Phospho-HSP90β (S226) Polyclonal Antibody, 100µg, (ATB-P0565)

Description

Background:

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.

Product datasheet:

Overview
Product Description	Phospho-HSP90β (S226) Polyclonal Antibody, 100µg, (ATB-P0565)
Image
Species Reactivities	Human,Mouse,Rat
Immunogen	Synthesized peptide derived from human HSP90β around the phosphorylation site of S226.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. Down-regulation of heat shock protein HSP90ab1 in radiation-damaged lung cells other than mast cells. Haase MG, et al. J Histochem Cytochem, 2014 May. PMID 24670792
2. Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. Hunter MC, et al. PLoS One, 2014. PMID 24466266 Free PMC Article
3. Heat shock protein-90-beta facilitates enterovirus 71 viral particles assembly. Wang RY, et al. Virology, 2013 Sep 1. PMID 23711381
4. Heat shock protein 90 (Hsp90) inhibition targets canonical TGF-β signalling to prevent fibrosis. Tomcik M, et al. Ann Rheum Dis, 2014 Jun. PMID 23661493
5. The -144C/A polymorphism in the promoter of HSP90beta is associated with multiple organ dysfunction scores. Zhao Y, et al. PLoS One, 2013. PMID 23516526 Free PMC Article
6. Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family.
   Rebbe N.F., Ware J., Bertina R.M., Modrich P., Stafford D.W.
   Gene 53:235-245(1987) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
7. Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene.
   Rebbe N.F., Hickman W.S., Ley T.J., Stafford D.W., Hickman S.
   J. Biol. Chem. 264:15006-15011(1989) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
8. Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens.
   Hoffmann T., Hovemann B.
   Gene 74:491-501(1988) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
9. Cloning a new isoform of heat shock 90kDa in testis.
   Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.
   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
10. Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.
    Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B.
    , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
    Genome Res. 11:422-435(2001) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.