Rabbit anti-Most Hsp70 Polyclonal Antibody | anti-HSPA1A antibody

Hsp70

Cat. Num. AAA500058

• Gene Names: HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70.1; HSP70-1A; HEL-S-103
• Reactivity: Most
• Applications: Western Blot
• Purity: Affinity Purified from Pooled Serum
• Synonyms: Hsp70; Polyclonal Antibody; anti-HSPA1A antibody

• Host: Rabbit
• Reactivity: Most
• Clonality: Polyclonal
• Purity/Purification: Affinity Purified from Pooled Serum
• Form/Format: 100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol.
• Sequence Length: 641

• Applicable Applications for anti-HSPA1A antibody: Western Blot (WB)
• Application Notes: WB: 1:1,000
• Immunogen: Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr153 conjugated to KLH; Immunogen Species
• Purification Note: The antibody is prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.
• Preparation and Storage: Store at -20 degree C

Related Product Information for anti-HSPA1A antibody

The Hsp70 family of heat shock proteins are considered stress-induced survival proteins as they are expressed when exposed to factors such as heat, hypoxia, oxidative stress, altered pH or by underlying factors like cancer (Daugaard et al. 2007). Hsp70 proteins are able to bind hydrophobic residues on misfolded proteins, thereby preventing their aggregation and thus serving important roles in protein homeostasis. To date, there have been 8 members of the family identified; the majority of which are found in the cytosol though some have specific function in tissue or an organelle (Murphy, 2013). Hsp70 has also been shown to play a major role in cancer; from tumor grade to prognosis, as well as chemotherapeutic drug resistance (Ciocca et al, 2005). There have been several phospho-serine and threonine sites identified within Hsp70, the role of each one has yet to be determined.

Product Categories/Family for anti-HSPA1A antibody

Signal Transduction

NCBI and Uniprot Product Information

• NCBI GI #: 194248072
• NCBI GeneID: 3303
• NCBI Accession #: NP_005336.3
• NCBI GenBank Nucleotide #: NM_005345.5
• UniProt Accession #: P0DMV8; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0; B4E3B6
• Molecular Weight: ~70 kDA
• NCBI Official Full Name: heat shock 70 kDa protein 1A
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 1A
• NCBI Official Symbol: HSPA1A
• NCBI Official Synonym Symbols: HSP72; HSPA1; HSP70I; HSP70-1; HSP70.1; HSP70-1A; HEL-S-103
• NCBI Protein Information: heat shock 70 kDa protein 1A
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: HSPA1A
• UniProt Synonym Gene Names: HSP70.1

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: Chaperone; Heat shock protein; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 6p21.33

Cellular Component: centriole; centrosome; cytoplasm; cytosol; endoplasmic reticulum; extracellular region; focal adhesion; inclusion body; mitochondrion; nuclear speck; nucleoplasm; nucleus; perinuclear region of cytoplasm; protein complex; ribonucleoprotein complex; ubiquitin ligase complex; vesicle

Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; cadherin binding; denatured protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; histone deacetylase binding; protein binding; protein N-terminus binding; receptor binding; RNA binding; ubiquitin protein ligase binding; unfolded protein binding

Biological Process: activation of NF-kappaB transcription factor; ATP metabolic process; chaperone-mediated protein complex assembly; mRNA catabolic process; negative regulation of apoptosis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; neutrophil degranulation; positive regulation of interleukin-8 production; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein refolding; protein stabilization; regulation of mRNA stability; regulation of protein ubiquitination; response to unfolded protein