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Description
FAP Recombinant Rabbit mAb (S-3094-29)Product Specification Host Rabbit Antigen FAP Synonyms Prolyl endopeptidase FAP; 170 kDa melanoma membrane bound gelatinase; Dipeptidyl peptidase FAP; Fibroblast activation protein alpha (FAPalpha); Gelatine degradation protease FAP; Integral membrane serine protease Immunogen Synthetic Peptide Location Cytoplasm, Secreted, Cell membrane Accession Q12884 Clone Number S 3094 29 Antibody Type Recombinant mAb Isotype IgG Application WB, IHC P Reactivity
Product Specification
| Host | Rabbit |
| Antigen | FAP |
| Synonyms | Prolyl endopeptidase FAP; 170 kDa melanoma membrane-bound gelatinase; Dipeptidyl peptidase FAP; Fibroblast activation protein alpha (FAPalpha); Gelatine degradation protease FAP; Integral membrane serine protease |
| Immunogen | Synthetic Peptide |
| Location | Cytoplasm, Secreted, Cell membrane |
| Accession | Q12884 |
| Clone Number | S-3094-29 |
| Antibody Type | Recombinant mAb |
| Isotype | IgG |
| Application | WB, IHC-P |
| Reactivity | Hu |
| Positive Sample | SK-MEL-28, WI-38 |
| Purification | Protein A |
| Concentration | 0.5 mg/ml |
| Conjugation | Unconjugated |
| Physical Appearance | Liquid |
| Storage Buffer | PBS, 40% Glycerol, 0.05% BSA, 0.03% Proclin 300 |
| Stability & Storage | 12 months from date of receipt / reconstitution, -20 °C as supplied |
Dilution
| application | dilution | species |
| WB | 1:1000 | Hu |
| IHC-P | 1:2000-1:4000 | Hu |
Background
Fibroblast Activation Protein (FAP) is a 97-kDa type-II transmembrane serine protease that is virtually absent from healthy adult tissues but becomes highly and persistently up-regulated on activated fibroblasts during wound healing, fibrosis, arthritis, atherosclerosis and in the stroma of over 90 % of epithelial cancers, where its unique endopeptidase (Gly-Pro-X) and dipeptidyl-peptidase activities drive extracellular-matrix remodelling, immune evasion, M2 macrophage polarization and tumour-cell proliferation, migration and invasion via signalling axes such as ITGB1/PI3K/AKT and interactions with fibronectin, collagen and immune-checkpoint ligands, making it a powerful prognostic biomarker and an attractive therapeutic target across multiple malignancies and fibrotic diseases.
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Exchange/Return Notes
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