| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Prolyl endopeptidase FAP ;3.4.21.26 ;170 kDa melanoma membrane-bound gelatinase ;Dipeptidyl peptidase FAP ;3.4.14.5 ;Fibroblast activation protein alpha ;FAPalpha ;Gelatine degradation protease FAP ;3.4.21.- ;Integral membrane serine protease ;Post-proline cleaving enzyme ;Serine integral membrane protease ;SIMP ;Surface-expressed protease ;Seprase ;Antiplasmin-cleaving enzyme FAP, soluble form ;APCE ;3.4.14.5 ;3.4.21.- ;3.4.21.26 ;FAP ; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | A synthesized peptide derived from human FAP1 |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-FAP1 Rabbit Monoclonal Antibody is an antibody targeting FAP. Common applications include WB, IHC. Key specifications include host: Rabbit; clonality: Monoclonal; clone: Clone: AbF22; isotype: Rabbit IgG; reactivity: Human,Mouse,Rat; observed MW: 95 kDa; calculated MW: 87713 MW.
Boster Bio Anti-FAP1 Rabbit Monoclonal Antibody catalog # M00422. Tested in WB, IHC applications. This antibody reacts with Human, Mouse, Rat.
Key elements and design rationale
- Target: FAP — Prolyl endopeptidase FAP
- Antibody format: Host: Rabbit; Clonality: Monoclonal; Clone: Clone: AbF22; Isotype: Rabbit IgG
- Species reactivity: Human,Mouse,Rat
- Molecular weight guidance: Observed: 95 kDa; Calculated: 87713 MW
Biological background
Protein function (datasheet): 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 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). 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 (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). 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. .
Cellular localization (datasheet): Prolyl endopeptidase FAP: Cell surface . Cell membrane ; Single- pass type II membrane protein . Cell projection, lamellipodium membrane ; Single-pass type II membrane protein . Cell projection, invadopodium membrane ; Single-pass type II membrane protein . Cell projection, ruffle membrane ; Single-pass type II membrane protein . Membrane ; Single-pass type II membrane protein . Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. .
Tissue details (datasheet): Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines. .
Research relevance and current trends
- Commonly studied in contexts related to Proteolysis/Ubiquitin,Proteolytic Enzymes,Signal Transduction,Tumor Biomarkers.
- Supports comparative expression analysis across conditions, genotypes, or treatments when paired with appropriate controls.
- Useful for confirming target presence and subcellular distribution using orthogonal readouts (e.g., microscopy vs. immunoblotting).
Common research applications
- Western blot (WB): Compare relative target abundance and apparent size/isoforms across samples; interpret bands in light of expected MW and potential PTMs.
- Immunohistochemistry (IHC): Assess tissue distribution and cell-type patterns; interpret staining with appropriate negative controls and antigen context.
Notes for experimental interpretation
- Consider isoforms, post-translational modifications, and processing that can shift apparent molecular weight or localization.
- Use appropriate positive and negative controls (e.g., KO/KD, blocking peptide, or isotype controls) to support specificity interpretation.
As a monoclonal antibody, this reagent is expected to recognize a defined epitope, which can support consistency across lots when epitope accessibility is preserved.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
