IMMUNOPHILINS

PROTEINS

SE-105
Cyclophilin A (Human, recombinant)
Peptidylproline cis-trans-isomerase
>90% SDS-PAGE, (EC 5.2.1.8) MW=18 kDa, Storage: 4°C
Expressed in E. coli. Supplied in 20 mM Tris-HCl, pH 7.8. Catalyzes the cis-trans-isomeration of X-Pro-peptide bonds. Protein folding which is limited by the isomeration of X-Pro-peptide bonds can be accelerated by cyclophilin A. Also binds to cyclosporins^1,2.
100 µg
5 x 100 µg


IMMUNOPHILIN LIGANDS

See "Calcineurin" for related reagents

A-165
Ascomycin
>95%, MW=792.0 [11011-38-4] Storage: -20°C
Ascomycin is a close structural analog of FK506³ and is a potent immunosuppressant. It binds to FKBP (FK506-binding protein) and suppresses its proline rotamase activity. The ascomycin-FKBP complex inhibits calcineurin, a type 2B phosphatase^1,4
1 mg
5 x 1 mg
NEW LOWER PRICE

A-195
Cyclosporin A
>98%, MW=1202.6 [59865-13-3] Storage: -20°C
Cyclosporin A (CsA) is an immunosuppressant that has revolutionized organ transplantation through its use in the prevention of graft rejection. CsA binds to cyclophilin and suppresses its proline rotamase activity. The CsA-cyclophilin complex inhibits calcineurin, a type 2B phosphatase^1,4.
100 mg
500 mg

A-275
Rapamycin
98%, MW=914.2 [53123-88-9] Storage: -20°C
Rapamycin is one member of a family of macrolide immunosuppressants which bind to and inhibit the FK506 binding protein (FKBP) proline rotamase⁵. Rapamycin is bound simultaneously by FKBP12 and FRAP (FKBP12-Rapamycin-Associated-Protein)⁶. FRAP (RAFT1) is a 289 kDa protein with homology to PI 4- and PI 3-kinases^7,8, which has PI 4-kinase⁹ and autophosphorylating¹⁰ activities. The rapamycin/FKBP complex does not inhibit the FRAP PI 4-kinase activity⁹, but does inhibit FRAP autophosphorylation¹⁰. Rapamycin is unique in its ability to inhibit lymphokine induced cell proliferation at the G1 to S phase^11,12. It irreversibly arrests Saccharomyces cerevisiae cells in the G1 phase¹³. Rapamycin selectively blocks signalling leading to the activation of p70/85 S6 kinase^14,15,16, an effect which may be due to inhibition of FRAP autophosphorylation or protein kinase activity¹⁰.
1 mg
5 mg
NEW LOWER PRICE

ANTIBODIES

SA-133
Anti-Cyclophilin 40, C-terminal
Rabbit polyclonal antibody. Immunogen: C-terminal human cyclophilin 40 (356-370) peptide^17,18. Supplied as serum. Recognizes cyclophilin 40 kDa protein in yeast, human, and rat tissue. Does not cross-react with cyclophilin 18. Applications: WB 1/1000, IP.
100 µl

SA-134
Anti-Cyclophilin 40, whole protein
Rabbit polyclonal antibody. Immunogen: Recombinant cyclophilin 40 expressed in E. coli^17,18. Supplied as serum. Specific to cyclophilin 40 in human and rat tissue. Does not cross-react with cyclophilin 18. Applications: WB 1/1000.
100 µl

SA-135
Anti-Cyclophilin A
Rabbit polyclonal antibody. Immunogen: Recombinant human cyclophilin A expressed in E. coli. Supplied as serum. Recognizes human, rat, and mouse cyclophilin A 18 kDa protein. Slight cross-reaction to cyclophilin B and C. Applications: WB 1/1000.
100 µl

SA-218
Anti-FKBP12
Rabbit polyclonal antibody. Immunogen: Human FKBP12 (1-13) peptide. Supplied as peptide affinity purified IgG. Recognizes FKBP12 in human, rat, and mouse. Does not crossreact with FKBP13, 25 or 56. Applications: WB 1/2000, IH 1/500 and IP.
100 µl

SA-136
Anti-FKBP59/HSP56
Rabbit polyclonal antibody. Immunogen: C-terminal 19 amino acid peptide sequence of FKBP59/HSP56^19,20. Supplied as purified IgG, lyophilized. Recognizes human, mouse, and rabbit 52 kDa protein. Applications: WB 1 µg/ml.
100 µg


REFERENCES

1. J. Kunz and M.M. Hall Trends in Biochem. Sci. 1993 18 334

2. D.A. Fruman et al. FASEB J. 1994 8 391

3. K.K. Wallace et al. J. Am. Chem. Soc. 1994 116 11600

4. J. Liu and M.N. Hall Trends Pharmacol. Sci. 1993 14 182

5. J.Y. Chang et al. Trends Pharmacol. Sci. 1991 12 218

6. J. Choi et al. Science 1996 273 183

7. E.J. Brown et al. Nature 1994 369 756

8. D.M. Sabatini et al. Cell 78 35

9. D.M. Sabatini et al. J. Biol. Chem. 1995 270 20875

10. E.J. Brown et al. Nature 1995 377 441

11. J.E. Kay et al. Immunology 1991 72 544

12. W.G. Morice et al. J. Biol. Chem. 1993 268 3734

13. J. Heitman et al. Science 1991 253 905

14. D.J. Price et al. Science 1992 257 973

15. D.C. Fingar et al. J. Biol. Chem. 1993 268 3005

16. J. Chung et al. Cell 1992 69 1227

17. L. Kieffer et al. J. Biol. Chem. 1992 267 5503

18. L. Kieffer et al. J. Biol. Chem. 1993 268 12303

19. M.C. Lebeau et al. J. Biol. Chem. 1992 267 4281

20. V.A. Ruff et al. J. Biol. Chem. 1992 267 21285