Recombinant E. coli HSP70/HSPA1A Protein

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SDS-Page: Hsp70 Protein [NBC1-18358] - Dna K, 41.6kDa (384aa) with a purity of 95% by SDS - PAGE

Product Details

Summary
Reactivity EcSpecies Glossary
Applications PAGE
Concentration
1 mg/ml

Order Details

Recombinant E. coli HSP70/HSPA1A Protein Summary

Description
An un-tagged recombinant protein corresponding to the amino acids 1-384 of E.coli HSP70/HSPA1A

Source: E.coli

Amino Acid Sequence: MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTG

Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
HSPA1A
Purity
>95% pure by SDS-PAGE

Applications/Dilutions

Theoretical MW
41.6 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
25 mM Tris-HCl, pH7.5, 100 mM NaCl, 5 mM DTT, 10% glycerol
Preservative
No Preservative
Concentration
1 mg/ml
Purity
>95% pure by SDS-PAGE

Alternate Names for Recombinant E. coli HSP70/HSPA1A Protein

  • dnaK-type molecular chaperone HSP70-1
  • FLJ54303
  • FLJ54370
  • FLJ54392
  • FLJ54408
  • FLJ75127
  • Heat shock 70 kDa protein 1/2
  • heat shock 70 kDa protein 1A/1B
  • heat shock 70kD protein 1A
  • heat shock 70kDa protein 1A
  • heat shock-induced protein
  • HSP70
  • HSP70.1/HSP70.2
  • HSP70-1
  • HSP70-1/HSP70-2
  • HSP70-1A
  • HSP70I
  • HSP72
  • HSPA1
  • HSPA1A
  • HSPA1B

Background

DnaK, originally identified for its DNA replication by bacteriophage lambda in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain(residues385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol HSPA1A
Entrez