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SRP5190

HSP70, His tagged human

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

Synonym(s):

HSP70-1, HSP72, HSPA1, HSPA1A, HSPA1B

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About This Item

CAS Number:
2071612-66-1
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
buffered aqueous glycerol solution
Assay:
≥70% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
Mol wt:
~70 kDa

Key Documents

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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.

NM_005345

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HSPA1A(3303)

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).

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.

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
GHS08,GHS07

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

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

288-32-4

CAS No.

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Certificates of Analysis (COA)

Lot/Batch Number
R087-1

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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)
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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