Rabbit Anti-HSPA1B Recombinant Antibody (A295) (CBMAB-AP10556LY)

Heat Shock Protein Family A (Hsp70) Member 1B

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 1B; Heat Shock 70kDa Protein 1B; Heat Shock 70 KDa Protein 2; Heat Shock 70kD Protein 1B; HSP70-2; HSP70.2; Heat Shock 70 KDa Protein 1A/1B;

A10897

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: GO_Central
Chaperone cofactor-dependent protein refolding Source: GO_Central
mRNA catabolic process Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell death Source: ParkinsonsUK-UCL
Negative regulation of cell growth Source: UniProtKB
Negative regulation of cell population proliferation Source: UniProtKB
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 protein ubiquitination 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: GO_Central
Positive regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Protein refolding Source: UniProtKB
Protein stabilization Source: UniProtKB
Regulation of mitotic spindle assembly Source: UniProtKB
Regulation of protein ubiquitination Source: BHF-UCL
Vesicle-mediated transport Source: GO_Central

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

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.