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Peptidyl-Prolyl Cis-Trans Isomerase A (PPIA) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS717065

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

$315 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Peptidyl-prolyl cis-trans isomerase A (PPIA), Recombinant Protein
Full Product Name
Recombinant Human Peptidyl-prolyl cis-trans isomerase A
Product Gene Name
Product Synonym Gene Name
CYPA
Product Synonym Names
Cyclophilin A; Cyclosporin A-binding protein; Rotamase A
Sequence
VNPTVFFDIA VDGEPLGRVS FELFADKVPK TAENFRALST GEKGFGYKGS CFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFEDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMNIVEA MERFGSRNGK TSKKITIADC GQLE
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Matching Pairs
Antibody: PPIA (MBS7041918)
Standard: Peptidyl-prolyl cis-trans isomerase A (MBS717065)
Comments: Standards are recommendations only. Compatibility of the standards in the user developed application needs to be established and confirmed by the researcher.
Molecular Weight
17.9 kDa
Sequence Positions
2-165aa; Full Length of Mature Protein
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
123840
3D Structure
ModBase 3D Structure for P62937

Product Categories/Family for PPIA recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for PPIA recombinant protein

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)

Other Notes

Small volumes of PPIA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for PPIA purchase

MBS717065 is a recombinant protein targeting PPIA. Also known as Recombinant Human Peptidyl-prolyl cis-trans isomerase A. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for PPIA. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Peptidyl-prolyl cis-trans isomerase A
UniProt Synonym Protein Names
Cyclophilin A; Cyclosporin A-binding protein; Rotamase A
UniProt Gene Name
PPIA
UniProt Synonym Gene Names
CYPA; PPIase A
UniProt Entry Name
PPIA_HUMAN
NCBI Protein Information
peptidyl-prolyl cis-trans isomerase A

NCBI Summary for PPIA

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]
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UniProt Comments for PPIA

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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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