Recombinant Human ADAM10 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human ADAM10 Protein, CF Summary

Details of Functionality
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.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human ADAM10 protein
Thr214-Glu672, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Thr214
Structure / Form
Recombinant Human ADAM10 is prone to proteolytic cleavage at C-terminus. The predominant form of the purified protein lacks the His tag.
Protein/Peptide Type
Recombinant Enzymes
Gene
ADAM10
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
52 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60 kDa, reducing conditions
Publications
Read Publications using
936-AD in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, ZnCl2,Glycerol and Brij-35.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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

Notes

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

Alternate Names for Recombinant Human ADAM10 Protein, CF

  • 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.

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Publications for ADAM10 (936-AD)(13)

We have publications tested in 5 confirmed species: Human, Mouse, E.coli, Hamster, N/A.

We have publications tested in 4 applications: Bioassay, EnzAct, Enzyme Assay, inhibition.


Filter By Application
Bioassay
(5)
EnzAct
(3)
Enzyme Assay
(4)
inhibition
(1)
All Applications
Filter By Species
Human
(9)
Mouse
(1)
E.coli
(1)
Hamster
(1)
N/A
(1)
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Showing Publications 1 - 10 of 13. Show All 13 Publications.
Publications using 936-AD Applications Species
K Goto, J Arai, A Stephanou, N Kato Novel therapeutic features of disulfiram against hepatocellular carcinoma cells with inhibitory effects on a disintegrin and metalloproteinase 10 Oncotarget, 2018;9(27):18821-18831. 2018 [PMID: 29721164] (Enzyme Assay, N/A) Enzyme Assay N/A
K Conant, S Daniele, PL Bozzelli, T Abdi, A Edwards, A Szklarczyk, I Olchefske, D Ottenheime, K Maguire-Ze Matrix metalloproteinase activity stimulates N-cadherin shedding and the soluble N-cadherin ectodomain promotes classical microglial activation J Neuroinflammation, 2017;14(1):56. 2017 [PMID: 28302163] (Bioassay, Human) Bioassay Human
Harnessing the natural inhibitory domain to control TNF? Converting Enzyme (TACE) activity in vivo Sci Rep, 2016;6(0):35598. 2016 [PMID: 27982031] (Enzyme Assay, Human) Enzyme Assay Human
Growth factor and co-receptor release by structural regulation of substrate metalloprotease accessibility Sci Rep, 2016;6(0):37464. 2016 [PMID: 27876763] (Enzyme Assay, Human) Enzyme Assay Human
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 Serological immune response against ADAM10 pro-domain is associated with favourable prognosis in stage III colorectal cancer patients Oncotarget, 2016;7(48):80059-80076. 2016 [PMID: 27517630] (EnzAct, Human) EnzAct Human
Kloverpris S, Mikkelsen J, Pedersen J, Jepsen M, Laursen L, Petersen S, Oxvig C Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A. J Biol Chem, 2015;290(36):21915-24. 2015 [PMID: 26195635] (Enzyme Assay, Human) Enzyme Assay Human
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 ADAM8 as a drug target in pancreatic cancer. Nat Commun, 2015;6(0):6175. 2015 [PMID: 25629724] (Bioassay, Human) Bioassay Human
Lajoie L, Congy-Jolivet N, Bolzec A, Gouilleux-Gruart V, Sicard E, Sung H, Peiretti F, Moreau T, Vie H, Clemenceau B, Thibault G ADAM17-mediated shedding of FcgammaRIIIA on human NK cells: identification of the cleavage site and relationship with activation. J Immunol, 2014;192(2):741-51. 2014 [PMID: 24337742] (Bioassay, Human) Bioassay Human
McDonald A, Dibble J, Evans E, Millhauser G A new paradigm for enzymatic control of alpha-cleavage and beta-cleavage of the prion protein. J Biol Chem, 2014;289(2):803-13. 2014 [PMID: 24247244] (EnzAct, E.coli) EnzAct E.coli
Hayes C, Dey D, Palavicini J, Wang H, Patkar K, Minond D, Nefzi A, Lakshmana M Striking reduction of amyloid plaque burden in an Alzheimer&#039;s mouse model after chronic administration of carmustine. BMC Med, 2013;11(0):81. 2013 [PMID: 23531149] (inhibition, Hamster) inhibition Hamster
Show All 13 Publications.

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Bioinformatics

Gene Symbol ADAM10
Entrez
Uniprot