HSPB1 antibody - C-terminal region (ARP30177_T100)
- Known as:
- HSPB1 (anti-) - C-terminal region (ARP30177_T100)
- Catalog number:
- arp30177_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- HSPB1 antibody - C-terminal region (ARP30177_T100)
Related genes to: HSPB1 antibody - C-terminal region (ARP30177_T100)
- Gene:
- HSPB1 NIH gene
- Name:
- heat shock protein family B (small) member 1
- Previous symbol:
- -
- Synonyms:
- HSP27, HSP28, Hs.76067, Hsp25, CMT2F
- Chromosome:
- 7q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-09
- Date modifiied:
- 2019-04-23
- Gene:
- ODF1 NIH gene
- Name:
- outer dense fiber of sperm tails 1
- Previous symbol:
- -
- Synonyms:
- ODFPG, ODF27, RT7, HSPB10, CT133
- Chromosome:
- 8q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-10-25
- Date modifiied:
- 2018-04-16
Related products to: HSPB1 antibody - C-terminal region (ARP30177_T100)
Related articles to: HSPB1 antibody - C-terminal region (ARP30177_T100)
- Small heat shock proteins (sHsps) belong to molecular chaperones, which protect prokaryotic and eukaryotic cells against deleterious effects, of stress. sHsps prevent stress induced, irreversible aggregation of damaged proteins and facilitate renaturation of bound substrates cooperating with other molecular chaperones. This review summarizes recent studies focused mainly on the involvement of sHsps in diseases related to protein aggregation. sHsps are often a component of protein aggregates forming during progress of neurodegenerative disorders. Mutation in sHsps genes have been identified, which are responsible for development of cataract, desmin related myopathy and neuropathies. sHsps protect cells against oxidative stress resulting from ischemia/reperfusion during heart or brain stroke. Several studies indicate that sHsp participate in regulation of apoptosis and are involved in cancerogenesis. Uncovering the sHsps role in diseases enable to develop new therapeutic strategies. - Source: PubMed
Laskowska Ewa - Nine proteins have been assigned to date to the superfamily of mammalian small heat shock proteins (sHsps): Hsp27 (HspB1, Hsp25), myotonic dystrophy protein kinase-binding protein (MKBP) (HspB2), HspB3, alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), Hsp20 (p20, HspB6), cardiovascular heat shock protein (cvHsp [HspB7]), Hsp22 (HspB8), and HspB9. The most pronounced structural feature of sHsps is the alpha-crystallin domain, a conserved stretch of approximately 80 amino acid residues in the C-terminal half of the molecule. Using the alpha-crystallin domain of human Hsp27 as query in a BLAST search, we found sequence similarity with another mammalian protein, the sperm outer dense fiber protein (ODFP). ODFP occurs exclusively in the axoneme of sperm cells. Multiple alignment of human ODFP with the other human sHsps reveals that the primary structure of ODFP fits into the sequence pattern that is typical for this protein superfamily: alpha-crystallin domain (conserved), N-terminal domain (less conserved), central region (variable), and C-terminal tails (variable). In a phylogenetic analysis of 167 proteins of the sHsp superfamily, using Bayesian inference, mammalian ODFPs form a clade and are nested within previously identified sHsps, some of which have been implicated in cytoskeletal functions. Both the multiple alignment and the phylogeny suggest that ODFP is the 10th member of the superfamily of mammalian sHsps, and we propose to name it HspB10 in analogy with the other sHsps. The C-terminal tail of HspB10 has a remarkable low-complexity structure consisting of 10 repeats of the motif C-X-P. A BLAST search using the C-terminal tail as query revealed similarity with sequence elements in a number of Drosophila male sperm proteins, and mammalian type I keratins and cornifin-alpha. Taken together, the following findings suggest a specialized role of HspB10 in cytoskeleton: (1) the exclusive location in sperm cell tails, (2) the phylogenetic relationship with sHsps implicated in cytoskeletal functions, and (3) the partial similarity with cytoskeletal proteins. - Source: PubMed
Fontaine Jean-MarcRest Joshua SWelsh Michael JBenndorf Rainer - To obtain an inventory of all human genes that code for alpha-crystallin-related small heat shock proteins (sHsps), the databases available from the public International Human Genome Sequencing Consortium (IHGSC) and the private Celera human genome project were exhaustively searched. Using the human Hsp27 protein sequence as a query in the protein databases, which are derived from the predicted genes in the human genome, 10 sHsp-like proteins were retrieved, including Hsp27 itself. Repeating the search procedure with all 10 proteins and with a variety of more distantly related animal sHsps, no further human sHsps were detected, as was the case when searches were performed at deoxyribonucleic acid level. The 10 retrieved proteins comprised the 9 earlier recognized human sHsps (Hsp27/HspB1, HspB2, HspB3, alphaA-crystallin/HspB4, alphaB-crystallin/HspB5, Hsp20/HspB6, cvHsp/HspB7, H11/HspB8, and HspB9) and a sperm tail protein known since 1993 as outer dense fiber protein 1 (ODF1). Although this latter protein probably serves a structural role and has a high cysteine content (14%), it clearly contains an alpha-crystallin domain that is characteristic for sHsps. ODF1 can as such be designated as HspB10. The expression of all 10 human sHsp genes was confirmed by expressed sequence tag (EST) searches. For Hsp27/HspB1, 2 retropseudogenes were detected. The HspB1-10 genes are dispersed over 9 chromosomes, reflecting their ancient origin. Two of the genes (HspB3 and HspB9) are intronless, and the others have 1 or 2 introns at various positions. The transcripts of several sHsp genes, notably HspB7, display low levels of alternative splicing, as supported by EST evidence, which may result in minor amounts of isoforms at the protein level. - Source: PubMed
Kappé GuidoFranck ErikVerschuure PaulineBoelens Wilbert CLeunissen Jack A Mde Jong Wilfried W