HSP60 Recombinant Protein Antigen

• Reactivity: Hu
• Applications: AC

HSP60 Recombinant Protein Antigen Summary

• Description: A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human HSP60.

  Source: E. coli

  Amino Acid Sequence: KGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGL

  Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

  This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions.

• Source: E. coli
• Protein/Peptide Type: Recombinant Protein Antigen
• Gene: HSPD1
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Applications/Dilutions

• Dilutions:
  • Antibody Competition 10 - 100 molar excess
• Application Notes: This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-55503.

  It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.

  For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com

• Theoretical MW: 32 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 -20C. Avoid freeze-thaw cycles.
• Buffer: PBS and 1M Urea, pH 7.4.
• Preservative: No Preservative
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Alternate Names for HSP60 Recombinant Protein Antigen

• 60 kDa chaperonin
• Chaperonin 60
• cpn60
• GROEL
• heat shock 60kD protein 1 (chaperonin)
• heat shock 60kDa protein 1 (chaperonin)
• Heat shock protein 60
• heat shock protein 65
• HLD4
• HSP60
• HSP-60
• HSP60SPG13
• HSP65
• HSPD1
• HuCHA60
• Mitochondrial matrix protein P1,60 kDa heat shock protein, mitochondrial
• P60 lymphocyte protein
• short heat shock protein 60 Hsp60s1
• spastic paraplegia 13 (autosomal dominant)
• SPG13

Background

Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60 and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years) and this fact together with the high degree of homology between the divergent Hsp60s would indicate that these proteins carry out a primitive but important function which is similar to all of these different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of magnesium ions and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures. These similarities are supported by recent studies where the single ring human mitochondrial homolog, Hsp60 with its co chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Data demonstrates that recombinant Hsp60 and Hsp10 have been shown to accelerate the activation of procaspase 3 by cytochrome c and dATP in an ATP dependent manner. Hsps are intracellular proteins which are thought to serve protective functions against infection and cellular stress, however several recent studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, arthrosclerosis and chlamydial disease.

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.

Bioinformatics

• Gene Symbol: HSPD1