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Home Antibody All anti-HSP90AA1 antibodies

Anti-HSP90AA1 Antibody 4F3.E8

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326369
  • Mouse monoclonal Hsp90 (total) Antibody
  • Free Sample of Positive Control: HEK293T cell transient overexpression lysate (LC400399) , 20ug
200µg 325 3-7 Days
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WB(1)
IF(1)
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Also for HSP90AA1 (NM_001017963)
cDNA Clone shRNA/siRNA Lysate Protein Antibody

OriGene Data

ImmunogenRecombinant Human Hsp90 purified from E.coli
Clone Name4F3.E8 IsotypeIgG1
Species ReactivityHuman, Mouse, Rat. Other species not tested yet. Concentration1mg/mL
Guaranteed Application *WB, IF Suggested DilutionsWB: 1:2000
BufferPBS pH7.2, 50% glycerol
Purification Protein G Purified
Note This antibody detects both a and ß forms of Hsp90 equally well.

Reference Data

Target NameHomo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 1
Alternative NameEL52; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP-2; LAP2
Database LinkNP_001017963
FunctionHSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms and , which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment . Despite the similarities, HSP90 exists predominantly as a homodimer while HSP90 exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (12% of cytosolic protein). It carries out a number of housekeeping functions including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling . The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function .
Related Pathway
Cell cycle

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WB Image
Western blot analysis of Hsp90Total in rat tissues, using a 1:1000 dilution of the antibody
IF Image
Hsp90 Total visualized using the antibody

 

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