Sign in or Register   Sign in or Register
  |  

Mouse Anti-ADAM9 Recombinant Antibody (V2-6081) (CBMAB-0026CQ)

This product is a mouse antibody that recognizes ADAM9. The antibody 8A15 can be used for immunoassay techniques such as: WB.
See all ADAM9 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-6081
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Human recombinant ADAM-9 (EC domain)
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS
Preservative
None
Concentration
0.5 mg/ml
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
ADAM metallopeptidase domain 9 (meltrin gamma)
Introduction
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. Using a yeast 2-hybrid analysis with the cytoplasmic tails of several ADAM proteins as bait. MAD2L2 (604094) interacts with MDC9 (ADAM9) and ADAM15 (605548) strongly and with ADAM19 (603640) weakly, but not with TACE (ADAM17; 603639), which interacts with MAD2L1 (601467). Further binding analyses determined that the interaction of MAD2L2 with ADAM9 is mediated through a proline-rich SH3-ligand domain of ADAM9.
Entrez Gene ID
8754
UniProt ID
Q13443
Alternative Names
ADAM9; ADAM metallopeptidase domain
Function
Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins.
Isoform 2: May act as alpha-secretase for amyloid precursor protein (APP).
Biological Process
Activation of MAPKK activity
Amyloid precursor protein catabolic process
Cell adhesion
Cell adhesion mediated by integrin
Cell-cell adhesion mediated by integrin
Cell-matrix adhesion
Cell migration
Cellular response to lipopolysaccharide
Integrin-mediated signaling pathway
Keratinocyte differentiation
Membrane protein ectodomain proteolysis
Membrane protein intracellular domain proteolysis
Monocyte activation
Positive regulation of cell adhesion mediated by integrin
Positive regulation of cell migration
Positive regulation of keratinocyte migration
Positive regulation of macrophage fusion
Positive regulation of membrane protein ectodomain proteolysis
Positive regulation of protein secretion
Protein processing
Response to calcium ion
Response to glucocorticoid
Response to hydrogen peroxide
Response to manganese ion
Response to tumor necrosis factor
Transforming growth factor beta receptor signaling pathway
Cellular Location
Isoform 1: Cell membrane
Isoform 2: Secreted
Involvement in disease
Cone-rod dystrophy 9 (CORD9): An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors.
Topology
Extracellular: 29-697 aa
Helical: 698-718 aa
Cytoplasmic: 719-819 aa
PTM
Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9.
Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA).

Buranaphatthana, W., Wu, S., Makeudom, A., Sastraruji, T., Supanchart, C., & Krisanaprakornkit, S. (2021). Involvement of the A disintegrin and metalloproteinase 9 in oral cancer cell invasion. European Journal of Oral Sciences, e12775.

Xiao, Y., Ma, W., Hu, W., Di, Q., Zhao, X., Ma, X., ... & Chen, W. (2021). Ubiquitin‐specific peptidase 39 promotes human glioma cells migration and invasion by facilitating ADAM9 mRNA maturation. Molecular Oncology.

Cui, L., Li, H., Xie, M., Xu, X., Zhang, Y., Wang, W., ... & Xiao, W. (2020). Relationship Between Proteinase with a Disintegrin and a Metalloproteinase Domain-9 (ADAM9), Inflammation, Airway Remodeling, and Emphysema in COPD Patients. International Journal of Chronic Obstructive Pulmonary Disease, 15, 3335.

Oh, S., Park, Y., Lee, H. J., Lee, J., Lee, S. H., Baek, Y. S., ... & Kwack, K. (2020). A disintegrin and metalloproteinase 9 (ADAM9) in advanced hepatocellular carcinoma and their role as a biomarker during hepatocellular carcinoma immunotherapy. Cancers, 12(3), 745.

Bazzone, L. E., King, M., MacKay, C. R., Kyawe, P. P., Meraner, P., Lindstrom, D., ... & Finberg, R. W. (2019). A disintegrin and metalloproteinase 9 domain (ADAM9) is a major susceptibility factor in the early stages of encephalomyocarditis virus infection. MBio, 10(1), e02734-18.

Hua, Y., Liang, C., Miao, C., Wang, S., Su, S., Shao, P., ... & Wang, Z. (2018). MicroRNA‑126 inhibits proliferation and metastasis in prostate cancer via regulation of ADAM9. Oncology letters, 15(6), 9051-9060.

Wang, X., Polverino, F., Rojas-Quintero, J., Zhang, D., Sánchez, J., Yambayev, I., ... & Owen, C. A. (2018). A disintegrin and metalloproteinase domain-9: a novel proteinase culprit with multifarious contributions to chronic obstructive pulmonary disease. American journal of respiratory and critical care medicine, 198(12), 1500-1518.

Qin, C., Zhao, Y., Gong, C., & Yang, Z. (2017). MicroRNA‑154/ADAM9 axis inhibits the proliferation, migration and invasion of breast cancer cells. Oncology letters, 14(6), 6969-6975.

Ask a question We look forward to hearing from you.
0 reviews or Q&As

Purchasing FAQs
Technical FAQs

Loading...
Have you used Mouse Anti-ADAM9 Recombinant Antibody (V2-6081)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

Online Inquiry

Documents

Contact us

  • Tel: (USA)
  • (UK)
  • Fax:
  • Email:

Submit A Review

Go to
Compare