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.\n\nApplications: \nSuitable for use in RID, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.\n\nRecommended Dilution:\nRID: 1:100,000\nWestern Blot: 1:2000-1:5000\nImmunoprecipitation: 1:100\nImmunohistochemistry: 1:400\nOptimal dilutions to be determined by the researcher.\n\nPositive Controls: \nH1838-01: HeLa Heat Shocked Cell Lysate\nC3450: Recombinant Human Chaperonin 10 Protein\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. 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.

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SPECIFICATIONS

Catalog Number

C3470-01A

Size

50ul

Applications

IHC, IP, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat, Bov, Can, GP, Prc, Rabbit, Sheep, Xen/Amph

Form

Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.

P Type

Pab

Purity

Purified by Protein A chromatography.

Isotype

IgG

References

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).

Additional Info

Recognizes human Chaperonin 10 at ~10kD. Species Crossreactivity: mouse, rat, Xenopus laevis, bovine, canine, guinea pig, porcine, rabbit and sheep.