HSPA5 Antibody

Heat Shock 70kDa protein 5, Mouse Anti Human
Cat. No.
BT11771
Source
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
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
Binding immunoglobulin protein (BiP or HSPA5), a member of the 70kDa heat shock protein (HSP70) family, acts as a stress response protein. Its production increases when agents or conditions disrupt endoplasmic reticulum (ER) function. HSPA5 plays a critical role in ensuring proper protein glycosylation and folding, maintaining cell homeostasis, and preventing apoptosis.
Physical Appearance
The product appears as a clear, colorless liquid that has been sterilized through filtration.
Formulation
The antibody is supplied in a solution containing 1mg/ml of antibody in a buffer composed of PBS at pH 7.4, 10% glycerol, and 0.02% sodium azide.
Storage Procedures
Store the antibody at 4°C for up to one month. For longer-term storage, 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
This HSPA5 antibody has been validated for ELISA and Western blot analysis, demonstrating its specificity and reactivity. However, optimal working dilutions should be determined empirically for each specific application. A starting dilution of 1:1000 is recommended.
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Purification Method
HSPA5 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
Type
Mouse Anti Human Monoclonal.
Clone
PAT3D2AT.
Immunogen
Anti-human HSPA5 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human HSPA5 protein 20-650 amino acids purified from Baculovirus.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.

Product Science Overview

Introduction

Heat Shock 70kDa Protein 5 (HSP70) is a member of the heat shock protein family, which plays a crucial role in protein folding, protection against stress, and cellular homeostasis. The HSP70 family is highly conserved across species, including humans and mice. The Mouse Anti-Human HSP70 antibody is a monoclonal antibody used in various research applications to detect and study the HSP70 protein in human tissues and cells.

Structure and Function

HSP70 proteins are characterized by their molecular weight of approximately 70 kDa. They consist of two main domains: the N-terminal ATPase domain and the C-terminal substrate-binding domain. The ATPase domain is responsible for binding and hydrolyzing ATP, which provides the energy required for the protein’s chaperone activity. The substrate-binding domain interacts with unfolded or misfolded proteins, preventing their aggregation and assisting in their proper folding.

HSP70 proteins are involved in several cellular processes, including:

  • Protein folding and assembly: HSP70 assists in the proper folding of newly synthesized proteins and the refolding of denatured proteins.
  • Protein transport: HSP70 facilitates the translocation of proteins across cellular membranes.
  • Protection against stress: HSP70 is upregulated in response to various stress conditions, such as heat shock, oxidative stress, and inflammation, to protect cells from damage.
  • Regulation of apoptosis: HSP70 can inhibit apoptosis by interacting with key components of the apoptotic pathway.
Preparation and Synthetic Routes

The Mouse Anti-Human HSP70 antibody is typically produced using hybridoma technology. This involves the following steps:

  1. Immunization: Mice are immunized with human HSP70 protein or peptides to elicit an immune response.
  2. Cell Fusion: Spleen cells from the immunized mice, which produce antibodies, are fused with myeloma cells to create hybridoma cells. These hybridoma cells can proliferate indefinitely and produce large quantities of the desired antibody.
  3. Screening and Selection: Hybridoma cells are screened for the production of antibodies that specifically recognize human HSP70. Positive clones are selected and expanded.
  4. Purification: The antibodies are purified from the hybridoma cell culture supernatant using techniques such as protein A or protein G affinity chromatography.
Applications

The Mouse Anti-Human HSP70 antibody is widely used in various research applications, including:

  • Western Blotting: To detect and quantify HSP70 protein levels in cell and tissue lysates.
  • Immunohistochemistry: To visualize the localization and expression of HSP70 in tissue sections.
  • Flow Cytometry: To analyze HSP70 expression in individual cells.
  • Immunoprecipitation: To isolate HSP70 protein complexes from cell lysates for further analysis.

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