ADAM10 Antibody (163003)

• Reactivity: Hu
• Applications: WB, IP, CyTOF-ready, Flow
• Clone: 163003
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Unconjugated
• Concentration: LYOPH

ADAM10 Antibody (163003) Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant human ADAM10
  Thr214-Glu672
  Accession # O14672
• Specificity: Detects human ADAM10 in direct ELISAs and Western blots. In Western blots, shows less than 5% cross-reactivity with recombinant human (rh) ADAM8, 9, 15, 17/TACE, and recombinant mouse ADAM10.
• Source: N/A
• Isotype: IgG2b
• Clonality: Monoclonal
• Host: Mouse
• Gene: ADAM10
• Purity Statement: Protein A or G purified from hybridoma culture supernatant

Applications/Dilutions

• Dilutions:
  • CyTOF-ready
  • Immunoprecipitation 25 ug/mL
  • Intracellular Staining by Flow Cytometry 2.5 ug/10^6 cells
  • Western Blot 1 ug/mL

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.5 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for ADAM10 Antibody (163003)

• a disintegrin and metalloprotease domain 10
• a disintegrin and metalloproteinase domain 10
• AD10
• ADAM 10
• ADAM metallopeptidase domain 10
• ADAM10
• CD156c antigen
• CD156c
• CDw156
• disintegrin and metalloproteinase domain-containing protein 10
• EC 3.4.24
• HsT18717
• kuz
• Kuzbanian protein homolog
• Kuzbanian
• MADM
• MADMEC 3.4.24.81
• Mammalian disintegrin-metalloprotease

Background

ADAM10 (also known as Kuzbanian, mammalian disintegrin metalloprotease, myelin-associated metalloproteinase) is a member of the ADAM family that contains a disintegrin and metalloprotease-like domain (1, 2). Like other membrane-anchored ADAMs, ADAM10 consists of the following domains, pro with a cysteine switch and furin cleavage sequence, catalytic with the zinc-binding site and Met-turn expected for reprolysins, disintegrin-like, cysteine-rich, EGF-like, transmembrane, and cytoplasmic. ADAM10 is highly conserved, with 97% amino acid identity between mouse, rat, bovine and human and 45% identity between mouse and Drosophila. The active enzyme processes notch, notch ligand delta, and amyloid protein precursor at the alpha site, playing an important role in neurogenesis (3, 4). It also processes the 26 kDa membrane-anchored pro-tumor necrosis factor-alpha (TNF-alpha ) to the 17 kDa mature TNF-alpha (5). It cleaves myelin basic protein and type IV collagen (6, 7). ADAM10 is widely expressed in tissues and resides both on the cell surface and in the cell (8, 9).

1. Rooke, et al. (1996) Science 273:1227.
2. Pan and Rubin (1997) Cell 90:271.
3. Qi, et al. (1999) Science 283:91.
4. Lammich, et al. (1999) Proc. Natl. Acad. Sci. USA 96:3922.
5. Rosendahl, et al. (1997) J. Biol. Chem. 272:24588.
6. Chantry, et al. (1989) J. Biol. Chem. 264:21603.
7. Millichip, et al. (1998) Biochem. Biophys. Res. Comm. 245:594.
8. Chantry and Glynn (1990) Biochem. J. 268:245.
9. Fahrenholz, et al. (2000) Ann. N.Y. Acad. Sci. 920:215.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for ADAM10 Antibody (MAB1427)(19)

Publications using MAB1427

• Nayanendu Saha, Du-San Baek, Rachelle P. Mendoza, Dorothea Robev, Yan Xu, Yehuda Goldgur et al. Fully human monoclonal antibody targeting activated ADAM10 on colorectal cancer cells Biomedicine & Pharmacotherapy 2023-05-01 [PMID: 36917886]
• M Zatovicova, I Kajanova, M Takacova, L Jelenska, O Sedlakova, M Labudova, S Pastorekov ADAM10 mediates shedding of carbonic anhydrase IX ectodomain non?redundantly to ADAM17 Oncology reports, 2022-12-16;49(2):. 2022-12-16 [PMID: 36524367] (ICC, Human)
• Anna Lischnig, Markus Bergqvist, Takahiro Ochiya, Cecilia Lässer Quantitative Proteomics Identifies Proteins Enriched in Large and Small Extracellular Vesicles Molecular & Cellular Proteomics 2022-09-01 [PMID: 35918030]
• Alessio Vittorio Colombo, Rebecca Katie Sadler, Gemma Llovera, Vikramjeet Singh, Stefan Roth, Steffanie Heindl et al. Microbiota-derived short chain fatty acids modulate microglia and promote A beta plaque deposition eLife 2021-04-13 [PMID: 33845942]
• Lorena Martin‐Jaular, Nathalie Nevo, Julia P Schessner, Mercedes Tkach, Mabel Jouve, Florent Dingli et al. Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV‐1 infection The EMBO Journal 2021-04-15 [PMID: 33709510]
• R Crescitell, C Lässer, J Lötvall Isolation and characterization of extracellular vesicle subpopulations from tissues Nature Protocols, 2021-01-25;0(0):. 2021-01-25 [PMID: 33495626] (Western Blot, Human)
• Federico Cocozza, Nathalie Névo, Ester Piovesana, Xavier Lahaye, Julian Buchrieser, Olivier Schwartz et al. Extracellular vesicles containing ACE2 efficiently prevent infection by SARS‐CoV‐2 Spike protein‐containing virus Journal of Extracellular Vesicles 2020-12-28 [PMID: 33391636]
• N Möller, S Ziesemer, P Hildebrand, N Assenheime, U Völker, JP Hildebrand S. aureus alpha-toxin monomer binding and heptamer formation in host cell membranes - Do they determine sensitivity of airway epithelial cells toward the toxin? PLoS ONE, 2020-05-29;15(5):e0233854. 2020-05-29 [PMID: 32470006] (Flow Cytometry, Human)
• A Colombo, HE Hsia, M Wang, PH Kuhn, MS Brill, P Canevazzi, R Feederle, C Taveggia, T Misgeld, SF Lichtentha Non-cell-autonomous function of DR6 in Schwann cell proliferation EMBO J., 2018-02-19;0(0):. 2018-02-19 [PMID: 29459438] (Western Blot, Mouse)
• PC Buchanan, KL Boylan, B Walcheck, R Heinze, MA Geller, PA Argenta, AP Skubitz Ectodomain Shedding of the Cell Adhesion Molecule Nectin-4 in Ovarian Cancer is Mediated by ADAM10 and ADAM17 J. Biol. Chem, 2017-02-23;0(0):. 2017-02-23 [PMID: 28232483] (Flow Cytometry, Human)
• An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth J Exp Med, 2016-08-08;0(0):. 8/8/2016 [PMID: 27503072]
• Maria Raffaella Zocchi, Caterina Camodeca, Elisa Nuti, Armando Rossello, Roberta Venè, Francesca Tosetti et al. ADAM10 new selective inhibitors reduce NKG2D ligand release sensitizing Hodgkin lymphoma cells to NKG2D-mediated killing OncoImmunology 2016-05-03 [PMID: 27467923]
• Zhenyu Cai, Anling Zhang, Swati Choksi, Weihua Li, Tao Li, Xue-Min Zhang et al. Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration Cell Research 2016-08-01 [PMID: 27444869]
• Zingoni A, Cecere F, Vulpis E, Fionda C, Molfetta R, Soriani A, Petrucci M, Ricciardi M, Fuerst D, Amendola M, Mytilineos J, Cerboni C, Paolini R, Cippitelli M, Santoni A Genotoxic Stress Induces Senescence-Associated ADAM10-Dependent Release of NKG2D MIC Ligands in Multiple Myeloma Cells. J Immunol, 2015-06-12;195(2):736-48. 2015-06-12 [PMID: 26071561] (Flow Cytometry, Human)
• Breshears L, Schlievert P, Peterson M A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1). J Biol Chem, 2012-07-25;287(39):32578-87. 2012-07-25 [PMID: 22833676] (Flow Cytometry, Human)
• Maria Raffaella Zocchi, Silvia Catellani, Paolo Canevali, Sara Tavella, Anna Garuti, Barbara Villaggio et al. High ERp5/ADAM10 expression in lymph node microenvironment and impaired NKG2D ligands recognition in Hodgkin lymphomas Blood 2012-02-09 [PMID: 22167753]
• Koenen RR, Pruessmeyer J, Soehnlein O, Fraemohs L, Zernecke A, Schwarz N, Reiss K, Sarabi A, Lindbom L, Hackeng TM, Weber C, Ludwig A Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood, 2009-03-03;113(19):4799-809. 2009-03-03 [PMID: 19258599] (Flow Cytometry, Human)
• Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, Blobel CP, Himanen JP, Lackmann M, Nikolov DB Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell, 2005-10-21;123(2):291-304. 2005-10-21 [PMID: 16239146] (ICC, Western Blot, Human)
• Johansson MW, Lye MH, Barthel SR, Duffy AK, Annis DS, Mosher DF Eosinophils adhere to vascular cell adhesion molecule-1 via podosomes. Am. J. Respir. Cell Mol. Biol., 2004-06-25;31(4):413-22. 2004-06-25 [PMID: 15220135] (Flow Cytometry, ICC, Human)

Bioinformatics

• Gene Symbol: ADAM10
• Uniprot:
  • O14672()