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Active Human HSP70 Protein

Active Human HSP70 Protein

388.00 EUR

Untagged recombinant human HSP70 Protein expressed in E. coli for WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA. This protein is biologically active (ATPase active).
Proveedor: Stressmarq
Disponibilidad: In Order
Número del catálogo: SPR-108B
Tamaño: 0.1 mg

  • Shipped on ice packs (+4ºC). Keep frozen at -20ºC.
  • Non-hazrdous for transportation according to both ADR and UN.
  • Protein type: Recombinant
  • Host species: Human
  • Expression system: E. coli
  • Tag: not tagged
  • Biological activity: Active (ATPase active)
  • Protein length: Full Length
  • Molecular weight: ~70 kDa
  • Purity: >90%
  • Purification method: Multi-Step Purified
  • Concentration: Usually ~1mg/ml. Check the CoA of the latest batch for precise information.
  • Storage Buffer : 50mM Tris/HCl pH7.5, 2.5mM Bme, 0.15M NaCl, 10% glycerol
  • Tested applications: WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
For research use only. Not to be used for human or anumal treatment or consumption. 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 44kDa 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

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