| 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 | |
| Form | Liquid |
| Host | |
| Immunogen | A synthesized peptide derived from human Lck The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells. Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
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| Target | |
| UniProt # |
Overview
This product is an anti-LCK antibody for target detection and characterization. Key identifiers include host species: Rabbit; Monoclonal; clone ADBE-12; isotype Rabbit IgG; reactivity: Human. Reported application contexts include WB, IHC, ICC, IF, IP, Flow (as provided in the source record). Boster Bio Anti-Lck Monoclonal Antibody catalog # M00425. Tested in WB, IHC, ICC/IF, IP, Flow Cytometry applications. This antibody reacts with Human.
Key elements and design rationale
- Target: LCK (Prolyl endopeptidase FAP).
- Antibody format: Monoclonal; clone ADBE-12; isotype Rabbit IgG.
- Host: Rabbit.
- Species reactivity: Human (confirm in your model system with appropriate controls).
This description is intended to help interpret the antibody design and the biological context of the target using the fields provided in the catalog record, alongside general experimental considerations.
Biological background
LCK (protein: T-cell surface glycoprotein CD4) is a commonly studied target in molecular and cellular biology. Functional context (as provided): 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. . Reported cellular localization context: 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 expression notes (as provided): 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
- Research context keywords from the source record include: Adaptive Immunity,Immunoglobulins,Immunology,Protein Phosphorylation,Receptors,Secreted Molecules,Signal Transduction,T Cells,Tyrosine Kinases.
- Current studies often focus on connecting target abundance/localization to pathway perturbations across models, tissues, and cell states.
- Quantitative and multiplexed assays (e.g., imaging + immunoblot panels) are commonly used to compare phenotypes across conditions and time-courses.
Common research applications
- Western blotting (WB): assess relative target abundance across samples, treatments, or time-points.
- Immunohistochemistry (IHC): evaluate spatial distribution of target-positive staining in tissue architecture.
- Immunofluorescence/ICC (IF/ICC): visualize subcellular localization patterns and cell-to-cell heterogeneity.
- Flow cytometry: quantify target-positive populations and compare shifts in marker distributions.
- Immunoprecipitation (IP): enrich target complexes for downstream immunoblot or interaction analyses.
Workflow ideas (metafield): Validate LCK antibody specificity using KO/KD control samples (WB/IF/IHC as appropriate), Detect LCK expression by Western blot in cell or tissue lysates, Detect LCK in FFPE tissue sections by immunohistochemistry, Localize LCK by immunofluorescence/immunocytochemistry in cultured cells, Quantify LCK-positive cells by flow cytometry in single-cell suspensions, Enrich LCK by immunoprecipitation from lysates for downstream analysis
Notes for experimental interpretation
- Consider isoforms and post-translational modifications (PTMs) that may shift apparent molecular weight or epitope accessibility.
- Apparent molecular weight may vary by sample type and processing (observed MW: 11 kDa; calculated MW: 87713 MW).
- Control concepts: include appropriate negative controls (e.g., isotype, KO/KD samples) and orthogonal validation when feasible.
Additional product details (from the source record)
- Molecular weight (observed): 11 kDa
- Cellular localization (provided): 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 (provided): 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. .
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