HSP90B1 P94B9AT Antibody

Heat Shock Protein 90kDa Beta (GRP94) Member 1 , Mouse Anti Human
Cat. No.
BT11630
Source
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
Appearance
Sterile filtered colorless 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
HSP90B1, a member of the Hsp90 family, is an abundant molecular chaperone found within the endoplasmic reticulum (ER) lumen. This stress protein plays a crucial role in maintaining protein homeostasis within the secretory pathway. Additionally, HSP90B1 participates in the intracellular trafficking of peptides, directing them from the extracellular space to the MHC class I antigen processing pathway in antigen-presenting cells. HSP90B1 is involved in various cellular processes, including signal transduction, protein folding, protein degradation, and morphological development. This protein interacts with numerous cochaperones, assisting in the folding of newly synthesized proteins and stabilizing or refolding denatured proteins following stress. Notably, HSP90B1 exhibits high expression levels throughout the entire cell cycle in human gastric carcinoma BGC-823 cells.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The antibody solution has a concentration of 1 mg/ml and is prepared in a buffer containing PBS with a pH of 7.4, 10% glycerol, and 0.02% sodium azide.
Storage Procedures
For storage up to 1 month, maintain the antibody at 4°C. For extended storage, store at -20°C. Avoid repeated freeze-thaw cycles.
Stability / Shelf Life
The antibody remains stable for 12 months when stored at -20°C and for 1 month at 4°C.
Applications
The HSP90B1 antibody has undergone rigorous testing in various applications, including ELISA, Western blot analysis, ICC/IF, and Flow cytometry, to confirm its specificity and reactivity. However, it is essential to optimize the antibody concentration for each specific application to achieve the best results.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
Purification Method
HSP90B1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
Type
Mouse Anti Human Monoclonal.
Clone
P94B9AT.
Immunogen
Anti-human HSP90B1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human HSP90B1 protein 22-803 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.

Product Science Overview

Introduction

Heat Shock Protein 90kDa Beta (GRP94) Member 1, also known as HSP90B1, is a molecular chaperone that plays a crucial role in the folding and stabilization of other proteins. It is a member of the heat shock protein 90 (HSP90) family and is predominantly found in the endoplasmic reticulum (ER). This protein is also referred to as endoplasmin, gp96, or ERp99 .

Structure and Function

HSP90B1 is an ATP-metabolizing molecular chaperone that assists in the proper folding of secreted and membrane-bound proteins. It has ATPase activity, which is essential for its chaperone function. The protein is involved in the endoplasmic reticulum-associated degradation (ERAD) pathway, where it helps in the degradation of misfolded proteins .

HSP90B1 is also known to participate in the unfolding of cytosolic leaderless cargos, such as interleukin 1 (IL-1), to facilitate their translocation into the ER-Golgi intermediate compartment (ERGIC) and subsequent secretion. This translocation process is mediated by the cargo receptor TMED10 .

Biological Significance

HSP90B1 plays a critical role in various biological processes, including:

  • Protein Folding: It assists in the folding of proteins within the ER, ensuring that they attain their proper conformation.
  • Immune Response: HSP90B1 is essential for the proper folding of Toll-like receptors (TLRs) and integrins, which are crucial for both innate and adaptive immunity .
  • Stress Response: It is involved in the cellular response to stress, particularly in the unfolded protein response (UPR) pathway .
  • Calcium Homeostasis: HSP90B1 helps in sequestering calcium ions within the ER, maintaining calcium homeostasis .
Clinical Relevance

The expression of HSP90B1 is associated with various pathogenic states, including tumor formation. It has been implicated in cancer progression and is considered a potential target for cancer therapy. Additionally, mutations in the HSP90B1 gene have been linked to diseases such as Pelizaeus-Merzbacher-Like Disease and Nemaline Myopathy 9 .

Mouse Anti Human HSP90B1

Mouse anti-human HSP90B1 antibodies are commonly used in research to study the protein’s function and its role in various diseases. These antibodies are generated by immunizing mice with human HSP90B1 protein, leading to the production of antibodies that specifically recognize and bind to the human version of the protein. These antibodies are valuable tools for detecting HSP90B1 in various experimental settings, including Western blotting, immunohistochemistry, and immunoprecipitation .

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