM-22, purified from hybridoma cell culture
SAB4200714 Anti-Heat Shock Protein 70 (HSP70) antibody, Mouse monoclonal
clone BRM-22, purified from hybridoma cell culture
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Pricing
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions
Brocchieri L, et al.
BMC Evolutionary Biology, 8(1), 1-20 (2008)
Mohan E Tulapurkar et al.
PloS one, 10(2), e0118010-e0118010 (2015-02-07)
Sepsis, a devastating and often lethal complication of severe infection, is characterized by fever and dysregulated inflammation. While infections activate the inflammatory response in part through Toll-like receptors (TLRs), fever can partially activate the heat shock response with generation of
Fang Xie et al.
Cell stress & chaperones, 21(5), 907-914 (2016-07-21)
Although accumulating evidence indicates that heat shock protein 70 (HSP70) could be secreted into plasma and its levels have been found to have an ambiguous association with atherosclerosis, our knowledge for the exact role of circulating HSP70 in the development
Ling Wang et al.
PloS one, 9(10), e109465-e109465 (2014-10-21)
The soybean pod borer (Leguminivora glycinivorella Matsumura) successfully survives the winter because of its high expression of 70-kDa heat shock proteins (HSP70s) during its overwintering diapause. The amount of HSP70s is different under different environmental stresses. In this study, inducible
Bacterial lipopolysaccharide augments febrile-range hyperthermia-induced heat shock protein 70 expression and extracellular release in human THP1 cells
Tulapurkar ME, et al.
Testing, 10(2), e0118010-e0118010 (2015)
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