| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Disintegrin and metalloproteinase domain-containing protein 10; ADAM 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD156c; ADAM10; KUZ; MADM |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human ADAM10 recombinant protein (Position: A217-D311). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-ADAM10 Antibody Picoband® is an antibody reagent for detection of ADAM10 (ADAM metallopeptidase domain 10). Researchers commonly use anti-ADAM10 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-ADAM10 Antibody Picoband® catalog # A00566-5. 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: ADAM10 (ADAM metallopeptidase domain 10). Alternative names: Disintegrin and metalloproteinase domain-containing protein 10; ADAM 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD156c; ADAM10; KUZ; MADM
- Antibody format: Polyclonal; Rabbit IgG
- Species context: Host: Rabbit, Reactivity: Human
- Purification: Immunogen affinity purified.
- Immunogen: E.coli-derived human ADAM10 recombinant protein (Position: A217-D311).
- Molecular weight context: observed 70 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: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).
Cellular localization: Cell membrane.
Tissue details: Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.
Background: A Disintegrin and metalloproteinase domain-containing protein 10, also known as ADAM10 or CDw156 or CD156c is a protein that in humans is encoded by the ADAM10 gene. Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. Alternate splicing results in multiple transcript variants encoding different proteins that may undergo similar processing.
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.