Saltar al contenido
Merck

SRP5190

Sigma-Aldrich

HSP70, His tagged human

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

Sinónimos:

HSP70-1, HSP72, HSPA1, HSPA1A, HSPA1B

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

Número de CAS:
UNSPSC Code:
12352200
NACRES:
NA.32

biological 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

Pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

Storage Class

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

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico