HSP90 Alpha Antibody

Heat shock protein HSP 90-alpha, Mouse Anti Human
Cat. No.
BT11433
Source
Synonyms
HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90A, HSP90N, HSPCAL1, HSPCAL4, FLJ31884, Heat shock protein HSP 90-alpha, Renal carcinoma antigen NY-REN-38, HSP 86, HSP90AA1.
Appearance
Sterile Filtered clear solution.
Purity
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Product Specs

Introduction
HSP90 is a ubiquitous heat shock protein found in the cytosol, nucleus, and endoplasmic reticulum of various tissues. It can constitute up to 2% of total cellular protein in tissues like smooth muscle. Functioning as a dimer within heterocomplexes, HSP90 possesses an ATP-binding site and exhibits low ATPase activity. It can associate with actin filaments under specific conditions and bind to unoccupied steroid hormone receptors. As a molecular chaperone, HSP90 maintains target proteins in a folding-competent state, with enhanced chaperone activity in its oligomeric form at elevated temperatures. HSP90's function is sensitive to the concentration of bivalent cations.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The solution contains 1mg/ml of HSP90 Alpha Antibody in a buffer consisting of PBS at pH 7.4, 0.02% sodium azide, and 10% glycerol.
Storage Procedures
For storage up to 1 month, the antibody can be kept at 4°C. For longer-term storage, it is recommended to store at -20°C. Repeated freezing and thawing should be avoided.
Stability / Shelf Life
The antibody has a shelf life of 12 months when stored at -20°C and 1 month when stored at 4°C.
Applications
HSP90A antibody has been validated for use in ELISA, Western blot, and immunohistochemistry, demonstrating its specificity and reactivity. Optimal working dilutions may vary depending on the specific application and should be determined empirically. For Western blot analysis, a dilution range of 1:500 to 1:2,000 is recommended, with a starting dilution of 1:1,000. For immunohistochemistry, a dilution range of 1:100 to 1:200 is recommended, with a starting dilution of 1:100.
Synonyms
HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90A, HSP90N, HSPCAL1, HSPCAL4, FLJ31884, Heat shock protein HSP 90-alpha, Renal carcinoma antigen NY-REN-38, HSP 86, HSP90AA1.
Purification Method
HSP90A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
Type
Mouse Anti Human Monoclonal.
Clone
P4F10AT.
Immunogen
Anti-human HSP90A mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSP90A amino acids 1-732 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.

Product Science Overview

Introduction

Heat shock proteins (HSPs) are a family of proteins that play a crucial role in protecting cells from stress. Among them, Heat Shock Protein 90-alpha (HSP90α) is a highly conserved molecular chaperone involved in the proper folding, stabilization, and degradation of many proteins. This article delves into the background of HSP90α, particularly focusing on the mouse anti-human HSP90α antibody.

Heat Shock Protein 90-alpha (HSP90α)

HSP90α is one of the isoforms of the HSP90 family, which also includes HSP90β. It is a cytosolic protein that is highly expressed in eukaryotic cells and accounts for 1-2% of total cellular proteins under non-stressed conditions. This percentage can increase to 4-6% under stress conditions .

Structure and Function

HSP90α is composed of three main domains:

  1. N-terminal domain (NTD): Involved in ATP binding and hydrolysis.
  2. Middle domain (MD): Facilitates client protein binding.
  3. C-terminal domain (CTD): Responsible for dimerization and interaction with co-chaperones .

The primary function of HSP90α is to act as a molecular chaperone, assisting in the proper folding of nascent proteins, stabilization of proteins against heat stress, and aiding in protein degradation. It also plays a significant role in the maturation and activation of various client proteins, including steroid hormone receptors, kinases, and transcription factors .

Clinical Significance

HSP90α is implicated in various diseases, particularly cancer. It stabilizes several oncoproteins, making it a target for anti-cancer therapies. HSP90 inhibitors are being investigated for their potential to disrupt the function of HSP90α, thereby destabilizing its client proteins and inhibiting tumor growth .

Mouse Anti-Human HSP90α Antibody

Mouse anti-human HSP90α antibodies are monoclonal or polyclonal antibodies developed in mice to specifically target the human HSP90α protein. These antibodies are widely used in research and diagnostic applications, including Western blotting, immunoprecipitation, immunohistochemistry, and flow cytometry .

Development and Applications

The development of mouse anti-human HSP90α antibodies involves immunizing mice with human HSP90α protein or peptides, followed by the collection and purification of the antibodies produced. These antibodies are then validated for their specificity and reactivity with human HSP90α .

In research, these antibodies are used to study the expression, localization, and function of HSP90α in various biological contexts. They are also employed in diagnostic assays to detect HSP90α levels in clinical samples, aiding in the diagnosis and prognosis of diseases such as cancer .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.