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Home Antibody All anti-HSP90AA1 antibodies

Anti-HSP90AA1 Antibody D7A

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326447
  • Mouse Monoclonal Anti-Hsp90 Antibody
  • FREE positive control: HEK293T cell transient overexpression lysate (LC400399) , 20ug
100µg $325 3-7 Days
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WB(1)
IHC(1)
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Also for HSP90AA1 (NM_001017963)
cDNA Clone shRNA/siRNA Lysate Protein Antibody

OriGene Data

ImmunogenFull length protein Hsp90 purified from chicken brain
Clone NameD7A IsotypeIgG1
Species ReactivityBovine, Chicken, Human, Mouse, Porcine (Pig), Rat, Rabbit Concentration1mg/mL
Guaranteed Application *WB, IHC Suggested DilutionsWB: 1:500, IP: 5ug with 20ul Protein A beads
BufferPBS, 50% glycerol, 0.09% sodium azide
Purification Protein G Purified
Note Recognizes 90kDa proteins corresponding to the molecular mass of Hsp90. Hsp90a specific for human samples. Can isolate complexes of Hsp90, Src kinase and cec37.

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; LAP2
Database LinkNP_001017963
FunctionHsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex . 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 known 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. 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 immune-oadsorption 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 Hsp90 in rat tissue lysates using a 1:1000 dilution of the antibody
IHC Image
IHC staining of inflammatory cells in mouse colon tissue.

 

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