ADAM9 Antibody [Unconjugated]

HAF017). Specific bands were detected for ADAM9 at approximately 110 and 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." > HAF017). Specific bands were detected for ADAM9 at approximately 110 and 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." title="Western blot shows lysates of C2C12 mouse myoblast cell line and WI-38 human lung fibroblast cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). Specific bands were detected for ADAM9 at approximately 110 and 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." />

Western blot shows lysates of C2C12 mouse myoblast cell line and WI-38 human lung fibroblast cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

HAF017). Specific bands were detected for ADAM9 at approximately 78 and 110 kDa (as indicated) in the parental HeLa cell line, but is not detectable in knockout HeLa cell line. GAPDH (AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." > HAF017). Specific bands were detected for ADAM9 at approximately 78 and 110 kDa (as indicated) in the parental HeLa cell line, but is not detectable in knockout HeLa cell line. GAPDH (AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." title="Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and ADAM9 knockout HeLa cell line (KO). PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). Specific bands were detected for ADAM9 at approximately 78 and 110 kDa (as indicated) in the parental HeLa cell line, but is not detectable in knockout HeLa cell line. GAPDH (AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." />

Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and ADAM9 knockout HeLa cell line (KO). PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

Rescue of ADAM9 expression restores EMCV replication in ADAM9 KO cells. WT and ADAM9 KO HeLa cells were transduced with retroviral vectors with wild-type (WT) murine ADAM9 (mADAM9), catalytically inactive mutant ADAM9 (E>A), cytoplasmic-tail-deleted ( delta CT) ADAM9 constructs, or GFP control vectors. (A) WT, KO, and rescue cell lysates were analyzed by Western blot using two different ADAM9 antibodies. Top panel, rabbit anti-human ADAM9 that detects an epitope in the intracellular domain of human ADAM9 and cross-reacts with mouse ADAM9 (black asterisk). Middle panel, goat anti-mouse ADAM9 that detects the extracellular domain of murine ADAM9 but not human ADAM9 (blue asterisk). Bottom panel, anti-actin which detects both human and murine beta -actin. Top panel, WT but not KO cells expressed human ADAM9. Middle panel, rescue but not KO cells expressed murine ADAM9. Bottom panel, actin loading control. (B) WT clones, ADAM9 KO clones, and rescued ADAM9-expressing clones were infected with EMCV or CVB3 at various MOIs and incubated at 37°C for 24 h. Viability of EMCV-infected and CVB3-infected clones was measured by CellGlo ATP luminescence. (C) EMCV replication was quantified in infected culture supernatants by plaque assay. Neither the functional sequence of the ADAM9 metalloproteinase domain nor the cytoplasmic tail is required for EMCV infection. ***, P < 0.0001, KO versus WT and KO versus rescue. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30723129), licensed under a CC-BY license. Not internally tested by R&D Systems.

VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the membrane. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." > VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the membrane. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." title="ADAM9 was detected in immersion fixed paraffin-embedded sections of mouse kidney using Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) at 10 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the membrane. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." />

ADAM9 was detected in immersion fixed paraffin-embedded sections of mouse kidney using Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) at 10 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # <a class=

AB-108-C, open histogram) followed by Allophycocyanin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0108). View our protocol for Staining Membrane-associated Proteins. " > AB-108-C, open histogram) followed by Allophycocyanin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0108). View our protocol for Staining Membrane-associated Proteins. " title="C2C12 cells were stained with Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949, filled histogram) or isotype control antibody (Catalog # AB-108-C, open histogram) followed by Allophycocyanin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0108). View our protocol for Staining Membrane-associated Proteins. " />

C2C12 cells were stained with Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949, filled histogram) or isotype control antibody (Catalog # <a class=

• Reactivity: Hu, Mu
• Applications: WB, Flow, IHC, IP, CyTOF-ready, KO
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

ADAM9 Antibody [Unconjugated] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant mouse ADAM9
  Ala206-Asp697
  Accession # Q61072
• Specificity: Detects mouse ADAM9 Ectodomain in direct ELISAs and Western blots. In Western blots no cross-reactivity with the Ectodomain of recombinant mouse ADAM10 and rhADAM8, 15, and 17 (TACE) is observed.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: ADAM9
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • CyTOF-ready
  • Flow Cytometry 0.25 ug/10^6 cells
  • Immunohistochemistry 5-15 ug/mL
  • Immunoprecipitation 25 ug/mL
  • Knockout Validated
  • 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. See Certificate of Analysis for details.
  *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 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Notes

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

Alternate Names for ADAM9 Antibody [Unconjugated]

• 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 B-chain and fibronectin (2, 4). Besides its catalytic activity, ADAM9 functions as an adhesion molelcule 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, M.L. et al. (2001) Drug Discov. Today 6:417.
2. Roghani, M. et al. (1999) J. Biol. Chem. 274:3531.
3. Izumi, Y. et al. (1998) EMBO J. 17:7260.
4. Schwettmann, L. and H. Tschesche (2001) Protein. Expr. Purif. 21:65. 
5. Nath, D. et al. (2000) J. Cell Sci. 113:2319.
6. Zhou, M. et al. (2001) Biochem. Biophys. Res. Comm. 280:574.
7. Howard, L. et al. (1999) J. Biol. Chem. 274:31693.
8. Weskamp, G. et al. (1996) J. Cell Biol. 132:717.

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 ADAM9 Antibody (AF949)(15)

Publications using AF949

• Jotatsu, Y;Sung, SY;Wu, MH;Takeda, S;Hirata, Y;Maeda, K;Fang, SB;Chen, KC;Shigemura, K; An Antibody of the Secreted Isoform of Disintegrin and Metalloprotease 9 (sADAM9) Inhibits Epithelial-Mesenchymal Transition and Migration of Prostate Cancer Cell Lines International journal of molecular sciences 2024-06-17 [PMID: 38928352] (Neutralization, Human, Mouse)
• Bazzone, LE;Zhu, J;King, M;Liu, G;Guo, Z;MacKay, CR;Kyawe, PP;Qaisar, N;Rojas-Quintero, J;Owen, CA;Brass, AL;McDougall, W;Baer, CE;Cashman, T;Trivedi, CM;Gack, MU;Finberg, RW;Kurt-Jones, EA; ADAM9 promotes type I interferon-mediated innate immunity during encephalomyocarditis virus infection Nature communications 2024-05-16 [PMID: 38755212] (Western Blot, Human)
• WC Cheng, CY Chang, CC Lo, CY Hsieh, TT Kuo, GC Tseng, SC Wong, SF Chiang, KC Huang, LC Lai, TP Lu, KSC Chao, YP Sher Identification of theranostic factors for patients developing metastasis after surgery for early-stage lung adenocarcinoma Theranostics, 2021-01-26;11(8):3661-3675. 2021-01-26 [PMID: 33664854] (IHC, Human)
• Anna N. Abety, Elke Pach, Nives Giebeler, Julia E. Fromme, Lavakumar Reddy Aramadhaka, Cornelia Mauch et al. Loss of ADAM9 Leads to Modifications of the Extracellular Matrix Modulating Tumor Growth Biomolecules 2020-09-07 [PMID: 32906814] (Western Blot, Mouse)
• LE Bazzone, M King, CR MacKay, PP Kyawe, P Meraner, D Lindstrom, J Rojas-Quin, CA Owen, JP Wang, AL Brass, EA Kurt-Jones, RW Finberg A Disintegrin and Metalloproteinase 9 Domain (ADAM9) Is a Major Susceptibility Factor in the Early Stages of Encephalomyocarditis Virus Infection MBio, 2019-02-05;10(1):. 2019-02-05 [PMID: 30723129] (Western Blot, Human)
• KJ Mygind, T Störiko, ML Freiberg, J Samsøe-Pet, J Schwarz, OM Andersen, M Kveiborg Sorting nexin 9 (SNX9) regulates levels of the transmembrane disintegrin and metalloproteinase (ADAM)-9 at the cell surface J. Biol. Chem., 2018-04-05;0(0):. 2018-04-05 [PMID: 29622675] (Western Blot, Human)
• Kasper J. Mygind, Jeanette Schwarz, Pranshu Sahgal, Johanna Ivaska, Marie Kveiborg Loss of ADAM9 expression impairs beta 1 integrin endocytosis, focal adhesion formation and cancer cell migration Journal of Cell Science 2017-04-21 [PMID: 29142101]
• CY Lin, CF Cho, ST Bai, JP Liu, TT Kuo, LJ Wang, YS Lin, CC Lin, LC Lai, TP Lu, CY Hsieh, CN Chu, DC Cheng, YP Sher ADAM9 promotes lung cancer progression through vascular remodeling by VEGFA, ANGPT2, and PLAT Sci Rep, 2017-11-08;7(1):15108. 2017-11-08 [PMID: 29118335] (Neutralization, Human)
• 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] (IHC, Mouse)
• Wing Yip Tam The association between laminin and microglial morphology in vitro Sci Rep, 2016-06-23;6(0):28580. 2016-06-23 [PMID: 27334934] (IHC, Mouse)
• Sarah Louise Dombernowsky, Jacob Samsøe-Petersen, Camilla Hansson Petersen, Rachael Instrell, Anne-Mette Bornhardt Hedegaard, Laurel Thomas et al. The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17 Nature Communications 2015-06-25 [PMID: 26108729] (Flow Cytometry, Western Blot, Human)
• JUN ZHANG, JUAN QI, NING CHEN, WEINENG FU, BAOSEN ZHOU, ANGUANG HE High expression of a disintegrin and metalloproteinase-9 predicts a shortened survival time in completely resected stage I non-small cell lung cancer Oncology Letters 2013-05-01 [PMID: 23761811]
• Delarasse C, Auger R, Gonnord P, Fontaine B, Kanellopoulos JM The purinergic receptor P2X7 triggers alpha-secretase-dependent processing of the amyloid precursor protein. J. Biol. Chem., 2010-11-16;286(4):2596-606. 2010-11-16 [PMID: 21081501] (ICC, Western Blot, Mouse)
• Mauch C, Zamek J, Abety AN, Grimberg G Accelerated wound repair in ADAM-9 knockout animals. J. Invest. Dermatol., 2010-04-08;130(8):2120-30. 2010-04-08 [PMID: 20376065] (Western Blot, Mouse)
• Saunders WB, Bohnsack BL, Faske JB, Anthis NJ, Bayless KJ, Hirschi KK, Davis GE Coregulation of vascular tube stabilization by endothelial cell TIMP-2 and pericyte TIMP-3. J. Cell Biol., 2006-10-09;175(1):179-91. 2006-10-09 [PMID: 17030988] (Western Blot, Human)

Bioinformatics

• Gene Symbol: ADAM9
• Uniprot:
  • Q61072()