Rabbit anti-Human HSPA1A  Antibody | anti-HSPA1A  antibody

Rabbit anti Human HSPA1A  Monoclonal Antibody

Cat. Num. AAA2544275

• Gene Names: HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70.1; HSP70-1A; HEL-S-103
• Reactivity: Human
• Applications: Immunohistochemistry, Immunofluorescence, ELISA
• Purity: Affinity purification
• Synonyms: HSPA1A ; Rabbit anti Human HSPA1A Monoclonal Antibody; HEL-S-103; HSP70-1; HSP70-1A; HSP70I; HSP72; HSPA1; anti-HSPA1A antibody

• Host: Rabbit
• Reactivity: Human
• Isotype: IgG
• Purity/Purification: Affinity purification
• Form/Format: 0.2 um filtered solution in PBS

• Applicable Applications for anti-HSPA1A antibody: Immunohistochemistry (IHC), Immunofluorescence (IF), ELISA
• Application Notes: IHC 1:500-1:2000, IF 1:20-1:100
• Note: Centrifuge before opening to ensure complete recovery of vial contents.
• Immunogen: Fusion protein of human HSPA1A
• Preparation and Storage: Store at -20°C, Avoid freeze / thaw cycles

Immunohistochemistry (IHC)

(Immunohistochemistry of paraffin-embedded human hepatoma tissue slide using HSPA1A Monoclonal Antibody at dilution of 1:1000.)

Immunofluorescence (IF)

(Immunofluorescent analysis of Hela cells using HSPA1A Monoclonal Antibody at dilution of 1:60)

Related Product Information for anti-HSPA1A  antibody

HSPA1A is a member of the Hsp7 protein family. The 7 kilodalton heat shock proteins (Hsp7s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates presentation of antigen peptide to T cells. Molecular chaperones of the Hsp7 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp7 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp7 chaperones use the same mechanism of ATP-driven polypeptide binding and release. 

NCBI and Uniprot Product Information

• NCBI GI #: 194248072
• NCBI GeneID: 3303
• NCBI GenBank Nucleotide #: NM_005345.5
• 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
• UniProt Gene Name: HSPA1A
• UniProt Synonym Gene Names: HSPA1; HSX70; HSP70.1
• UniProt Entry Name: HS71A_HUMAN

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: 6p21.3

Cellular Component: cell-cell adherens junction; centriole; cytoplasm; cytosol; focal adhesion; inclusion body; 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

Biological Process: activation of NF-kappaB transcription factor; ATP metabolic process; negative regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; 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