Chicken Hsp70 Polyclonal Antibody | anti-HSPA1A antibody
Hsp70 Antibody: PerCP
Western Blot (WB)
(Western blot analysis of Human Cervical cancer cell line (HeLa) lysate showing detection of HSP70 protein using Chicken Anti-HSP70 Polyclonal Antibody (SPC-178). Load: 15 ugprotein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Chicken Anti-HSP70 Polyclonal Antibody (SPC-178) at 1:1000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.)
Scientific Background: Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (5). The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.
NCBI and Uniprot Product Information
HSPA1B; HSP70-1/HSP70-2; HSP70.1/HSP70.2
NCBI Description
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]
Uniprot Description
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; Chaperone; Motility/polarity/chemotaxis
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; 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; double-stranded RNA binding; unfolded protein 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; gene expression; protein refolding; negative regulation of protein ubiquitination; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis
