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Hsp70-derived octapeptide
CAS No. 736171-62-3
Hsp70-derived octapeptide( —— )
Catalog No. M30315 CAS No. 736171-62-3
A group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated.
Purity : >98% (HPLC)
COA
Datasheet
HNMR
HPLC
MSDS
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Biological Information
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Product NameHsp70-derived octapeptide
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NoteResearch use only, not for human use.
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Brief DescriptionA group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated.
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DescriptionA group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated.
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In Vitro——
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In Vivo——
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Synonyms——
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PathwayCytoskeleton/Cell Adhesion Molecules
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TargetHSP
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Recptor——
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Research Area——
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Indication——
Chemical Information
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CAS Number736171-62-3
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Formula Weight858.89
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Molecular FormulaC36H58N8O16
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Purity>98% (HPLC)
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SolubilityIn Vitro:?H2O : 1.82 mg/mL (2.12 mM)
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SMILES——
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Chemical NameSequence:{Gly}{Pro}{Thr}{Ile}{Glu}{Glu}{Val}{Asp}
Shipping & Storage Information
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Storage(-20℃)
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ShippingWith Ice Pack
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Stability≥ 2 years
Reference
Tutar Y, et al. Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supportinggrowth and prion propagation in Saccharomyces cerevisiae. Genetics. 2006 Feb;172(2):851-61.
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