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Chaperonin 10 (Cpn10, Heat Shock Protein 10, HSP10)

Chaperonin 10 (Cpn10, Heat Shock Protein 10, HSP10)

Cat no: C3470-01A

Supplier: United States Biological
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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. Applications: 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 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.
Catalogue number: C3470-01A
Reactivities: Human, Mouse, Rat, Bovine, Canine, Guinea Pig, Porcine, Rabbit, Sheep, Xenopus/Amphibian
Hosts: Rabbit
Applications: Immunohistochemistry, Immunoprecipitation, Western Blot
Size: 50ul
Form: Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.
P type: Pab
Isotype: IgG
Purity: Purified by Protein A chromatography.
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.

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