Human, Mouse, Rat, Beluga, Bovine, Canine, Chicken, Fish, Guinea Pig, Hamster, Primate, Rabbit, Sheep, and water mold.
Alternate Names for HSP90 Antibody (2D12)
Heat shock 86 kDa
heat shock 90kD protein 1, alpha
heat shock 90kD protein 1, alpha-like 4
heat shock 90kD protein, alpha-like 4
heat shock 90kDa protein 1, alpha
heat shock protein 90kDa alpha (cytosolic), class A member 1
heat shock protein HSP 90-alpha
Renal carcinoma antigen NY-REN-38
The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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Heat Shock Proteins: An Overview Heat Shock Proteins (HSPs) are a ubiquitous group of molecular chaperone proteins that have evolved unique mechanisms, within their host cells, to facilitate survival in hostile environments such as heat, oxidative (hypoxia), pH and cold. Under permis... Read full blog post.