Recombinant Human ADAM9 Protein, CF

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Summary
Product Discontinued
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    • Catalog Number
      939-AD
    • Availability
      Product Discontinued

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Recombinant Human ADAM9 Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a fluorogenic peptide substrate Mca-PLAQAV-Dpa-RSSSR-NH2 (Catalog # ES003). The specific activity is >1.0 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human ADAM9 protein
Ala206-Asp697, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ala206
Structure / Form
Mature form
Protein/Peptide Type
Recombinant Enzymes
Gene
ADAM9
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
55 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
64 kDa, reducing conditions
Publications
Read Publications using
939-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, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Assay Buffer: 25 mM Tris, 2.5 µM ZnCl2, 0.005% (w/v) Brij-35, pH 9.0
  • Recombinant Human ADAM-9 (rhADAM9) (Catalog # 939-AD)
  • Fluorogenic Peptide Substrate III: MCA-Pro-Leu-Ala-Gln-Ala-Val-DPA-Arg-Ser-Ser-Ser-Arg-NH2 (Catalog # ES003)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhADAM9 to 40 µg/mL in Assay Buffer.
  2. Dilute substrate to 20 µM in Assay Buffer.
  3. Combine equal volumes of 40 µg/mL rhADAM9 and 20 µM substrate. Include a control containing Assay Buffer and 20 µM substrate without any rhADAM9.
  4. Incubate reactions at 37 °C for 30 minutes.
  5. Load 100 μL of reactions and control per well in a black plate.
  6. Read with excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in endpoint mode.
  7. 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 Control
     **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhADAM9: 2.0 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 ADAM9 Protein, CF

  • a disintegrin and metalloproteinase domain 9 (meltrin gamma)
  • ADAM 9
  • ADAM metallopeptidase domain 9 (meltrin gamma)
  • ADAM metallopeptidase domain 9
  • ADAM9
  • Cellular disintegrin-related protein
  • cone rod dystrophy 9
  • CORD9
  • disintegrin and metalloproteinase domain-containing protein 9
  • EC 3.4.24
  • EC 3.4.24.-
  • MCMP
  • MCMPMDC9KIAA0021Mltng
  • MDC9
  • Meltrin gamma
  • Meltrin-gamma
  • Metalloprotease/disintegrin/cysteine-rich protein 9
  • MLTNG
  • Myeloma cell metalloproteinase

Background

ADAM9, also known as MDC9 or meltrin gamma , is a member of the ADAM family that contains a disintegrin and metalloprotease‑like domain (1). Like other membrane-anchored ADAMs, ADAM9 consists of a pro domain with a cysteine switch and furin cleavage sequence, a catalytic domain with the zinc‑binding site and Met-turn expected for reprolysins, a disintegrin-like domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and the cytoplasmic domain. ADAM9 is able to cleave peptides corresponding to cleavage sites of tumor necrosis factor-alpha (TNF-alpha ), the p75 TNF receptor, the beta -amyloid protein precursor, and the c‑kit ligand-1, implying that it may participate in shedding of these membrane proteins (2). In fact, ADAM9 has been shown to shed membrane‑anchored heparin-binding EGF-like growth factor (3). In addition, it also cleaves oxidized insulin beta -chain and fibronectin (2,4). Besides its catalytic activity, ADAM9 functions as an adhesion molecule through binding of its disintegrin domain to integrins such as alpha v beta 5 and alpha 6 beta 1 (5, 6). The cytoplasmic domain of ADAM9 interacts with Src homology 3
(SH3)‑containing proteins and protein kinase C, and may mediate different signaling pathways (3, 7). ADAM9 is widely expressed in tissues (8).
  1. Moss, et al. (2001) DDT 6:417.
  2. Roghan, et al. (1999) J. Biol. Chem. 274:3531.
  3. Izumi, et al. (1998) EMBO J. 17:7260.
  4. Schwettmann and Tschesche (2001) Prot. Expre. & Purif. 21:65.
  5. Nath, et al. (2000) J. Cell Sci. 113:2319.
  6. Zhou, et al. (2001) Biochem. Biophys. Res. Comm. 280:574.
  7. Howard, et al. (1999) J. Biol. Chem. 274:31693.
  8. Weskamp, et al. (1996) J. Cell. Biol. 132:717.

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939-AD
Species: Hu
Applications: Enzyme Activity

Publications for ADAM9 (939-AD)(11)

We have publications tested in 3 confirmed species: Human, Mouse, Primate - Chlorocebus aethiops (African Green Monkey).

We have publications tested in 3 applications: Bioassay, ELISA Capture, Enzyme Assay.


Filter By Application
Bioassay
(4)
ELISA Capture
(2)
Enzyme Assay
(5)
All Applications
Filter By Species
Human
(7)
Mouse
(1)
Primate - Chlorocebus aethiops (African Green Monkey)
(1)
All Species
Showing Publications 1 - 10 of 11. Show All 11 Publications.
Publications using 939-AD Applications Species
Mineva, ND;Pianetti, S;Das, SG;Srinivasan, S;Billiald, NM;Sonenshein, GE; A Novel Class of Human ADAM8 Inhibitory Antibodies for Treatment of Triple-Negative Breast Cancer Pharmaceutics 2024-04-13 [PMID: 38675197] (ELISA Capture, Human) ELISA Capture Human
JA Scribner, SW Hicks, KW Sinkeviciu, NC Yoder, G Diedrich, JG Brown, J Lucas, ME Fuller, T Son, A Dastur, J Hooley, CW Espelin, M Themeles, FZ Chen, Y Li, M Chiechi, J Lee, B Barat, L Widjaja, S Gorlatov, J Tamura, V Ciccarone, O Ab, KA McEachem, S Koenig, EH Westin, PA Moore, T Chittenden, RJ Gregory, E Bonvini, D Loo Preclinical Evaluation of IMGC936, a Next Generation Maytansinoid-based Antibody-drug Conjugate Targeting ADAM9-expressing Tumors Molecular Cancer Therapeutics, 2022-07-05;0(0):. 2022-07-05 [PMID: 35511740] (ELISA Capture, Human) ELISA Capture Human
TT Le, CL Hsieh, IH Lin, CY Chu, AD Do, SH Chen, K Shigemura, K Kitagawa, M Fujisawa, MC Liu, KC Chen, SY Sung The ADAM9/UBN2/AKR1C3 axis promotes resistance to androgen-deprivation in prostate cancer American journal of cancer research, 2022-01-15;12(1):176-197. 2022-01-15 [PMID: 35141012] (Bioassay, Human) Bioassay Human
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, 2018-04-10;9(27):18821-18831. 2018-04-10 [PMID: 29721164] (Enzyme Assay) Enzyme Assay
N Giebeler, A Schönefu beta , J Landsberg, T Tüting, C Mauch, P Zigrino Deletion of ADAM-9 in HGF/CDK4 mice impairs melanoma development and metastasis Oncogene, 2017-05-29;0(0):. 2017-05-29 [PMID: 28553955] (Enzyme Assay) Enzyme Assay
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, 2015-01-28;6(0):6175. 2015-01-28 [PMID: 25629724] (Primate - Chlorocebus aethiops (African Green Monkey)) Primate - Chlorocebus aethiops (African Green Monkey)
Roychaudhuri R, Hergrueter A, Polverino F, Laucho-Contreras M, Gupta K, Borregaard N, Owen C ADAM9 is a novel product of polymorphonuclear neutrophils: regulation of expression and contributions to extracellular matrix protein degradation during acute lung injury. J Immunol, 2014-07-25;193(5):2469-82. 2014-07-25 [PMID: 25063875] (Bioassay, Enzyme Assay, Human) Bioassay, Enzyme Assay Human
Moss ML, Bomar M, Liu Q, Sage H, Dempsey P, Lenhart PM, Gillispie PA, Stoeck A, Wildeboer D, Bartsch JW, Palmisano R, Zhou P The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J. Biol. Chem., 2007-09-25;282(49):35712-21. 2007-09-25 [PMID: 17895248] (Bioassay, Human) Bioassay Human
Zhou BB, Peyton M, He B, Liu C, Girard L, Caudler E, Lo Y, Baribaud F, Mikami I, Reguart N, Yang G, Li Y, Yao W, Vaddi K, Gazdar AF, Friedman SM, Jablons DM, Newton RC, Fridman JS, Minna JD, Scherle PA Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell, 2006-07-01;10(1):39-50. 2006-07-01 [PMID: 16843264] (Enzyme Assay, Human) Enzyme Assay Human
Karadag A, Zhou M, Croucher PI ADAM-9 (MDC-9/meltrin-gamma), a member of the a disintegrin and metalloproteinase family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the alpha(v)beta5 integrin. Blood, 2005-12-22;107(8):3271-8. 2005-12-22 [PMID: 16373656] (Bioassay, Human) Bioassay Human
Show All 11 Publications.

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Bioinformatics

Gene Symbol ADAM9
Uniprot