Peptidyl-prolyl cis-trans isomerase A Recombinant Protein | PPIA recombinant protein

Recombinant Human Peptidyl-prolyl cis-trans isomerase A

Cat. Num. AAA717065

• Gene Names: PPIA; CYPA; CYPH; HEL-S-69p
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Peptidyl-prolyl cis-trans isomerase A; Recombinant Human Peptidyl-prolyl cis-trans isomerase A; Cyclophilin A; Cyclosporin A-binding protein; Rotamase A; PPIA recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-165. Full length of the mature protein.
• Sequence: VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
• Sequence Length: 165

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for PPIA recombinant protein

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

Product Categories/Family for PPIA recombinant protein

Immunology

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 665821274
• NCBI GeneID: 5478
• NCBI Accession #: NP_001287910.1
• NCBI GenBank Nucleotide #: NM_001300981.1
• UniProt Accession #: P62937; P05092; Q3KQW3; Q567Q0; Q6IBU5; Q96IX3; Q9BRU4; Q9BTY9; Q9UC61; A8K220
• Molecular Weight: 17.9 kDa
• NCBI Official Full Name: peptidyl-prolyl cis-trans isomerase A isoform 2
• NCBI Official Synonym Full Names: peptidylprolyl isomerase A
• NCBI Official Symbol: PPIA
• NCBI Official Synonym Symbols: CYPA; CYPH; HEL-S-69p
• NCBI Protein Information: peptidyl-prolyl cis-trans isomerase A
• UniProt Protein Name: Peptidyl-prolyl cis-trans isomerase A
• Protein Family: Peptidyl-prolyl cis-trans isomerase
• UniProt Gene Name: PPIA
• UniProt Synonym Gene Names: CYPA; PPIase A
• UniProt Entry Name: PPIA_HUMAN

NCBI Description

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]

Uniprot Description

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