Reactivity | MuSpecies Glossary |
Applications | WB |
Clone | 122823 |
Clonality | Monoclonal |
Host | Rat |
Conjugate | Unconjugated |
Immunogen | Mouse myeloma cell line NS0-derived recombinant mouse ADAM9 Ala205-Cys673 Accession # Q61072 |
Specificity | Detects mouse ADAM9 in direct ELISAs and Western blots. In direct ELISAs, approximately 5% cross-reactivity with recombinant human (rh) ADAM9 is observed and no cross-reactivity with rhADAM8, recombinant mouse ADAM10, rhADAM15, rhBACE, or rhTACE is observed. In Western blots, approximately 100% cross-reactivity with rhADAM9 and rmADAM15 is observed and less than 5% cross-reactivity with rmADAM10 is observed. |
Source | N/A |
Isotype | IgG2a |
Clonality | Monoclonal |
Host | Rat |
Gene | ADAM9 |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
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).
Secondary Antibodies |
Isotype Controls |
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