H7283
Heat Shock Protein 70 human
recombinant, expressed in E. coli, buffered aqueous solution, ≥90% (SDS-PAGE)
Synonyme(s) :
HSP 70
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About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in E. coli
Pureté
≥90% (SDS-PAGE)
Forme
buffered aqueous solution
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... HSPA8(3312)
Application
Heat shock protein 70 human has been used as a control for checking antibody reactivity.
Actions biochimiques/physiologiques
HSPA8 (heat shock 70kDa protein 8) is a human cytoplasmic chaperone which is involved in protein folding, protein aggregation prevention and protein transport. During nutrient stress, it participates in antigen transport to regulate MHC (major histocompatibility) class II presentation. It is upregulated in cancer cells and is involved in protein homeostasis, leading to cancer cell growth and survival.
Forme physique
Solution in 2.7 mM KCl, 1.5 mM KH2PO4, 137 mM NaCl, and 8.1 mM Na2HPO4.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
Structure (London, England : 1993), 23(3), 472-482 (2015-02-17)
The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the tetratricopeptide repeat (TPR)
Molecular immunology, 68(2 Pt A), 85-88 (2015-05-09)
Cells rely on multiple intracellular trafficking pathways to capture antigens for proteolysis. The resulting peptides bind to MHC class II molecules to promote CD4(+) T cell recognition. Endocytosis enhances the capture of extracellular and cell surface bound antigens for processing
Journal of virology, 82(14), 6962-6971 (2008-05-02)
Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of SARS, an emerging disease characterized by atypical pneumonia. Using a yeast two-hybrid screen with the nucleocapsid (N) protein of SARS-CoV as a bait, the C terminus (amino acids 251
PloS one, 9(5), e96785-e96785 (2014-05-08)
Heat shock cognate protein 70 (Hsc70) acts as a molecular chaperone for the maintenance of intracellular proteins, which allows cancer cells to survive under proteotoxic stress. We attempted to use Hsc70 to identify key molecules in cancer cell survival. Here
PloS one, 10(8), e0135603-e0135603 (2015-08-20)
Mild heat stress promotes thermotolerance and protection against several different stresses in aquatic animals, consequences correlated with the accumulation of heat shock protein 70 (Hsp70). The purpose of this study was to determine if non-lethal heat shock (NLHS) of the
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