Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody

Details for Product No. ABIN121243
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Antigen
Reactivity
Chicken, Mammalian
(185), (114), (103), (19), (18), (16), (15), (12), (4), (2), (2), (2), (2)
Host
Mouse
(139), (56), (1)
Clonality
Monoclonal
Conjugate
Un-conjugated
(3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB)
(180), (91), (90), (58), (38), (38), (32), (13), (12), (10), (1), (1), (1), (1)
Pubmed 5 references available
Quantity 0.1 mg
Shipping to United States (Change)
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Catalog No. ABIN121243
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Immunogen Purified recombinant human Hsp90 beta (1)
Isotype IgM
Purification Purified
Alternative Name HSP90AB1 / HSP90 beta
Background The 90 kDa molecular chaperone family comprises several proteins including the 90 kDa heat shock protein, Hsp90 and the 94 kDa glucose-regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90 alpha and Hsp90 beta which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90 alpha is 85% and 90% homologous to that of Hsp90 beta respectively (2). All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions which have been shown to contain independent chaperone sites with different substrate specificity (3,4). These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steroid receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90 (5). It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways. Recent studies indicate that when Drosophila Hsp90 buffering is compromised by e.g., temperature, cryptic variants are expressed and selection can lead to the continued expression of these traits, even if Hsp90 function is restored (6).
UniProt P08238
Application Notes Western blotting. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Storage 4 °C
Storage Comment Store for 2-4 weeks at 4°C. For optimal storage, aliquot to smaller portions and store at -20°C to avoid temperature fluctuations. For maximum product recovery centrifuge the product vial before removing cap. Shelf Life: one year from despatch.
Expiry Date 12 months
Supplier Images
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody Western blot analysis of Hsp90 beta in Jurkat whole cell lysate using SM7037 at 1 ug/ml.
General Nemoto, Sato, Iwanari et al.: "Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis." in: The Journal of biological chemistry, Vol. 272, Issue 42, pp. 26179-87, 1997 (PubMed).

Nemoto, Sato: "Oligomeric forms of the 90-kDa heat shock protein." in: The Biochemical journal, Vol. 330 ( Pt 2), pp. 989-95, 1998 (PubMed).

Scheibel, Buchner: "The Hsp90 complex--a super-chaperone machine as a novel drug target." in: Biochemical pharmacology, Vol. 56, Issue 6, pp. 675-82, 1998 (PubMed).

Rutherford, Lindquist: "Hsp90 as a capacitor for morphological evolution." in: Nature, Vol. 396, Issue 6709, pp. 336-42, 1998 (PubMed).

Scheibel, Siegmund, Jaenicke et al.: "The charged region of Hsp90 modulates the function of the N-terminal domain." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 4, pp. 1297-302, 1999 (PubMed).

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