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Key Documents

SRP5190

Sigma-Aldrich

HSP70, His tagged human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonyme(s) :

HSP70-1, HSP72, HSPA1, HSPA1A, HSPA1B

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About This Item

Numéro CAS:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥70% (SDS-PAGE)

Forme

buffered aqueous glycerol solution

Poids mol.

~70 kDa

Numéro d'accès NCBI

Application(s)

cell analysis

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... HSPA1A(3303)

Description générale

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

Actions biochimiques/physiologiques

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).

Forme physique

Supplied in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

Notes préparatoires

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Code de la classe de stockage

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
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)
Hsp70 accelerates the recovery of nucleolar morphology after heat shock.
Pelham HR
The Embo Journal, 3(13), 3095-3100 (1984)
Polymorphisms in the Hsp70 gene locus are genetically associated with systemic lupus erythematosus
Barbara G
Rheumatic Diseases Clinics of North America null

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