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Home Antibody All anti-HSP90AA1 antibodies

Anti-HSP90AA1 Antibody 2G5.G3

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326368
  • Mouse monoclonal Hsp90 alpha Antibody
  • Free Sample of Positive Control: HEK293T cell transient overexpression lysate (LC400399) , 20ug Explanation
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

ImmunogenHuman Hsp90alpha
Clone Name2G5.G3 IsotypeIgG1 Kappa
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 Hsp90a-specific (>96% a-specific by ELISA)

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
Entrez Gene 3320 Human
Entrez Gene 15519 Mouse
Entrez Gene 299331 Rat
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 (1-2% 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 PathwayDruggable Genome Antigen processing and presentationNOD-like receptor signaling pathwayProgesterone-mediated oocyte maturationPathways in cancerProstate cancer

* Availability is in business days
* OriGene provides validated application data and protocol, with money back guarantee.

WB Image
Western blot analysis of Hsp90Alpha in rat tissues, using a 1:1000 dilution of the antibody
IF Image
Hsp90Alpha visulaized using the antibody

 

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