Overview
- Peptide CTPGESKNLGQKENG, corresponding to amino acid residues 400 - 414 of mouse ADAM10 (Accession O35598). Extracellular, N-terminus.
- Western blot analysis of rat brain membranes (lanes 1 and 3) and mouse brain membranes (lanes 2 and 4):1-2. Anti-ADAM10 (extracellular) Antibody (#ANR-156), (1:500). 3-4. Anti-ADAM10 (extracellular) Antibody, preincubated with ADAM10 (extracellular) Blocking Peptide (BLP-NR156).
- Western blot analysis of rat spleen lysate (lanes 1 and 3) and mouse spleen lysate (lanes 2 and 4):1-2. Anti-ADAM10 (extracellular) Antibody (#ANR-156), (1:500). 3-4. Anti-ADAM10 (extracellular) Antibody, preincubated with ADAM10 (extracellular) Blocking Peptide (BLP-NR156).
- Western blot analysis of human Jurkat T-cell leukemia cell line lysate (lanes 1 and 3) and human K562 erythroleukemia cell line lysate (lanes 2 and 4):1-2. Anti-ADAM10 (extracellular) Antibody (#ANR-156), (1:200). 3-4. Anti-ADAM10 (extracellular) Antibody, preincubated with ADAM10 (extracellular) Blocking Peptide (BLP-NR156).
- Expression of ADAM10 in mouse parietal cortex.Immunohistochemical staining of perfusion-fixed frozen mouse brain sections with Anti-ADAM10 (extracellular) Antibody (#ANR-156), (1:300), followed by goat anti-rabbit-AlexaFluor-488. A. ADAM10 immunoreactivity (green) appears in neuronal profiles (horizontal arrows). B. Pre-incubation of the antibody with ADAM10 (extracellular) Blocking Peptide (BLP-NR156), suppressed staining. Cell nuclei are stained with DAPI (blue).
- Cell surface detection of ADAM10 by indirect flow cytometry in live intact human THP-1 monocytic leukemia cells:___ Cells.
___ Cells + goat-anti-rabbit-FITC.
___ Cells + Anti-ADAM10 (extracellular) Antibody (#ANR-156), (2.5µg) + goat-anti-rabbit-FITC.
- Przemyslaw. et al. (2013), BMP REP, 46, 139.
- Wetzel. et al. (2017), Mol Cell research, 1864, 2071.
- Pruessmeyer and Ludwig. (2009), Semin. Cell Dev. Biol., 20, 164.
Disintegrin and metalloproteinase domain-containing protein 10, also known as ADAM10, is a membrane-anchored protease that belongs to the ADAM protease family. ADAMs are type I transmembrane proteins with a large extracellular domain and a shorter cytosolic part, they contain a metalloprotease domain, a disintegrin domain, a cystein-rich domain, an EGF-like domain, a transmembrane domain and a cytoplasmic tail2. 37 murine and 22 human ADAMs are known and only some of them contain the catalytically relevant domain (HEXGHXXGXXHD) and are therefore able to cleave the extracellular domains of several membrane-bound proteins in a process known as 'ectodomain shedding'1. This process represents a unique and irreversible posttranslational event regulating the function and half-life of many intracellular and extracellular proteins and hence the ADAM family protein's activity is essential for regulation of various cellular functions2. ADAM10 has many substrates, among which are cellular adhesion molecules such as cadherin, receptors and ligands3. it is also capable of anti-amyloidogenic proteolysis of the amyloid precursor protein, this is why ADAM10 mutations were shown to be correlated with Alzheimer's disease2. In addition, it was shown to involved in various human diseases and disorders such as Huntington's disease, psoriasis, lupus, and multiple types of cancer. The central role of ADAM10 in various cell processes and diseases reveals the potency of ADAM10-targeting drug development as a future therapeutic option2.
Application key:
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Anti-ADAM10 (extracellular) Antibody (#ANR-156) is a highly specific antibody directed against an extracellular epitope of mouse ADAM10. The antibody can be used in western blot, Indirect flow cytometry and immunohistochemistry. It has been designed to recognize ADAM10 from mouse, rat and human samples.