product summary
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company name :
MyBioSource
product type :
protein
product name :
HSP70 recombinant protein
catalog :
MBS515090
quantity :
0.02 mg
price :
260 USD
more info or order :
product information
catalog number :
MBS515090
products type :
Recombinant Protein
products full name :
HSP70 recombinant protein
products short name :
HSP70
products name syn :
HSPA1A; HSP70-1; HSP72; HSPA1; HSPA1B. DAQB-147D11.1
other names :
Homo sapiens heat shock 70kDa protein 1A (HSPA1A), mRNA; Heat shock 70 kDa protein 1A/1B; heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70 kDa protein 1/2; dnaK-type molecular chaperone HSP70-1; heat shock 70kDa protein 1A; Heat shock 70 kDa protein 1/2
products gene name :
HSP70
products gene name syn :
HSPA1A; HSP70-1; HSP72; HSPA1; HSPA1B. DAQB-147D11.1
other gene names :
HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HSPA1; HSX70; HSP70-1/HSP70-2
uniprot entry name :
HSP71_HUMAN
host :
E Coli
sequence length :
2445
purity :
>90%
form :
50mM Tris-HCl, pH 7.5, 150mM NaCl, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
concentration :
0.2 ug/ul
storage stability :
Store product at -70 degree C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles. Stability: 1 year at -70 degree C from date of shipment.
tested application :
ATPase Assay, Western Blot (WB)
other info1 :
Type: Recombinant Fusion Protein. Species: Human. Tag Information: GST tag. Expression System: E.coli. Source Note: Recombinant full-length human HSP70 was expressed in E. coli cells. Accession Number: NM 005345
products categories :
Cell Stress & Chaperone Proteins; Signaling Proteins - Cell Stress & Chaperone Proteins
products description :
Recombinant full-length human HSP70 was expressed in E. coli cells using an N-terminal GST tag. Scientific Background: HSP70 is a member of the heat shock protein family and is synthesized by cells of many organisms in response to stress (1). HSP70 is found mostly but not exclusively in the nucleus of unstressed cells. For several hours after a short heat shock, however, it is strongly concentrated in nucleoli (2). Nucleoli are transiently damaged by such a heat shock: their morphology changes and assembly and export of ribosomes is blocked for several hours. HSP70 helps to stabilize the morphological changes of the nucleoli.
products references :
1. Moran, L A. et al: The major heat-shock protein (hsp70) gene family: related sequences in mouse, Drosophila, and yeast. Can J Biochem Cell Biol. 1983 Jun;61(6):488-99. 2. Pelham, H R: Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J. 1984 Dec 20;3(13):3095-100.
ncbi gi num :
194248071
ncbi acc num :
NP_005336.3
ncbi gb acc num :
NM_005345
uniprot acc num :
P08107
ncbi mol weight :
~96 kDa
ncbi pathways :
Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Apoptosis Modulation By HSP70 Pathway (198877); Direct P53 Effectors Pathway (137939); Endocytosis Pathway (102279); Endocytosis Pathway (102181); Epstein-Barr Virus Infection Pathway (585562); Epstein-Barr Virus Infection Pathway (587115); Estrogen Signaling Pathway (799177); Estrogen Signaling Pathway (799197)
ncbi summary :
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]
uniprot summary :
Function: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Ref.20. Subunit structure: Component of the CatSper complex . By similarity. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts with METTL21A. Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.26 Ref.29 Ref.30. Subcellular location: Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.21. Tissue specificity: HSPA1B is testis-specific. Induction: By heat shock. Sequence similarities: Belongs to the heat shock protein 70 family.
size1 :
0.02 mg
price1 :
260 USD
size2 :
0.05 mg
price2 :
415
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

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