The Mouse Monoclonal anti-HSP90AA1 antibody (Clone D7alpha) (ABIN452367) specifically detects HSP90AA1 in WB, IP and IHC (fro).
The antibody is reactive with Human, Mouse, Rat, Rabbit, Cow, Chicken and Pig samples.
This antibody recognizes 90 kDa proteins corresponding to the molecular mass of hsp90. Hsp90alpha specific for human samples. Can isolate complexes of hsp90, Src kinase and cdc37 (1, 2, 3).
Cross-Reactivity (Details)
Species reactivity (tested):Bovine, Chicken, Human, Mouse, Porcine (Pig), Rat, Rabbit.
Immunoprecipitation (1, 2, 3): 5 μg with 20 μL Protein A beads. Immunohistochemistry on frozen sections.
Restrictions
For Research Use only
Concentration
1.0 mg/mL
Buffer
Mouse IgG in PBS buffer, 0.09 % sodium azide and 50 % glycerol
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C/-20 °C
Storage Comment
Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer. Avoidrepeated freezing and thawing. Shelf life: one year from despatch.
Expiry Date
12 months
Target
HSP90AA1
(Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
Alternative Name
HSP90AA1 / HSP90 alpha
Background
Hsp90 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 (4-7). 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 (8-9). 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(6). 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 (10).Synonyms: HSP86, HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, Heat shock protein HSP 90-alpha, NY-REN-38