protein

Recombinant Human Seprase

MBS1265618

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Seprase

Seprase

170 kDa melanoma membrane-bound gelatinase2

Prolyl endopeptidase FAP; prolyl endopeptidase FAP; fibroblast activation protein alpha; 170 kDa melanoma membrane-bound gelatinase

FAP

FAP; FAP; FAPA; SIMP; DPPIV; APCE

SEPR_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

26-760

239

LRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISG
QEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNY
GLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVR
GNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPF
QITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKF
LAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKN
PVVRIFIIDTTYPAYVGPQEV

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.

Cancer

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.

Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers.Scanlan M.J., Raj B.K.M., Calvo B., Garin-Chesa P., Sanz-Moncasi M.P., Healey J.H., Old L.J., Rettig W.J.Proc. Natl. Acad. Sci. U.S.A. 91:5657-5661(1994) Molecular cloning of seprase a serine integral membrane protease from human melanoma.Goldstein L.A., Ghersi G., Pineiro-Sanchez M.L., Salamone M., Yeh Y., Flessate D., Chen W.-T.Biochim. Biophys. Acta 1361:11-19(1997) Identification of the 170-kDa melanoma membrane-bound gelatinase (seprase) as a serine integral membrane protease.Pineiro-Sanchez M.L., Goldstein L.A., Dodt J., Howard L., Yeh Y., Chen W.-T.J. Biol. Chem. 272:7595-7601(1997) Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform.Goldstein L.A., Chen W.-T.J. Biol. Chem. 275:2554-2559(2000) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)

NP_001278736.1

Q12884

112.4kD

The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014]

FAP: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers. Belongs to the peptidase S9B family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: EC 3.4.21.26; Protease; Membrane protein, integral; EC 3.4.14.5. Chromosomal Location of Human Ortholog: 2q23. Cellular Component: apical part of cell; cell surface; cytoplasm; extracellular space; focal adhesion; integral to membrane; lamellipodium; plasma membrane. Molecular Function: dipeptidyl-peptidase activity; endopeptidase activity; integrin binding; metalloendopeptidase activity; peptidase activity; protease binding; protein binding; protein dimerization activity; protein homodimerization activity; serine-type endopeptidase activity; serine-type peptidase activity. Biological Process: angiogenesis; cell adhesion; endothelial cell migration; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of fibrinolysis

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

950

0.5 mg (Yeast)

950