Anti-Fibroblast activation protein, alpha/FAP Antibody Picoband®

Overview

Anti-Fibroblast activation protein, alpha/FAP Antibody Picoband® is an antibody reagent for detection of FAP (fibroblast activation protein alpha). Researchers commonly use anti-FAP antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, Flow, ELISA).

Boster Bio Anti-Fibroblast activation protein, alpha/FAP Antibody Picoband® catalog # A00422-5. Tested in ELISA, Flow Cytometry, WB applications. This antibody reacts with Human. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Target: FAP (fibroblast activation protein alpha). Alternative names: Prolyl endopeptidase FAP
• Antibody format: Polyclonal; Rabbit IgG
• Species context: Host: Rabbit, Reactivity: Human
• Purification: Immunogen affinity purified.
• Immunogen: E.coli-derived human Fibroblast activation protein, alpha/FAP recombinant protein (Position: Q65-Q580).
• Molecular weight context: observed 97 kDa (reported)
• Provided application(s): WB, IHC, Flow, ELISA

These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.

Biological background

Function: 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: Prolyl endopeptidase FAP: Cell surface.

Tissue details: 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.

Background: Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that in humans is encoded by the FAP gene. 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.

Cross reactivity: No cross-reactivity with other proteins.

Research relevance and current trends

• Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
• Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
• Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.

Common research applications

• Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
• Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
• Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.

Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.

Notes for experimental interpretation

• Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
• Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
• Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.

For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.

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.