FAP protein Active Protein | FAP active protein

Recombinant Mouse FAP protein (His Tag)

Cat. Num. AAA2569381

• Gene Names: Fap; SIMP
• Purity: >90% as determined by reducing SDS-PAGE
• Synonyms: FAP protein; Recombinant Mouse FAP protein (His Tag); 170kDa melanoma membrane bound gelatinase; 170kDa melanoma membrane-bound gelatinase; DPPIV; FAP; FAPA; Fibroblast activation protein alpha; Integral membrane serine protease; SEPR; Seprase; FAPalpha; SIMP; FAP active protein

• Host: E Coli
• Purity/Purification: >90% as determined by reducing SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4
• Sequence: 26L-349G

• Species: Mouse
• Tag: N/C-His
• Protein Construction: A DNA sequence encoding the Mouse FAP protein (P97321)(26L-349G) was expressed with a polyhistidine tag at the N-terminus.
• Activity: Immunogen (E-AB-40349)
• Preparation and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80 degree C. Reconstituted protein solution can be stored at 4-8 degree C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.; This product is provided as lyophilized powder which is shipped with ice packs.

SDS-Page

Related Product Information for FAP active protein

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).

NCBI and Uniprot Product Information

• NCBI GI #: 6679749
• NCBI GeneID: 14089
• NCBI Accession #: NP_032012.1
• NCBI GenBank Nucleotide #: NM_007986.3
• UniProt Accession #: P97321
• Molecular Weight: 84,096 Da
• NCBI Official Full Name: prolyl endopeptidase FAP
• NCBI Official Synonym Full Names: fibroblast activation protein
• NCBI Official Symbol: Fap
• NCBI Official Synonym Symbols: SIMP
• NCBI Protein Information: prolyl endopeptidase FAP
• UniProt Protein Name: Prolyl endopeptidase FAP
• Protein Family: Prolyl endopeptidase
• UniProt Gene Name: Fap
• UniProt Synonym Gene Names: APCE

NCBI Description

This gene belongs to the serine protease family. The encoded protein is an inducible cell-surface bound glycoprotein specifically expressed in tumor-associated fibroblasts and pericytes of epithelial tumors and has protease and gelatinase activity. The protein plays a role in remodeling of the extracellular matrix (ECM) and may affect tumorigenesis and tissue repair. Alternately spliced transcript variants of this gene are described in the literature (PMID 9139873), but the full-length sequence of these variants is not available. [provided by RefSeq, Apr 2013]

Uniprot Description

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.