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Hsp70 antibody, MAb (ATTO-594)

Research Use Only
ORB147561
Biorbyt
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, Other Application
Product group Antibodies
ReactivityAmphibian, Bacteria, Chicken, Drosophila, Fish, Human, Mouse, Rat, Yeast, Other Species
Price on request
Packing Size
Large volume orders?
Order with a bulk request

Overview

  • Supplier
    Biorbyt
  • Product Name
    Hsp70 antibody, MAb (ATTO-594)
  • Delivery Days Customer
    10
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, Other Application
  • Applications Supplier
    WB (1:5000), ICC/IF (1:500), IP (2µg) AM, ICC, IP, WB, IHC
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    3A3
  • Concentration
    1 mg/ml
  • Conjugate
    Atto 594
  • Host
    Mouse
  • Isotype
    IgG1
  • Scientific Description
    Mouse monoclonal to Hsp70 (ATTO-594). 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. 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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. 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.
  • Reactivity
    Amphibian, Bacteria, Chicken, Drosophila, Fish, Human, Mouse, Rat, Yeast, Other Species
  • Storage Instruction
    2°C to 8°C
  • UNSPSC
    12352203