Human/Mouse/Rat HSP70/HSPA1A Antibody Summary
Accession # NP_005336
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human and Mouse HSP70/ HSPA1A by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line and NIH-3T3 mouse embryonic fibroblast cell line untreated (-) or treated (+) with a 42 °C heat shock for 30 minutes with a 3 hour recovery. PVDF membrane was probed with 0.1 µg/mL of Mouse Anti-Human/Mouse/Rat HSP70/HSPA1A Monoclonal Antibody (Catalog # MAB1663), followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for HSP70/HSPA1A at approximately 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.
HSP70/HSPA1A in Human Liver Cancer Tissue. HSP70/HSPA1A was detected in immersion fixed paraffin-embedded sections of human liver cancer tissue using Mouse Anti-Human/Mouse/Rat HSP70/HSPA1A Monoclonal Antibody (Catalog # MAB1663) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Detection of Human HSP70/HSPA1A by Simple WesternTM. Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line untreated (-) or treated (+) by heat shocked (HS), loaded at 0.2 mg/mL. A specific band was detected for HSP70/HSPA1A at approximately 67 kDa (as indicated) using 0.5 µg/mL of Mouse Anti-Human/Mouse/Rat HSP70/HSPA1A Monoclonal Antibody (Catalog # MAB1663). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
The heat shock proteins are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. Some HSPs are expressed at low levels under normal physiological conditions but show dramatically increased expression in response to cellular stress, others are constitutively expressed. Specific HSPs play a role in regulating apoptosis by interacting directly with key components of the apoptotic pathway.
Citations for Human/Mouse/Rat HSP70/HSPA1A Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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Comparative analysis of the interaction of HSPs in dendritic cells, macrophages, RGM-1 cells infected by Helicobacter pylori
Authors: Guangxin Li
Am J Transl Res, 2016;8(10):4184-4194.
Sample Types: Whole Cells
Applications: Western Blot
Exosomes released from macrophages infected with intracellular pathogens stimulate a proinflammatory response in vitro and in vivo.
Authors: Bhatnagar S, Shinagawa K, Castellino FJ, Schorey JS
Sample Types: Exosomes
Applications: Western Blot
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