HSP70/HSPA1A Antibody (S5)

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Product Details

Summary
Product Discontinued
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Order Details


    • Catalog Number
      NBP1-45629
    • Availability
      Product Discontinued

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HSP70/HSPA1A Antibody (S5) Summary

Immunogen
Recombinant human Hsp70.
Isotype
IgG1
Clonality
Monoclonal
Host
Mouse
Gene
HSPA1A
Purity
Protein A or G purified
Innovator's Reward
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Applications/Dilutions

Dilutions
  • Western Blot 1 ug/ml
  • Immunohistochemistry 5 - 20 ug/ml
  • Immunohistochemistry-Frozen 5 - 20 ug/ml
  • Immunohistochemistry-Paraffin 5 - 20 ug/ml
  • Immunoprecipitation 5 - 10 ug/ml
Application Notes
The antibody recognizes a 70 kDa protein, corresponding to the apparent molecular weight of the inducible Hsp70 on SDS-PAGE immunoblots. This antibody has no reactivity with the constitutive Hsc70 (Hsp73).

Reactivity Notes

Human.

Packaging, Storage & Formulations

Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
PBS, 1.0 mg/ml BSA, 50% Glycerol. Preservative: 1.5 mM Sodium Azide
Preservative
Sodium Azide
Purity
Protein A or G purified

Alternate Names for HSP70/HSPA1A Antibody (S5)

  • dnaK-type molecular chaperone HSP70-1
  • FLJ54303
  • FLJ54370
  • FLJ54392
  • FLJ54408
  • FLJ75127
  • Heat shock 70 kDa protein 1/2
  • heat shock 70 kDa protein 1A/1B
  • heat shock 70kD protein 1A
  • heat shock 70kDa protein 1A
  • heat shock-induced protein
  • HSP70
  • HSP70.1/HSP70.2
  • HSP70-1
  • HSP70-1/HSP70-2
  • HSP70-1A
  • HSP70I
  • HSP72
  • HSPA1
  • HSPA1A
  • HSPA1B

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 5O% 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 Cterminal 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.

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.

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Bioinformatics

Gene Symbol HSPA1A
Entrez
Uniprot