antibody

Hsp70 antibody (clone 4E7)

MBS200049

0.05 mL

240 USD

monoclonal

mouse

nonconjugated

4.00E+07

western blot, ELISA, immunohistochemistry, enzyme immunoassay

Antibody

Hsp70 antibody (clone 4E7)

Hsp70

HSPA1A; HSPA1; HSPA1B; HSP70; HSP70.1; HSP70-1/HSP70-2; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1; heat shock 70kDa protein 1A

heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1A/1B; heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; heat shock 70 kDa protein 1/2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70kDa protein 1A; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2

Hsp70

HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HEL-S-103; HSPA1; HSX70; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSP71_HUMAN

Monoclonal

IgG1, k

4.00E+07

Mouse

Human

641

By protein-G affinity chromatography

Liquid. Supplied in Phosphate-Buffered Saline (pH 7.4) with 0.1% Sodium Azide.

1mg/ml

Can be stored at 4 degree C. For long term storage, aliquot and store at -20 degree C. Avoid repeated freezing and thawing cycles.

ELISA (EIA), Western Blot (WB) (Cell lysate), Immunohistochemistry (IHC)

The antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:500 ~ 1:2,000 and immunohistochemistry analysis is 1:100~200. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:100.

Antigen Species: Human. Clone: Anti-human Hsp70 mAb, clone 4E7, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human Hsp70 protein. Immunogen: Recombinant human Hsp70 (1-641aa) purified from E Coli

Heat Shock Proteins

Hsp70 is a human heat shock protein. Hsp70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. Hsp70 can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc. ), and the chaperone function of hsp70 is required for protection against stress-induced apoptosis.

Lewis MJ, et al., (1985) EMBO J 4:3137-3143 Gething M-J, et al., (1992) Nature 355:33-45 Dick D.M, et al., (2000) Mol Cell Biol 20(19):7146-7159

194248072

NP_005336

NM_005345.5

63,937 Da

AUF1 (hnRNP D0) Destabilizes MRNA Pathway (187212); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Apoptosis Modulation By HSP70 Pathway (198877); Attenuation Phase Pathway (1127556); Cellular Response To Heat Stress Pathway (1127553); Cellular Responses To Stress Pathway (645258); Direct P53 Effectors Pathway (137939); Disease Pathway (530764); Endocytosis Pathway (102279)

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Protein type: Motility/polarity/chemotaxis; Chaperone; Heat shock protein. Chromosomal Location of Human Ortholog: 6p21.3. Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; ribonucleoprotein complex; cytosol; centriole; nucleoplasm; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; ubiquitin ligase complex; vesicle. Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; ATPase activity; unfolded protein binding; double-stranded RNA binding; protein N-terminus binding; ATPase activity, coupled; ATP binding. Biological Process: negative regulation of cell proliferation; entry of virus into host cell; protein stabilization; positive regulation of erythrocyte differentiation; mRNA catabolic process; protein refolding; negative regulation of protein ubiquitination; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis

0.05 mL

240 USD

0.1 mL

315