Pregnancy zone Recombinant Protein | PZP recombinant protein

Recombinant Human Pregnancy zone protein, partial

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Pregnancy zone; Recombinant Human Pregnancy zone protein; partial; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6; PZP 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: 472-821. Partial of Isoform 2
• Sequence: MKPEAELSVSSVYNLLTVKDLTNFPDNVDQQEEEQGHCPRPFFIHNGAIYVPLSSNEADIYSFLKGMGLKVFTNSKIRKPKSCSVIPSVSAGAVGQGYYGAGLGVVERPYVPQLGTYNVIPLNNEQSSGPVPETVRSYFPETWIWELVAVNSSGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEVFTLKATVLNYLPKCIRAEGIEQEKTFSSMTCASGANVSEQLSLKLPSNVVKESARASFSVLGDILGSAMQNIQNLLQMPYGCGEQNMVLFAPNIYVLNYLNETQQLTQEIKAKAVGYLITGYQRQLNYKHQDGSYSTFG

• 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 PZP recombinant protein

Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme rains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.

Product Categories/Family for PZP recombinant protein

Neuroscience

References

Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP cDNA clone by the polymerase chain reaction.Devriendt K., van den Berghe H., Cassiman J.-J., Marynen P.Biochim. Biophys. Acta 1088:95-103(1991) The finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Alpha-macroglobulin domain structure studied by specific limited proteolysis.Thomsen N.K., Sottrup-Jensen L.Arch. Biochem. Biophys. 300:327-334(1993) A genetic polymorphism in a functional domain of human pregnancy zone protein the bait region. Genomic structure of the bait domains of human pregnancy zone protein and alpha 2 macroglobulin.Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.FEBS Lett. 262:349-352(1990) The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins.Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H.J. Biol. Chem. 264:15781-15789(1989) Characterization of human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L.J. Biol. Chem. 260:15723-15735(1985) A cluster of alpha 2-macroglobulin-related genes (alpha 2 M) on human chromosome 12p cloning of the pregnancy-zone protein gene and an alpha 2M pseudogene.Devriendt K., Zhang J., van Leuven F., van den Berghe H., Cassiman J.-J., Marynen P.Gene 81:325-334(1989) Pregnancy zone protein, a proteinase-binding macroglobulin. Interactions with proteinases and methylamine.Christensen U., Simonsen M., Harrit N., Sottrup-Jensen L.Biochemistry 28:9324-9331(1989) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) 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) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 281185515
• UniProt Accession #: P20742; Q15273; Q2NKL2; Q7M4N7; A6ND27
• Molecular Weight: 42.3 kDa
• NCBI Official Full Name: Pregnancy zone protein
• UniProt Protein Name: Pregnancy zone protein
• UniProt Gene Name: PZP
• UniProt Synonym Gene Names: CPAMD6
• UniProt Entry Name: PZP_HUMAN