Technical Data
Chaperonin 10 (Cpn10, Heat Shock Protein 10, HSP10)
Homologs of E. coli Chaperonin 10 make up a family of small heat shock proteins with an approximate molecular mass of 10kD (Hsp10s). Chaperonin 10 acts as a co-chaperone and interacts with members of the Hsp60 family (GroEL in E. coli) to promote proper folding of polypeptides. In chlamydia, Chaperonin 10 is thought to interact with cHsp60, a reported immunopathological antigen, identifying Chaperonine 10 as a potential contributor to an immunological response.

Suitable for use in RID, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
RID: 1:100,000
Western Blot: 1:2000-1:5000
Immunoprecipitation: 1:100
Immunohistochemistry: 1:400
Optimal dilutions to be determined by the researcher.

Positive Controls:
H1838-01: HeLa Heat Shocked Cell Lysate
C3450: Recombinant Human Chaperonin 10 Protein

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
50ul4C (-20C Glycerol)Blue IceHumanRabbit
Synthetic peptide corresponding to aa 92-102 RDGDILGKYVD of human Cpn10 (KLH). Cellular Localization: Mitochondria.
Purified by Protein A chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.
Recognizes human Chaperonin 10 at ~10kD. Species Crossreactivity: mouse, rat, Xenopus laevis, bovine, canine, guinea pig, porcine, rabbit and sheep.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1.Ruepp SU et al. Genomics and proteomics analysis of acetaminophen toxicity in mouse liver. Toxicol Sci 65:135-50 (2002). 2. Ravagnan L et al. Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat Cell Biol 3:839-43 (2001). 3. Samali A et al. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J 18:2040-8 (1999). 4. Gething MJ & Sambrook J Protein folding in the cell. Nature 355:33-45 (1992). 5. Gatenby AA et al. Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria. Trends Biotechnol 8:354-8 (1990). 6. Hemmingsen SM et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333:330-4 (1988).7. Morton H et al. Immunosuppression detected in pregnant mice by rosette inhibition test. Nature 249:459-60 (1974).