Hsp70 (human recombinant, baculovirus expressed)

Hsp70 (human recombinant, baculovirus expressed) Basic information
Product Name:Hsp70 (human recombinant, baculovirus expressed)
Synonyms:Hsp70 (human recombinant, baculovirus expressed)
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Hsp70 (human recombinant, baculovirus expressed) Structure
Hsp70 (human recombinant, baculovirus expressed) Chemical Properties
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Hsp70 (human recombinant, baculovirus expressed) Usage And Synthesis
DescriptionHeat shock protein 70s (Hsp70s) are abundant and stress-inducible 70 kDa molecular chaperone proteins encoded by a highly conserved, multigene family. They are monomeric proteins that can be divided into two functional domains: an N-terminal ATPase domain and a substrate binding domain that contains a highly conserved EEVD motif at its C-terminus. Hsp70s are found in the cytosol, nuclei, endoplasmic reticulum, mitochondria, and chloroplasts of eukaryotes, as well as in bacteria. They function as molecular chaperones that assist in a wide range of cellular processes, including refolding of aggregated or misfolded proteins, co- and post-translational folding and assembly of nascent peptides, membrane translocation of secretory and organellar proteins, controlling activity of regulatory nuclear receptors, kinases and transcription factors, as well as acting cooperatively with the Hsp90 chaperone system in eukaryotes. The Hsp70 chaperone cycle is ATP-dependent and initiated by transient interaction of the Hsp70 substrate binding domain with hydrophobic regions within a peptide or protein. It consists of an alteration between the low-affinity ATP-bound state with fast rates of substrate exchange and the high-affinity ADP bound state with slow rates of substrate exchange. Hsp70s are subject to a variety of post-translational modifications and their expression is upregulated under conditions of cellular stress and in a variety of disease states. This product contains human recombinant Hsp70 expressed and purified from baculovirus infected insect cells. This Eukaryotic expression system allows post-translational modifications to occur on the protein product (i.e., glycosylation, phosphorylation, acetylation, etc).
References[1] W R BOORSTEIN  E A C  T Ziegelhoffer. Molecular evolution of the HSP70 multigene family.[J]. Journal of Molecular Evolution, 1994, 38 1: 1-17. DOI: 10.1007/bf00175490
Hsp70 (human recombinant, baculovirus expressed) Preparation Products And Raw materials
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