antibody

HSP70/HSP72 polyclonal antibody

MBS565175

0.05 mg

240 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat, cow

western blot, immunoprecipitation

Antibody

HSP70/HSP72 polyclonal antibody

[HSP70/HSP72]

[Hsp70; HspA1A; Heat shock protein 70; HspA1B; Hsp72]

[heat shock 70 kDa protein 1A; Heat shock 70 kDa protein 1A; heat shock 70 kDa protein 1A; heat shock protein family A (Hsp70) member 1A; Heat shock 70 kDa protein 1; HSP70-1]

[HSP70/HSP72]

[HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70.1; HSP70-1A; HEL-S-103; HSPA1; HSX70; HSP70.1]

HS71A_HUMAN

Polyclonal

Rabbit

Human, Mouse, Rat, Beluga, Bovine, Dog, Hamster, Monkey, Porcine, Sheep

641

Recognizes human, mouse, rat, bovine, beluga, dog, hamster, monkey, pig and sheep HSP70 (HSP72). Detects a band of ~70kDa by Western blot.

Protein A affinity purified.

Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.

Long term storage: -20 degree C. Avoid freeze/thaw cycles. Shipping: shipped on Blue ice.

Immunoprecipitation (IP), Western Blot (WB)

Western Blot (1:1,000, ECL). Suggested dilutions/conditions may not be available for all applications. Detects a band of ~70kDa by Western blot. Optimal conditions must be determined individually for each application.

Western Blot (WB)

Immunogen: Synthetic peptide corresponding to a portion of human Hsp70.

Protein Synthesis & Folding

The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

194248072

NP_005336.3

NM_005345

P08107

63,937 Da

AUF1 (hnRNP D0) Binds And Destabilizes MRNA Pathway (1269726); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Apoptosis Modulation By HSP70 Pathway (198877); Attenuation Phase Pathway (1270424); Cellular Response To Heat Stress Pathway (1270421); Cellular Responses To Stress Pathway (1270414); Disease Pathway (1268854); Endocytosis Pathway (102279); Endocytosis Pathway (102181)

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: Heat shock protein; Motility/polarity/chemotaxis; Chaperone. Chromosomal Location of Human Ortholog: 6p21.3. Cellular Component: centriole; cytoplasm; cytosol; focal adhesion; inclusion body; mitochondrion; nucleoplasm; perinuclear region of cytoplasm; ubiquitin ligase complex. Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; histone deacetylase binding; protein binding; receptor binding; ubiquitin protein ligase binding; unfolded protein binding; viral receptor activity. Biological Process: activation of NF-kappaB transcription factor; ATP metabolic process; entry of virus into host cell; gene expression; negative regulation of protein ubiquitination; positive regulation of interleukin-8 production; protein refolding; protein stabilization; regulation of mRNA stability; regulation of protein ubiquitination

0.05 mg

240 USD

0.2 mg

475