Anti-Heat Shock Protein 90α Antibody

Control
HeLa cell lysate

Evaluated by Western Blot in HeLa cell lysate.

Western Blot Analysis: 0.0625 µg/mL of this antibody detected Heat Shock Protein 90α on 10 µg of HeLa cell lysate.

Detect the Heat Shock Protein 90α protein using this Anti-Heat Shock Protein 90α validated for use in WB, IP, ICC & IHC.

Research Category
Protein Trafficking

Research Sub Category
Chaperones

Western Blot (Snap i.d.) Analysis: 1 µg/mL from a previous lot detected Heat Shock Protein 90α on 10 µg of NIH/3T3 cell lysate.

Immunohistochemistry Analysis: 1:100 dilution from a previous lot detected Heat Shock Protein 90α in human prostate adenocarcinoma tissue.

Immunocytochemistry Analysis: 1:500 dilution from a previous ot detected Heat Shock Protein 90α in A431 cells.

Immunoprecipitation Analysis: 10 µg from a previous lot immunoprecipitated Heat Shock Protein 90A from HeLa cell lysate.

This antibody recognizes Heat Shock Protein 90α at the N-terminus.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

The Heat Shock Protein 90 family is known as a group of molecular chaperones involved in the regulation of maturation, degradation, and folding transport for a select, yet varied group of proteins primarily comprised of signaling molecules, but also including tyrosine kinases, G-protein subunits, transcription factors, and telomerase. Heat Shock Protein 90 has two isoforms that share a homology of 76%; Heat Shock Protein 90α (HSP90α) and Heat Shock Protein 90β (HSP90β). HSP90α contains a charged sequence linker, a C-terminal domain, and N-terminal domain and a middle domain. It is induced by oxidative stress and has been observed in exosomes where it is secreted into the extracellular environment following translocation via TGFα stimulus. Extracellular HSP90α functions to facilitate the migration of both dermal and epidermal cells through its interaction with cell surface receptors CD91 and LRP1. HSP90α interaction with TERT is a necessary component of TERT holoenzyme complex assembly and stabilization. It has also been shown to interact with a variety of other proteins such as FNIP1, HSF1, TOM34, AHSA1, SMYD3, and DNAJC7.

~ 90 kDa observed

Epitope: N-terminus

KLH-conjugated linear peptide corresponding to the N-terminus of human Heat Shock Protein 90α.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Format: Purified

Protein A

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.