Recombinant Human ADAM10 Protein, CF

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Recombinant Human ADAM10 Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 (Catalog # ES010). The specific activity is >20 pmol/min/µg, as measured under the described conditions.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human ADAM10 protein
Thr214-Glu672, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Structure / Form
Recombinant Human ADAM10 may be prone to proteolytic cleavage at C-terminus. The poly-His tag may not be present in the preparation.
Predicted Molecular Mass
52 kDa
60 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Supplied as a 0.2 μm filtered solution in MES, NaCl, ZnCl2,Glycerol and Brij-35.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Assay Procedure

  • Assay Buffer: 25 mM Tris, 2 μM ZnCl2, 0.005% (w/v) Brij-35, pH 9.0
  • Recombinant Human ADAM10 (rhADAM10) (Catalog # 936-AD)
  • Fluorogenic Peptide Substrate: MCA-Lys-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES010), 6.2 mM in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhADAM10 to 1 ng/µL in Assay Buffer.
  2. Dilute substrate to 20 µM in Assay Buffer.
  3. Load into plate 50 µL of 1 ng/µL rhADAM10 and start the reaction by adding 50 µL of 20 µM Substrate. As a control load 50 µL of Assay Buffer and 50 µL of 20 µM Substrate.
  4. Seal plate and incubate at 37 °C for 30 minutes.
  5. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in endpoint mode.
  6. Calculate specific activity: 

     Specific Activity (pmol/min/µg) =

Adjusted Fluorescence* (RFU) x Conversion Factor** (pmol/RFU)
Incubation time (min) x amount of enzyme (µg)

     *Adjusted for Substrate Blank.
     **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhADAM10: 0.050 µg
  • Substrate: 10 µM
Reconstitution Calculator

Reconstitution Calculator

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Background: ADAM10

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.
Long Name
A Disintegrin and Metalloprotease-like Domain 10
Entrez Gene IDs
102 (Human); 11487 (Mouse)
Alternate Names
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; Mammalian disintegrin-metalloprotease

Citations for Recombinant Human ADAM10 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

22 Citations: Showing 1 - 10
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  1. A topological refactoring design strategy yields highly stable granulopoietic proteins
    Authors: J Skokowa, B Hernandez, M Coles, M Ritter, M Nasri, J Haaf, N Aghaallaei, Y Xu, P Mir, AC Krahl, KW Rogers, K Maksymenko, B Bajoghli, K Welte, AN Lupas, P Müller, M ElGamacy
    Nature Communications, 2022;13(1):2948.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Altered succinylation of mitochondrial proteins, APP and tau in Alzheimer's disease
    Authors: Y Yang, V Tapias, D Acosta, H Xu, H Chen, R Bhawal, ET Anderson, E Ivanova, H Lin, BT Sagdullaev, J Chen, WL Klein, KL Viola, S Gandy, V Haroutunia, MF Beal, D Eliezer, S Zhang, GE Gibson
    Nature Communications, 2022;13(1):159.
    Species: Human
    Sample Types: Peptides
    Applications: Bioassay
  3. ADAM10 attenuates the development of abdominal aortic aneurysms in a mouse model
    Authors: Q Renfeng, C Shuxiao, G Peixian, L Kun, F Xuedong, Y Hai, W Xuejun, L Gang
    Molecular Medicine Reports, 2021;24(5):.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  4. TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1
    Authors: AP Carreca, VM Pravatà, M Markham, S Bonelli, G Murphy, H Nagase, L Troeberg, SD Scilabra
    Sci Rep, 2020;10(1):12067.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  5. Design and synthesis of selective and blood-brain barrier-permeable hydroxamate-based gelatinase inhibitors
    Authors: A Bertran, D Khomiak, A Konopka, E Rejmak, E Bulska, J Seco, L Kaczmarek, T Tarragó, R Prades
    Bioorg. Chem., 2019;0(0):103365.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  6. ADAM10 is Expressed by Ameloblasts, Cleaves the RELT TNF Receptor Extracellular Domain and Facilitates Enamel Development
    Authors: A Ikeda, S Shahid, BR Blumberg, M Suzuki, JD Bartlett
    Sci Rep, 2019;9(1):14086.
    Species: Mouse
    Sample Types: Protein
    Applications: Bioassay
  7. Inhibiting pathologically active ADAM10 rescues synaptic and cognitive decline in Huntington's disease
    Authors: E Vezzoli, I Caron, F Talpo, D Besusso, P Conforti, E Battaglia, E Sogne, A Falqui, L Petricca, M Verani, P Martufi, A Caricasole, A Bresciani, O Cecchetti, P Rivetti di, G Sancini, O Riess, H Nguyen, L Seipold, P Saftig, G Biella, E Cattaneo, C Zuccato
    J. Clin. Invest., 2019;130(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  8. ADAM10 Sheddase Activity is a Potential Lung-Cancer Biomarker
    Authors: T Yoneyama, M Gorry, A Sobo-Vujan, Y Lin, L Vujanovic, A Gaither-Da, ML Moss, MA Miller, LG Griffith, DA Lauffenbur, LP Stabile, J Herman, NL Vujanovic
    J Cancer, 2018;9(14):2559-2570.
    Species: N/A
    Sample Types: Recombinant Protein
    Applications: Bioassay
  9. Non-cell-autonomous function of DR6 in Schwann cell proliferation
    Authors: A Colombo, HE Hsia, M Wang, PH Kuhn, MS Brill, P Canevazzi, R Feederle, C Taveggia, T Misgeld, SF Lichtentha
    EMBO J., 2018;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  10. Novel therapeutic features of disulfiram against hepatocellular carcinoma cells with inhibitory effects on a disintegrin and metalloproteinase 10
    Authors: K Goto, J Arai, A Stephanou, N Kato
    Oncotarget, 2018;9(27):18821-18831.
    Species: N/A
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  11. Matrix metalloproteinase activity stimulates N-cadherin shedding and the soluble N-cadherin ectodomain promotes classical microglial activation
    Authors: K Conant, S Daniele, PL Bozzelli, T Abdi, A Edwards, A Szklarczyk, I Olchefske, D Ottenheime, K Maguire-Ze
    J Neuroinflammation, 2017;14(1):56.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  12. Growth factor and co-receptor release by structural regulation of substrate metalloprotease accessibility
    Sci Rep, 2016;6(0):37464.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  13. Harnessing the natural inhibitory domain to control TNF? Converting Enzyme (TACE) activity in vivo
    Sci Rep, 2016;6(0):35598.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  14. Serological immune response against ADAM10 pro-domain is associated with favourable prognosis in stage III colorectal cancer patients
    Authors: SM Álvarez-Fe, M Barbariga, L Cannizzaro, CV Cannistrac, L Hurley, A Zanardi, A Conti, F Sanvito, A Innocenzi, N Pecorelli, M Braga, M Alessio
    Oncotarget, 2016;7(48):80059-80076.
    Species: Human
    Sample Types: Serum
    Applications: Enzyme Assay
  15. ADAM8 as a drug target in pancreatic cancer.
    Authors: Schlomann U, Koller G, Conrad C, Ferdous T, Golfi P, Garcia A, Hofling S, Parsons M, Costa P, Soper R, Bossard M, Hagemann T, Roshani R, Sewald N, Ketchem R, Moss M, Rasmussen F, Miller M, Lauffenburger D, Tuveson D, Nimsky C, Bartsch J
    Nat Commun, 2015;6(0):6175.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  16. Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A.
    Authors: Kloverpris S, Mikkelsen J, Pedersen J, Jepsen M, Laursen L, Petersen S, Oxvig C
    J Biol Chem, 2015;290(36):21915-24.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  17. A new paradigm for enzymatic control of alpha-cleavage and beta-cleavage of the prion protein.
    Authors: McDonald A, Dibble J, Evans E, Millhauser G
    J Biol Chem, 2014;289(2):803-13.
    Species: Bacteria - E. Coli
    Sample Types: Cell Lysates
    Applications: Enzyme Assay
  18. ADAM17-mediated shedding of FcgammaRIIIA on human NK cells: identification of the cleavage site and relationship with activation.
    Authors: Lajoie L, Congy-Jolivet N, Bolzec A, Gouilleux-Gruart V, Sicard E, Sung H, Peiretti F, Moreau T, Vie H, Clemenceau B, Thibault G
    J Immunol, 2014;192(2):741-51.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  19. Striking reduction of amyloid plaque burden in an Alzheimer's mouse model after chronic administration of carmustine.
    Authors: Hayes C, Dey D, Palavicini J, Wang H, Patkar K, Minond D, Nefzi A, Lakshmana M
    BMC Med, 2013;11(0):81.
    Species: Hamster
    Sample Types: Whole Cells
    Applications: Inhibition
  20. Anticancer chemotherapy inhibits MHC class I-related chain a ectodomain shedding by downregulating ADAM10 expression in hepatocellular carcinoma.
    Authors: Kohga K, Takehara T, Tatsumi T, Miyagi T, Ishida H, Ohkawa K, Kanto T, Hiramatsu N, Hayashi N
    Cancer Res., 2009;69(20):8050-7.
    Species: Human
    Sample Types: Whole Tissue
    Applications: Bioassay
  21. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events.
    Authors: Moss ML, Bomar M, Liu Q, Sage H, Dempsey P, Lenhart PM, Gillispie PA, Stoeck A, Wildeboer D, Bartsch JW, Palmisano R, Zhou P
    J. Biol. Chem., 2007;282(49):35712-21.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  22. Selective roles for tumor necrosis factor alpha-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: the juxtamembrane stalk determines cleavage efficiency.
    Authors: Hinkle CL, Sunnarborg SW, Loiselle D, Parker CE, Stevenson M, Russell WE, Lee DC
    J. Biol. Chem., 2004;279(23):24179-88.
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay


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Recombinant Human ADAM10 Protein, CF
By Youwen Zhang on 04/17/2020
Application: In vivo study