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HSP70 Antibody

     
  •  - HSP70 Antibody ASM10434
    Immunocytochemistry/Immunofluorescence analysis using Chicken Anti-Hsp70 Polyclonal Antibody (ASM10434). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Chicken Anti-Hsp70 Polyclonal Antibody (ASM10434) at 1:120 for 12 hours at 4°C. Secondary Antibody: R-PE Goat Anti-Chicken (yellow) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Perinuclear region of cytoplasm. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp70 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.
    detail
  • WB - HSP70 Antibody ASM10434
    Western blot analysis of Human HeLa cell lysates showing detection of HSP70 protein using Chicken Anti-HSP70 Polyclonal Antibody (ASM10434). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Chicken Anti-HSP70 Polyclonal Antibody (ASM10434) at 1:1000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.
    detail
  •  - HSP70 Antibody ASM10434
    Immunocytochemistry/Immunofluorescence analysis using Chicken Anti-Hsp70 Polyclonal Antibody (ASM10434). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Chicken Anti-Hsp70 Polyclonal Antibody (ASM10434) at 1:120 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Chicken (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Perinuclear region of cytoplasm. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp70 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.
    detail
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB, ICC
Primary Accession P08107
Other Accession NP_005336.3
Host Chicken
Isotype IgY
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Description Chicken Anti-Human HSP70 Polyclonal
Target/Specificity Detects ~70kDa.
Other Names HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody
Immunogen Full length Human HSP70
Purification PEG Purified
Storage -20ºC
Storage Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide
Shipping Temperature Blue Ice or 4ºC
Certificate of Analysis 1 µg/ml of SMC-178 was sufficient for detection of HSP70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-chicken IgG:HRP as the secondary antibody.
Cellular Localization Cytoplasm
Research Areas
Citations (0)
citation

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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 (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5). 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

References

1. Balashova N. et al. (2005) J Biol Chem 280: 2186-96.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38 (1): 1-17.
3. Rothman J. (1989) Cell 59: 591 -601.
4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.

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Cat# ASM10434
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