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Rat Anti-ADAM9 Recombinant Antibody (V2-179807) (CBMAB-A1170-YC)


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Summary

Host Animal
Rat
Specificity
Mouse
Clone
V2-179807
Antibody Isotype
IgG2
Application
WB

Basic Information

Immunogen
Purified Recombinant ADAM9 extracellular domain
Host Species
Rat
Specificity
Mouse
Antibody Isotype
IgG2
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
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
ADAM9 is 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 involvin
Entrez Gene ID
11502
UniProt ID
Q61072
Alternative Names
ADAM Metallopeptidase Domain 9; Metalloprotease/Disintegrin/Cysteine-Rich Protein 9; Cellular Disintegrin-Related Protein; Myeloma Cell Metalloproteinase; Cone Rod Dystrophy 9; Mltng; MCMP; MDC9; Disintegrin And Metalloproteinase Domain-Containing Protein
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).
More Infomation

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.

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For research use only. Not intended for any clinical use.

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