protein

Recombinant Human Peptidyl-prolyl cis-trans isomerase A

MBS717065

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Peptidyl-prolyl cis-trans isomerase A

Peptidyl-prolyl cis-trans isomerase A

Cyclophilin A; Cyclosporin A-binding protein; Rotamase A

peptidyl-prolyl cis-trans isomerase A isoform 2; Peptidyl-prolyl cis-trans isomerase A; peptidyl-prolyl cis-trans isomerase A; peptidylprolyl isomerase A; Cyclophilin A; Cyclosporin A-binding protein; Rotamase A

PPIA

CYPA

PPIA; PPIA; CYPA; CYPH; HEL-S-69p; CYPA; PPIase A

PPIA_HUMAN

E Coli

2-165

105

VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS
TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAK
TEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKIT
IADCGQLE

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Complementary DNA for human T-cell cyclophilin.Haendler B., Hofer-Warbinek R., Hofer E.EMBO J. 6:947-950(1987) Characterization of the human cyclophilin gene and of related processed pseudogenes.Haendler B., Hofer E.Eur. J. Biochem. 190:477-482(1990) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H., Wuethrich K., Walkinshaw M.D.Nature 353:276-279(1991) Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution.Ke H., Zydowsky L.D., Liu J., Walsh C.T.Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991) X-ray structure of a decameric cyclophilin-cyclosporin crystal complex.Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M., Walkinshaw M.D.Nature 361:91-94(1993) X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution.Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.J. Mol. Biol. 234:1119-1130(1993) Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.Zhao Y., Ke H.Biochemistry 35:7356-7361(1996) Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.Protein Sci. 6:2297-2307(1997) X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.Kallen J., Mikol V., Taylor P., Walkinshaw M.D.J. Mol. Biol. 283:435-449(1998) Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002) Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin.Jin L., Harrison S.C.Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002) Solution structure of the cyclosporin A/cyclophilin complex by NMR.Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T., Holzman T.F., Simmer R.L., Fesik S.W.Nature 361:88-91(1993) The NMR solution conformation of unligated human cyclophilin A.Ottiger M., Zerbe O., Guentert P., Wuethrich K.J. Mol. Biol. 272:64-81(1997) Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.Lammers M., Neumann H., Chin J.W., James L.C.Nat. Chem. Biol. 6:331-337(2010)

665821274

NP_001287910.1

NM_001300981.1

P62937

45.3kD

APOBEC3G Mediated Resistance To HIV-1 Infection Pathway (1269097); Assembly Of The HIV Virion Pathway (1269086); Basigin Interactions Pathway (1269376); Binding And Entry Of HIV Virion Pathway (1269060); Budding And Maturation Of HIV Virion Pathway (1269090); Cell Surface Interactions At The Vascular Wall Pathway (1269373); Disease Pathway (1268854); Early Phase Of HIV Life Cycle Pathway (1269059); HIV Infection Pathway (1269057); HIV Life Cycle Pathway (1269058)

This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported. [provided by RefSeq, Jul 2008]

PPIA: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Interacts with HIV-1 Capsid protein. Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Protein type: Isomerase; EC 5.2.1.8; RNA-binding; Cyclophilin. Chromosomal Location of Human Ortholog: 7p13. Cellular Component: cytosol; extracellular region; extracellular space; focal adhesion; membrane; nucleus. Molecular Function: peptide binding; peptidyl-prolyl cis-trans isomerase activity; protein binding; unfolded protein binding; virion binding. Biological Process: blood coagulation; entry into host cell; leukocyte migration; platelet activation; platelet degranulation; positive regulation of protein secretion; positive regulation of viral genome replication; protein folding; protein peptidyl-prolyl isomerization; regulation of viral genome replication; release of virus from host; RNA-dependent DNA replication; uncoating of virus; viral infectious cycle; viral reproduction; virus assembly

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180