antibody

HSP70 Monoclonal Antibody

MBS126127

0.05 mL

230 USD

monoclonal

mouse

nonconjugated

human, mouse, rat

Antibody

HSP70 Monoclonal Antibody

HSP70

HSP70: HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HSPA1A

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; heat shock 70kD protein 1B; heat shock 70 kDa protein 1/2; heat shock 70kDa protein 1B; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSPA1A

HSPA1B; HSPA1A; HSP70-2; HSP70-1B; HSPA1; HSX70; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSP71_HUMAN

Monoclonal

IgG

Mouse

Human, Mouse, Rat

641

Affinity Purification

Store at -20 degree C (regular) or -80 degree C (long term). Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Western Blot (WB)

WB: 1:2000 - 1:5000

Species: Human. Route: Synthetic Peptide. Gene ID: 3303. Category: Primary Antibody

Immunogen: A synthetic peptide of human HSP70. Calculated Molecular Weight: 70kDa

Monoclonal

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

147744565

P08107.5

P08107

641

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: Heat shock protein; Motility/polarity/chemotaxis; Chaperone. Chromosomal Location of Human Ortholog: 6p21.3. Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; ribonucleoprotein complex; cytosol; nucleoplasm; centriole; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; vesicle; ubiquitin ligase complex. Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; ubiquitin protein ligase binding; heat shock protein binding; double-stranded RNA binding; unfolded protein binding; ATPase activity; 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; negative regulation of protein ubiquitination; protein refolding; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis

0.05 mL

230 USD

0.1 mL

305

0.2 mL

460