anti-Hsp 90 alpha antibody [D7 alpha (D7a)]

anti-Hsp 90 alpha antibody [D7 alpha (D7a)] for Immunoprecipitation,Western blot and Bovine,Chicken,Human,Mouse,Pig,Rabbit,Rat

Cancer antibody; Signaling Transduction antibody


Product Description Mouse Monoclonal antibody [D7 alpha (D7a)] recognizes Hsp 90 alpha
Tested Reactivity Hu, Ms, Rat, Bov, Chk, Pig, Rb
Tested Application IP, WB
Specificity This antibody recognizes human, mouse, rat, rabbit, bovine, porcine, and chicken Hsp90α (90 kDa).
Host Mouse
Clonality Monoclonal
Clone D7 alpha (D7a)
Isotype IgG1
Target Name Hsp 90 alpha
Antigen Species Chicken
Immunogen Full-length Hsp90 purified from chicken brain
Conjugation Un-conjugated
Alternate Names EL52; Hsp90; HSPC1; Heat shock 86 kDa; LAP-2; HSP90N; LAP2; HSP90A; HSPCAL4; HSP89A; HSP86; HSP 86; HSPCA; Lipopolysaccharide-associated protein 2; HSPCAL1; LPS-associated protein 2; HSPN; Renal carcinoma antigen NY-REN-38; Heat shock protein HSP 90-alpha; Hsp89

Application Instructions

Application Note Western blot: use at 1 - 5 ug/ml. A band of ~90 kDa is detected.
Immunoprecipitation: 5 ug on 20 ul Protein A - Sepharose + 100 ul sample.
* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
Positive Control Heat-shocked HeLa cell lysate.


Form Liquid
Purification Protein G affinity chromatography
Buffer PBS (pH 7.4), 50% Glycerol and 0.09% Sodium azide
Preservative 0.09% Sodium azide
Stabilizer 50% Glycerol
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.


Database Links

GeneID: 15519 Mouse HSP90AA1

GeneID: 281832 Bovine HSP90AA1

GeneID: 299331 Rat HSP90AA1

Gene Symbol HSP90AA1
Gene Full Name heat shock protein 90kDa alpha (cytosolic), class A member 1
Background Hsp90 and the 94 kDa glucose-regulated protein, Grp94, are major molecular chapeones of the cytosol and endoplasmic reticulum. In mammalian cells, there are at least two Hsp90 isoforms, Hsp90α and Hsp90β, which are encoded by separate genes. All known members of the Hsp90 family are highly conserved, especially in the N-terminal and C-terminal regions. In the absence of stress, Hsp90 is an essential component of cellular processes such as hormone signaling and cell cycle control. Several regulatory proteins such as steroid receptors, cell cycle kinases and p53 have been identified as substrates of Hsp90.
Function Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). [UniProt]
Research Area Cancer antibody; Signaling Transduction antibody
Calculated MW 85 kDa
PTM ISGylated.
S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.

Clone References

A systems biology-based investigation into the therapeutic effects of Gansui Banxia Tang on reversing the imbalanced network of hepatocellular carcinoma.

WB, IHC-P / Mouse

Zhang Y et al.
Sci Rep.,  (2014)




LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in lung vascular endothelial cells and mouse lung.

Barabutis N et al.
Am J Physiol Lung Cell Mol Physiol.,  (2013)




Regulation of mouse steroidogenesis by WHISTLE and JMJD1C through histone methylation balance.

WB, IP / Mouse

Kim SM et al.
Nucleic Acids Res.,  (2010)




Hsp90 cleavage by an oxidative stress leads to its client proteins degradation and cancer cell death.

WB / Human

Beck R et al.
Biochem Pharmacol.,  (2009)




Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.

Johnson JL et al.
Mol Cell Biol.,  (1994)