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H5147

Sigma-Aldrich

Monoclonal Anti-Heat Shock Protein 70 antibody produced in mouse

clone BRM-22, ascites fluid

Synonyme(s) :

HSP70 Antibody - Monoclonal Anti-Heat Shock Protein 70 antibody produced in mouse, Hsp70 Antibody

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

BRM-22, monoclonal

Poids mol.

antigen 70 kDa

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

Description générale

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.

Spécificité

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.

Immunogène

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)
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.

Actions biochimiques/physiologiques

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.

Autres remarques

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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)
M P Mayer et al.
Cellular and molecular life sciences : CMLS, 62(6), 670-684 (2005-03-17)
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments
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
Anne Lyytinen et al.
PloS one, 7(2), e31446-e31446 (2012-02-10)
Individuals of widely spread species are expected to show local adaption in temperature tolerance as they encounter a range of thermal conditions. We tracked thermal adaptations of the Colorado potato beetle (Leptinotarsa decemlineata) that invaded Europe within the last 100

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