
- Species ReactivityHuman
- SpecificityDetects human Fibroblast Activation Proteinalpha /FAP in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human DPP6 is observed.
- SourceMonoclonal Mouse IgG1 Clone # 427819
- PurificationProtein A or G purified from hybridoma culture supernatant
- ImmunogenS. frugiperda insect ovarian cell line Sf 21-derived recombinant human Fibroblast Activation Proteinalpha /FAP
Leu26-Asp760
Accession # Q12884 - FormulationSupplied in a saline solution containing BSA and Sodium Azide.
- LabelPhycoerythrin
- Flow Cytometry10 µL/106 cellsSee below
- ShippingThe product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
- Stability & StorageProtect from light. Do not freeze.
- 12 months from date of receipt, 2 to 8 °C as supplied.
- Scanlan, M.J. et al. (1994) Proc. Natl. Acad. Sci. USA 91:5657.
- Park, J.E. et al. (1999) J. Biol. Chem. 274:36505.
- Pineiro-Sanchez, M.L. et al. (1997) J. Biol. Chem. 272:7595.
- O'Brien, P. and B.F. O'Connor (2008) Biochim. Biophys. Acta 1784:1130.
- Garin-Chesa, P. et al. (1990) Proc. Natl. Acad. Sci. USA 87:7235.
- Rettig, W.J. et al. (1988) Proc. Natl. Acad. Sci. USA 85:3110.
- Entrez Gene IDs:2191 (Human); 14089 (Mouse)
- Alternate Names:170 kDa melanoma membrane-bound gelatinase; DKFZp686G13158; DPPIV; EC 3.4.21.-; FAP; FAPA; Fibroblast Activation Protein alpha; fibroblast activation protein, alpha; Integral membrane serine protease; Seprase; vibronectin
Background:
FAP (also known as Seprase) is a 97 kDa Type II transmembrane serine protease that is structurally related to Dipeptidyl Peptidase IV (DPPIV) (1). FAP has substrate specificity similar to DPPIV, which is specific for N-terminal Xaa-Pro sequences, but FAP is also an endopeptidase able to degrade gelatin and Type I Collagen (2). The enzymatically active form of FAP is a dimer that migrates at ~170 kDa. It is associated with multiple integral membrane proteins such as Integrin alpha 3 beta 1, UPA and DPPIV (3,4). FAP has a restricted tissue distribution. It is occasionally detected in fibroblasts and pancreatic islet cells, but is highly expressed on reactive stromal fibroblasts in epithelial cancers, in granulation tissue during wound healing, and in bone and soft tissue sarcomas (4-6). Because of its expression patterns and enzymatic activities, FAP is believed to play roles in tumor invasion, tissue remodeling, and wound repair. The 760 amino acid (aa) human FAP contains a 735 aa extracellular domain that is glycosylated and necessary for activity (4). It shares 90% aa identity with mouse and rat FAP. A reported 672 aa splicing variant diverges prior to the active site charge relay residues at the C-terminus.
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