Mouse Anti-HSPA1A Recombinant Antibody (A294) (CBMAB-AP10542LY)

Heat Shock Protein Family A (Hsp70) Member 1A

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]

Heat Shock Protein Family A (Hsp70) Member 1A; Heat Shock 70kDa Protein 1A; Heat Shock 70 KDa Protein 1; Heat Shock 70kD Protein 1A; HSP70-1; HSP70.1; HSPA1; HSP72; DnaK-Type Molecular Chaperone HSP70-1; Epididymis Secretory Protein Li 103; Heat Shock 70 KDa Protein 1A/1B;

A3921

ATP metabolic process Source: BHF-UCL
Cellular heat acclimation Source: UniProtKB
Cellular response to heat Source: UniProtKB
Cellular response to oxidative stress Source: ParkinsonsUK-UCL
Cellular response to steroid hormone stimulus Source: Reactome
Cellular response to unfolded protein Source: ParkinsonsUK-UCL
Chaperone cofactor-dependent protein refolding Source: GO_Central
Chaperone-mediated protein complex assembly Source: CAFA
Lysosomal transport Source: UniProtKB
mRNA catabolic process Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell death Source: UniProtKB
Negative regulation of cell growth Source: UniProtKB
Negative regulation of cell population proliferation Source: UniProtKB
Negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
Negative regulation of inclusion body assembly Source: UniProtKB
Negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
Negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
Negative regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
Positive regulation of endoribonuclease activity Source: ParkinsonsUK-UCL
Positive regulation of erythrocyte differentiation Source: UniProtKB
Positive regulation of gene expression Source: BHF-UCL
Positive regulation of interleukin-8 production Source: UniProtKB
Positive regulation of microtubule nucleation Source: UniProtKB
Positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
Positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: UniProtKB
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Positive regulation of RNA splicing Source: ParkinsonsUK-UCL
Positive regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Protein refolding Source: UniProtKB
Protein stabilization Source: CAFA
Regulation of mitotic spindle assembly Source: UniProtKB
Regulation of protein ubiquitination Source: BHF-UCL
Response to unfolded protein Source: UniProtKB
Vesicle-mediated transport Source: GO_Central

Nucleus; Centrosome; Cytoplasm; Secreted. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

In certain aggressive cases of activated B cell-like diffuse large B-cell lymphoma (ABC-DLBCL), plays a role in the cytoplasmic sequestration of misfolded N-terminal mutated PRDM1 proteins, promotes their association with SYNV1/HRD1 and degradation through the SYNV1-proteasome pathway. HSPA1A inhibition restores PRDM1 nuclear localization and transcriptional activity in lymphoma cell lines and suppresses growth in xenografts.

In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.