Mouse Recombinant ADAM9 protein, His Tag (V2LY-0526-LY7781)

Name: Mouse Recombinant ADAM9 protein, His Tag
SKU: V2LY-0526-LY7781
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Mouse

Tag

His Tag

Protein Construction

This product is Mouse Recombinant ADAM9 protein, His Tag consist of Amino Acid: 1-697 and predicts a molecular mass of 74.9 kDa.

Molecule Mass

74.9 kDa

Sequence

Amino Acid: 1-697

Species

Mouse

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

Purity

≥85% as determined by SDS-PAGE.

Endotoxin

Please contact us for more information.

Format

Liquid

Buffer

PBS

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

ADAM metallopeptidase domain 9 (meltrin gamma)

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.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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