ELISA. Western blot: 1 μg/mL was sufficient for detection of Hsp90alpha/beta by Western Blot in20 μg of HeLa lysate. (Ref.1, 10)Immunohistochemistry on Frozen Sections. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions
For Research Use only
Concentration
1.0 mg/mL
Buffer
PBS, pH 7.2, 0.09 % Sodium Azide, 50 % Glycerol
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C/-20 °C
Stockage commentaire
Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch.
Date de péremption
12 months
Antigène
HSP90AA1
(Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
anticorps EL52, anticorps HSP86, anticorps HSP89A, anticorps HSP90A, anticorps HSP90N, anticorps HSPC1, anticorps HSPCA, anticorps HSPCAL1, anticorps HSPCAL4, anticorps HSPN, anticorps Hsp89, anticorps Hsp90, anticorps LAP2, anticorps Hsp86, anticorps Hspca, anticorps htpG, anticorps 86kDa, anticorps 89kDa, anticorps AL024080, anticorps AL024147, anticorps Hsp86-1, anticorps hsp4, anticorps HSP90, anticorps HSP90AA1, anticorps fb17b01, anticorps hsp90, anticorps hsp90a, anticorps hsp90a.1, anticorps hsp90alpha, anticorps wu:fb17b01, anticorps zgc:86652, anticorps Hsp90alpha, anticorps heat shock protein 90 alpha family class A member 1, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, anticorps Heat Shock Protein 90, cytosolic, anticorps heat shock protein 90A, anticorps molecular chaperone, anticorps heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1, anticorps heat shock protein HSP 90-alpha, anticorps heat shock protein 90kDa alpha (cytosolic), class A member 1, anticorps HSP90AA1, anticorps Hsp90aa1, anticorps HSP90A, anticorps hsp90A, anticorps hsp90aa1.1, anticorps LOC108698781
Sujet
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85 % sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) 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 (7-8). 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 (9).Synonyms: HSP-84, HSP-86, HSP-90, HSP84, HSP86, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSPC1, HSPC2, HSPCA, HSPCB, Heat shock protein HSP 90-alpha, Heat shock protein HSP 90-beta, Renal carcinoma antigen NY-REN-38