catalog number :
MBS143556
products type :
Recombinant Protein
products full name :
Recombinant Human Fibroblast Activation Protein Alpha
products short name :
Fibroblast Activation Protein Alpha
products name syn :
Seprase Human; Fibroblast Activation Protein Alpha Human Recombinant; 170 kDa melanoma membrane-bound gelatinase; DKFZp686G13158; DPPIV; FAPA; Fibroblast activation protein alpha; Integral membrane serine protease; Seprase; FAP; Seprase
other names :
prolyl endopeptidase FAP isoform 2; Prolyl endopeptidase FAP; prolyl endopeptidase FAP; 170 kDa melanoma membrane-bound gelatinase; FAPalpha; dipeptidyl peptidase FAP; gelatine degradation protease FAP; integral membrane serine protease; post-proline cleaving enzyme; seprase; serine integral membrane protease; surface-expressed protease; fibroblast activation protein, alpha; 170 kDa melanoma membrane-bound gelatinase; Dipeptidyl peptidase FAP; Fibroblast activation protein alpha; Gelatine degradation protease FAP; Integral membrane serine protease; Post-proline cleaving enzyme; Surface-expressed protease;
other gene names :
FAP; FAP; FAPA; SIMP; DPPIV
uniprot entry name :
SEPR_HUMAN
form :
Seprase is supplied in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol. Sterile Filtered clear solution (0.1mg/ml).
storage stability :
Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. Please avoid freeze thaw cycles.
products categories :
ENZYMES; Enzymes
products description :
Description: Seprase Human Recombinant produced in E Coli is single, a non-glycosylated, Polypeptide chain containing 203 amino acids (559-761 a.a.) and having a total Mw of 48kDa. Seprase is fused to a GST tag and is purified by proprietary chromatographic techniques. Introduction: Seprase is a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts. Seprase is a homodimeric integral membrane gelatinase, which is part of the serine protease family. Seprase is expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. Seprase protein has a role in the control of fibroblast growth or epithelial-mesenchymal interactions throughout development, tissue repair, and epithelial carcinogenesis.
ncbi acc num :
NP_001278736.1
ncbi gb acc num :
NM_001291807.1
ncbi summary :
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 summary :
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: Membrane protein, integral; EC 3.4.21.26; EC 3.4.14.5; Protease. Chromosomal Location of Human Ortholog: 2q23. Cellular Component: extracellular space; focal adhesion; cell surface; apical part of cell; lamellipodium; cytoplasm; integral to membrane; plasma membrane. Molecular Function: protein dimerization activity; peptidase activity; integrin binding; protein binding; protein homodimerization activity; protease binding; dipeptidyl-peptidase activity; serine-type peptidase activity; metalloendopeptidase activity; serine-type endopeptidase activity; endopeptidase activity. Biological Process: proteolysis involved in cellular protein catabolic process; endothelial cell migration; angiogenesis; cell adhesion; proteolysis; regulation of fibrinolysis