{"product_id":"anti-lck-monoclonal-antibody-bha21008936","title":"Anti-Lck Monoclonal Antibody","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eThis 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.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eTarget:\u003c\/strong\u003e LCK (Prolyl endopeptidase FAP).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAntibody format:\u003c\/strong\u003e Monoclonal; clone ADBE-12; isotype Rabbit IgG.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHost:\u003c\/strong\u003e Rabbit.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSpecies reactivity:\u003c\/strong\u003e Human (confirm in your model system with appropriate controls).\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eThis 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.\u003c\/p\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eLCK (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. .\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eResearch context keywords from the source record include: Adaptive Immunity,Immunoglobulins,Immunology,Protein Phosphorylation,Receptors,Secreted Molecules,Signal Transduction,T Cells,Tyrosine Kinases.\u003c\/li\u003e\n\u003cli\u003eCurrent studies often focus on connecting target abundance\/localization to pathway perturbations across models, tissues, and cell states.\u003c\/li\u003e\n\u003cli\u003eQuantitative and multiplexed assays (e.g., imaging + immunoblot panels) are commonly used to compare phenotypes across conditions and time-courses.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eWestern blotting (WB):\u003c\/strong\u003e assess relative target abundance across samples, treatments, or time-points.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eImmunohistochemistry (IHC):\u003c\/strong\u003e evaluate spatial distribution of target-positive staining in tissue architecture.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eImmunofluorescence\/ICC (IF\/ICC):\u003c\/strong\u003e visualize subcellular localization patterns and cell-to-cell heterogeneity.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFlow cytometry:\u003c\/strong\u003e quantify target-positive populations and compare shifts in marker distributions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eImmunoprecipitation (IP):\u003c\/strong\u003e enrich target complexes for downstream immunoblot or interaction analyses.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eWorkflow 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\u003c\/p\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eConsider isoforms and post-translational modifications (PTMs) that may shift apparent molecular weight or epitope accessibility.\u003c\/li\u003e\n\u003cli\u003eApparent molecular weight may vary by sample type and processing (observed MW: 11 kDa; calculated MW: 87713 MW).\u003c\/li\u003e\n\u003cli\u003eControl concepts: include appropriate negative controls (e.g., isotype, KO\/KD samples) and orthogonal validation when feasible.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eAdditional product details (from the source record)\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight (observed):\u003c\/strong\u003e 11 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCellular localization (provided):\u003c\/strong\u003e 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. .\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTissue details (provided):\u003c\/strong\u003e 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. .\u003c\/li\u003e\n\u003c\/ul\u003e \u003c!-- Sources (internal): - Antibodies — a laboratory manual overview — Cold Spring Harbor Protocols — https:\/\/cshprotocols.cshlp.org\/ - UniProt Knowledgebase — UniProt — https:\/\/www.uniprot.org\/ - NCBI Gene — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - Antibody validation and reproducibility — Nature methods (collections) — https:\/\/www.nature.com\/collections\/ - Immunohistochemistry\/Immunofluorescence basics — NIH \/ NCBI Bookshelf — https:\/\/www.ncbi.nlm.nih.gov\/books\/ --\u003e","brand":"Boster Bio","offers":[{"title":"100 uL\/vial \/ Unconjugated","offer_id":53071954346349,"sku":"M00425","price":370.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/m00425-wb7.jpg?v=1772618800","url":"https:\/\/www.ebiohippo.com\/products\/anti-lck-monoclonal-antibody-bha21008936","provider":"BioHippo","version":"1.0","type":"link"}