protein

Recombinant Human Pregnancy zone protein

MBS948491

0.05 mg (E-Coli)

185 USD

Recombinant Protein

Recombinant Human Pregnancy zone protein

Pregnancy zone

C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6

Pregnancy zone protein; Pregnancy zone protein; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6

PZP

CPAMD6

PZP; CPAMD6

PZP_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

472-821

1482

MKPEAELSVSSVYNLLTVKDLTNFPDNVDQQEEEQGHCP
RPFFIHNGAIYVPLSSNEADIYSFLKGMGLKVFTNSKIR
KPKSCSVIPSVSAGAVGQGYYGAGLGVVERPYVPQLGTY
NVIPLNNEQSSGPVPETVRSYFPETWIWELVAVNSSGVA
EVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQP
FFVELTMPYSVIRGEVFTLKATVLNYLPKCIRAEGIEQE
KTFSSMTCASGANVSEQLSLK

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Neuroscience

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.

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)

281185515

P20742.4

P20742

42.3kD

PZP: 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 remains 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. Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Secreted, signal peptide; Secreted. Chromosomal Location of Human Ortholog: 12p13-p12.2. Cellular Component: extracellular region. Molecular Function: endopeptidase inhibitor activity; serine-type endopeptidase inhibitor activity. Biological Process: female pregnancy

0.05 mg (E-Coli)

185 USD

0.2 mg (E-Coli)

420

0.5 mg (E-Coli)

680

1 mg (E-Coli)

1070