Se connecter pour consulter les tarifs organisationnels et contractuels.
Sélectionner une taille de conditionnement
A propos de cet article
Form:
buffered aqueous glycerol solution
Assay:
≥70% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
Mol wt:
~70 kDa
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderService technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderbiological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~70 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HSPA1A(3303)
General description
Heat shock protein 70 (HSP70) is a ubiquitous molecular chaperone. It comprises an N-terminal domain, nucleotide-binding domain (NBD), substrate-binding domain (SBD), and a C-terminal domain.
Application
Heat shock protein 70 (HSP70), His tagged human has been used:
- to study the interaction between HSP70 and receptor of advanced glycation endproducts (RAGE) using protein proximity ligand assay (PLA)
- to facilitate the import of superoxide dismutase 2 (SOD2) into the mitochondria
- to study its role in muscle catabolism
Biochem/physiol Actions
Heat shock protein 70 (HSP70) plays a role in the cellular protein folding and remodeling process. It is also involved in the translocation of polypeptides into the chloroplast, mitochondria, and endoplasmic reticulum. HSP70 facilitates dismantling of protein complexes and modulates protein activity. It also plays a role in guarding cells from proteotoxic stress, pathophysiological conditions, and organismal aging. HSP70 participates in the activation of several immune cells such as macrophages, natural killer (NK) cells, B lymphocytes, peripheral monocytes, and antigen-presenting cells (APCs).
Physical form
Supplied in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Classe de stockage
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Faites votre choix parmi les versions les plus récentes :
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
The major heat-shock protein (hsp70) gene family: related sequences in mouse, Drosophila, and yeast.
L A Moran et al.
Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire, 61(6), 488-499 (1983-06-01)
Heat shock induces the synthesis of a 70-kdalton protein in Escherichia coli, Drosophila, yeast, and mouse. We show that the genes for this heat-shock protein in mouse, yeast, and Drosophila share extensive sequence homology as determined by heteroduplex formation at
Hsp70 accelerates the recovery of nucleolar morphology after heat shock.
Pelham HR
The Embo Journal, 3(13), 3095-3100 (1984)
Human monocyte heat shock protein 72 responses to acute hypoxic exercise after 3 days of exercise heat acclimation.
Lee BJ
BioMed Research International (2015)
Analysis of serum heat shock protein 70 (HSPA1A) concentrations for diagnosis and disease activity monitoring in patients with rheumatoid arthritis.
Cell Stress & Chaperones, 20(3) (2015)
Polymorphisms in the Hsp70 gene locus are genetically associated with systemic lupus erythematosus
Barbara G
Rheumatic Diseases Clinics of North America null
Contenu apparenté
Instructions
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique
