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H8285

Sigma-Aldrich

Heat Shock Cognate Protein 70 bovine

≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

bovine

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

technique(s)

protein quantification: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

General description

HSCP70 (heat shock cognate protein 70) is a molecular chaperone and cognate member of the hsp70 family.

Application

Heat shock cognate protein 70 bovine has been used as an internal control to quantify the levels of Hsp70 (heat shock protein 70) in juvenile Concholepas concholepas (Mollusca) and Northern scallops Argopecten purpuratus.

Physical form

Solution in 30 mM Tris-HCl, pH 7.5, 300 mM NaCl, 2 mM DTT, and 1 mM EDTA.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Effects of the toxic dinoflagellate Alexandrium catenella on histopathogical and escape responses of the Northern scallop Argopecten purpuratus.
Hegaret H
Harmful Algae, 18, 74-83 (2012)
R P Ciavarra et al.
Cellular immunology, 129(2), 363-376 (1990-09-01)
We have investigated the effect of febrile temperatures (less than or equal to 41 degrees C) on T cell heat shock protein (hsp) synthesis and the acquisition of stress tolerance. Enhanced synthesis of hsps was detected in highly purified T
Effect of allozyme heterozygosity on basal and induced levels of heat shock protein (Hsp70), in juvenile Concholepas concholepas (Mollusca).
Brokordt K
Journal of Experimental Marine Biology and Ecology, 370, 18-26 (2009)
B Stahl et al.
European journal of cell biology, 78(6), 375-381 (1999-08-03)
The cysteine string protein (csp) is a synaptic vesicle protein found to be essential for normal neurotransmitter release. The precise function of csp in the synaptic vesicle cycle is still enigmatic. By interacting with the heat-shock cognate hsc70, a cochaperone-chaperone
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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