Seprase Recombinant Protein | SEPR recombinant protein

Recombinant Human Seprase

Cat. Num. AAA9420230

• Gene Names: FAP; FAPA; SIMP; DPPIV; FAPalpha
• Reactivity: Human
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Seprase; Recombinant Human Seprase; 170 kDa melanoma membrane-bound gelatinase2; SEPR recombinant protein

• Host: E Coli
• Reactivity: Human
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: 20mM Tris-HCl based buffer, pH8.0
• Sequence Positions: Full Length, 26-760aa

• Tag Info: GST-tag
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.

Related Product Information for SEPR recombinant protein

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue rodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma mbrane 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 mbrane 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 rodeling 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 syst. 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.

NCBI and Uniprot Product Information

• NCBI GI #: 620597362
• NCBI GeneID: 2191
• NCBI Accession #: NP_001278736.1
• NCBI GenBank Nucleotide #: NM_001291807.2
• UniProt Accession #: Q12884; O00199; Q53TP5; Q86Z29; Q99998; Q9UID4
• Molecular Weight: 112.4kD
• NCBI Official Full Name: prolyl endopeptidase FAP isoform 2
• NCBI Official Synonym Full Names: fibroblast activation protein alpha
• NCBI Official Symbol: FAP
• NCBI Official Synonym Symbols: FAPA; SIMP; DPPIV; FAPalpha
• NCBI Protein Information: prolyl endopeptidase FAP
• UniProt Protein Name: Prolyl endopeptidase FAP
• UniProt Gene Name: FAP
• UniProt Synonym Gene Names: APCE

NCBI Description

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]

Uniprot Description

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 3.4.14.5; EC 3.4.21.26; Membrane protein, integral; Protease

Chromosomal Location of Human Ortholog: 2q24.2

Cellular Component: cell surface; extracellular space; focal adhesion; lamellipodium; plasma membrane

Molecular Function: dipeptidyl-peptidase activity; endopeptidase activity; integrin binding; metalloendopeptidase activity; peptidase activity; protease binding; protein binding; protein homodimerization activity; serine-type endopeptidase activity; serine-type peptidase activity

Biological Process: endothelial cell migration; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of fibrinolysis