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Merck
CN

H8910

Heat Shock Cognate 70-interacting Protein from rat

≥70% (SDS-PAGE), recombinant, expressed in E. coli

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About This Item

NACRES:
NA.32
UNSPSC Code:
12352202
Form:
buffered aqueous solution
Assay:
≥70% (SDS-PAGE)
Biological source:
rat
Recombinant:
expressed in E. coli
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biological source

rat

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

buffered aqueous solution

concentration

1.1 mg protein/mL

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Quality Level

Gene Information

Biochem/physiol Actions

Hsc70 (heat shock cognate 70) is a molecular chaperone and constitutively expressed type of Hsp70 (heat shock protein 70). It participates in synaptic signal transduction. In hippocampal neurons, it can interact with NFκB (nuclear factor κB) p65. In presence of oxidative stress, it shows protective effect on cardiomyocytes, partly via association with α-enolase. Hsp70 and Hsc70 together are involved in the production and degradation of ERAD (endoplasmic reticulum-associated degradation) substrates. Hsc70 is also needed for myofibril structure maintenance and the suppression of myofibrillar degeneration in presence of mechanical stress.

Physical form

Solution in 20 mM MOPS, pH 7.2, 50 mM KCl, and 2 mM MgCl2

Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Yoshihiro Matsumura et al.
Molecular biology of the cell, 22(16), 2797-2809 (2011-06-24)
The Hsp/c70 cytosolic chaperone system facilitates competing pathways of protein folding and degradation. Here we use a reconstituted cell-free system to investigate the mechanism and extent to which Hsc70 contributes to these co- and posttranslational decisions for the membrane protein
Akinori Hishiya et al.
Circulation research, 107(10), 1220-1231 (2010-10-05)
A homozygous disruption or genetic mutation of the bag3 gene, a member of the Bcl-2-associated athanogene (BAG) family proteins, causes cardiomyopathy and myofibrillar myopathy that is characterized by myofibril and Z-disc disruption. However, the detailed disease mechanism is not yet
Christin Klenke et al.
PloS one, 8(6), e65280-e65280 (2013-06-14)
Signaling via NF-κB in neurons depends on complex formation with interactors such as dynein/dynactin motor complex and can be triggered by synaptic activation. However, so far a detailed interaction map for the neuronal NF-κB is missing. In this study we
Qi Luo et al.
Free radical research, 45(11-12), 1355-1365 (2011-10-01)
Constitutive heat shock protein 70 (Hsc70) is a molecular chaperone that has been shown to protect cardiomyocytes against oxidative stress. However, the molecular mechanism responsible for this protection remains uncertain. To understand the mechanism associated with the myocardial protective role

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