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SDS-PAGE

Plasminogen activator inhibitor 1 Recombinant Protein | SERPINE1 recombinant protein

Recombinant Human Plasminogen activator inhibitor 1

Gene Names
SERPINE1; PAI; PAI1; PAI-1; PLANH1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Plasminogen activator inhibitor 1; Recombinant Human Plasminogen activator inhibitor 1; Endothelial plasminogen activator inhibitor; Serpin E1; SERPINE1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Liquid containing glycerol
Sequence Positions
24-401aa; Partial
Sequence
VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVME
Sequence Length
402
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

SDS-PAGE
Related Product Information for SERPINE1 recombinant protein
Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.
Product Categories/Family for SERPINE1 recombinant protein
References
Endothelial plasminogen activator inhibitor (PAI) a new member of the Serpin gene family.Pannekoek H., Veerman H., Lambers H., Diergaarde P., Verweij C.L., van Zonneveld A.-J., van Mourik J.A.EMBO J. 5:2539-2544(1986) Structure of the human plasminogen activator inhibitor 1 gene nonrandom distribution of introns.Loskutoff D.J., Linders M., Keijer J., Veerman H., van Heerikhuizen H., Pannekoek H.Biochemistry 26:3763-3768(1987) cDNA cloning of human plasminogen activator-inhibitor from endothelial cells.Ginsburg D., Zeheb R., Yang A.Y., Rafferty U.M., Andreasen P.A., Nielsen L., Dano K., Lebo R.V., Gelehrter T.D.J. Clin. Invest. 78:1673-1680(1986) Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI-1.Follo M., Ginsburg D.Gene 84:447-453(1989) The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family.Strandberg L., Lawrence D., Ny T.Eur. J. Biochem. 176:609-616(1988) Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences.Bosma P.J., van den Berg E.A., Kooistra T., Siemieniak D.R., Slightom J.L.J. Biol. Chem. 263:9129-9141(1988) Pannekoek H.SeattleSNPs variation discovery resourceComplete 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) The DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003) Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor.Ny T., Sawdey M., Lawrence D., Millan J.L., Loskutoff D.J.Proc. Natl. Acad. Sci. U.S.A. 83:6776-6780(1986) Plasminogen activator inhibitor type-1 reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing.Andreasen P.A., Riccio A., Welinder K.G., Douglas R., Sartorio R., Nielsen L.S., Oppenheimer C., Blasi F., Danoe K.FEBS Lett. 209:213-218(1986) cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell.Wun T.C., Kretzmer K.K.FEBS Lett. 210:11-16(1987) Identification of a PAI-1 binding site in vitronectin.Sigurdardottir O., Wiman B.Biochim. Biophys. Acta 1208:104-110(1994) Human plasminogen activator inhibitor-1 (PAI-1) deficiency characterization of a large kindred with a null mutation in the PAI-1 gene.Fay W.P., Parker A.C., Condrey L.R., Shapiro A.D.Blood 90:204-208(1997) The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein.Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.J. Biol. Chem. 276:28889-28896(2001) Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity.Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.Biochem. J. 390:231-242(2005) Resveratrol-induced changes of the human adipocyte secretion profile.Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., Mariman E.C., Renes J.J. Proteome Res. 11:4733-4743(2012) Structural basis of latency in plasminogen activator inhibitor-1.Mottonen J., Strand A., Symersky J., Sweet R.M., Danley D.E., Geoghegan K.F., Gerard R.D., Goldsmith E.J.Nature 355:270-273(1992) Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1.Aertgeerts K., de Bondt H.L., de Ranter C.J., Declerck P.J.Nat. Struct. Biol. 2:891-897(1995) Interfering with the inhibitory mechanism of serpins crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide.Xue Y., Bjoerquist P., Inghardt T., Linschoten M., Musil D., Sjoelin L., Deinum J.Structure 6:627-636(1998) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion.Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B., Ginsburg D., Lawrence D.A., Read R.J.Structure 7:111-118(1999) Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation.Nar H., Bauer M., Stassen J.M., Lang D., Gils A., Declerck P.J.J. Mol. Biol. 297:683-695(2000) Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer.Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.Electrophoresis 18:686-689(1997) Characterization of single-nucleotide polymorphisms in coding regions of human genes.Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 22:231-238(1999) ErratumCargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 23:373-373(1999) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
46.7 kDa
NCBI Official Full Name
plasminogen activator inhibitor 1
NCBI Official Synonym Full Names
serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1
NCBI Official Symbol
SERPINE1
NCBI Official Synonym Symbols
PAI; PAI1; PAI-1; PLANH1
NCBI Protein Information
plasminogen activator inhibitor 1
UniProt Protein Name
Plasminogen activator inhibitor 1
UniProt Gene Name
SERPINE1
UniProt Synonym Gene Names
PAI1; PLANH1; PAI; PAI-1
UniProt Entry Name
PAI1_HUMAN

NCBI Description

This gene encodes a member of the serine proteinase inhibitor (serpin) superfamily. This member is the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), and hence is an inhibitor of fibrinolysis. Defects in this gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the gene product are associated with thrombophilia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009]

Uniprot Description

SERPINE1: a secreted protein that acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Belongs to the serpin family. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation. Plasma levels of PAI-1 and VCAM-1 together may be useful in predicting post-operative recurrence in patients with colorectal cancer.

Protein type: Secreted; Motility/polarity/chemotaxis; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 7q22.1

Cellular Component: extracellular matrix; extracellular region; extracellular space; plasma membrane

Molecular Function: protease binding; protein binding; receptor binding; serine-type endopeptidase inhibitor activity

Biological Process: angiogenesis; blood coagulation; chronological cell aging; circadian rhythm; defense response to Gram-negative bacterium; extracellular matrix organization and biogenesis; fibrinolysis; gene expression; negative regulation of blood coagulation; negative regulation of cell adhesion mediated by integrin; negative regulation of cell migration; negative regulation of fibrinolysis; negative regulation of smooth muscle cell migration; placenta development; platelet activation; platelet degranulation; positive regulation of angiogenesis; positive regulation of blood coagulation; positive regulation of inflammatory response; positive regulation of interleukin-8 production; positive regulation of receptor-mediated endocytosis; positive regulation of transcription from RNA polymerase II promoter; regulation of cell proliferation; regulation of receptor activity; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway

Disease: Plasminogen Activator Inhibitor-1 Deficiency

Research Articles on SERPINE1

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Product Notes

The SERPINE1 serpine1 (Catalog #AAA1265498) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 24-401aa; Partial. The amino acid sequence is listed below: VHHPPSYVAH LASDFGVRVF QQVAQASKDR NVVFSPYGVA SVLAMLQLTT GGETQQQIQA AMGFKIDDKG MAPALRHLYK ELMGPWNKDE ISTTDAIFVQ RDLKLVQGFM PHFFRLFRST VKQVDFSEVE RARFIINDWV KTHTKGMISN LLGKGAVDQL TRLVLVNALY FNGQWKTPFP DSSTHRRLFH KSDGSTVSVP MMAQTNKFNY TEFTTPDGHY YDILELPYHG DTLSMFIAAP YEKEVPLSAL TNILSAQLIS HWKGNMTRLP RLLVLPKFSL ETEVDLRKPL ENLGMTDMFR QFQADFTSLS DQEPLHVAQA LQKVKIEVNE SGTVASSSTA VIVSARMAPE EIIMDRPFLF VVRHNPTGTV LFMGQVME. It is sometimes possible for the material contained within the vial of "Plasminogen activator inhibitor 1, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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