SRP5190
HSP70, His tagged human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Sinonimo/i:
HSP70-1, HSP72, HSPA1, HSPA1A, HSPA1B
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About This Item
Prodotti consigliati
Origine biologica
human
Ricombinante
expressed in baculovirus infected Sf9 cells
Saggio
≥70% (SDS-PAGE)
Forma fisica
buffered aqueous glycerol solution
PM
~70 kDa
N° accesso NCBI
applicazioni
cell analysis
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Informazioni sul gene
human ... HSPA1A(3303)
Descrizione generale
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.
Applicazioni
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
Azioni biochim/fisiol
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).
Stato fisico
Supplied in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.
Nota sulla preparazione
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Codice della classe di stoccaggio
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate.
Zhang P, et.al
PLoS ONE, 9(7), e103518-e103518 (2014)
Putative model for heat shock protein 70 complexation with receptor of advanced glycation end products through fluorescence proximity assays and normal mode analyses
Marcelo Sartori Grunwald
Cell Stress & Chaperones (2017)
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
H R Pelham
The EMBO journal, 3(13), 3095-3100 (1984-12-20)
The major heat-shock protein, hsp70, is synthesized by cells of many organisms in response to stress. In the present study, Drosophila hsp70 was expressed from cloned genes in mouse L cells and monkey COS cells and detected by immunofluorescence using
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)
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