HspA4 Antibody (5A5)

Product Discontinued

HspA4 Antibody (5A5) Summary

• Immunogen: Human recombinant HSP70 overexpressed in E.coli
• Localization: Cytoplasm
• Specificity: May detect HSP70, HSC70, Grp78 and HSP72.
• Isotype: IgG1
• Clonality: Monoclonal
• Host: Mouse
• Gene: HSPA4
• Purity: Protein G purified

Applications/Dilutions

• Dilutions:
  • Immunocytochemistry/ Immunofluorescence 1:500
  • Immunohistochemistry
  • Immunoprecipitation 1ug
  • Western Blot 1:1000
• Application Notes: 1 ug/ml of this antibody was sufficient for detection of HSP70 in 20 ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
• Theoretical MW: 70 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Reactivity Notes

Yeast (Saccharomyces cerevisiae), Fruit Fly (Drosophila melanogaster)

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS pH7.2, 50% glycerol
• Preservative: 0.09% Sodium Azide
• Concentration: 1 mg/ml
• Purity: Protein G purified

Alternate Names for HspA4 Antibody (5A5)

• APG2
• APG-2
• heat shock 70 kDa protein 4
• heat shock 70kD protein 4
• heat shock 70kDa protein 4
• Heat shock 70-related protein APG-2
• heat shock protein, 110 kDa
• HS24/P52
• hsp70
• hsp70RY
• MGC131852
• RY

Background

HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5).All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Bioinformatics

• Gene Symbol: HSPA4