What form of ADAM9 does this antibody recognize? Can it detect both the pro- and mature forms?

This antibody was generated against the extracellular domain of human ADAM9. It is capable of detecting both the full-length pro-form (zymogen) of ADAM9, which runs at approximately 110-120 kDa, and the proteolytically processed, mature/active form, which is typically observed at ~84 kDa in Western Blots. The relative abundance of these forms can vary by cell type and physiological state.

Has this antibody been tested for cross-reactivity with other species or ADAM family members?

This antibody is specific for human ADAM9. Cross-reactivity with ADAM9 from other species has not been confirmed by Creative Biolabs and would need to be tested by the user. Due to its recombinant monoclonal nature, cross-reactivity with other human ADAM family proteins is minimal, but we always recommend running appropriate controls, such as using lysates from ADAM9-knockout/knockdown cells, to verify specificity in your system.

Rabbit Anti-ADAM9 Recombinant Antibody (V2-179804) (CBMAB-A1167-YC)

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Datasheet

SDS

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

Basic Information

Host Animal

Rabbit

Clone

V2-179804

Application

Immunogen

Synthetic peptide corresponding to residues near the carboxy terminus of human ADAM9

Host Species

Rabbit

Specificity

Human, Monkey, Mouse, Rat

Antibody Isotype

IgG

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1:1,000

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

Format

Liquid in 10 mM sodium HEPES pH 7.5, 150 mM NaCl, 100 mg/mL BSA, 0.02% sodium azide, 50% glycerol

Buffer

10mM sodium HEPES, pH7.5, 0.1mg/ml BSA, 50% glycerol

Preservative

0.02% sodium azide

Concentration

Batch dependent

Storage

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Epitope

C-terminus

More Infomation

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

Human	8754
Mouse	11502
Rat	290834
Monkey	701124

UniProt ID

Human	Q13443
Mouse	Q61072
Rat	Q58GH6
Monkey	F6SG12

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).

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)
Proteogenomics
Other Protocols

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Mouse Anti-ADAM9 Recombinant Antibody (V2-258053) (CAT#: CBMAB-M0986-FY)

Isotype control

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

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