Description
Product Usage Information
Western Blotting: 1:1000
Immunofluorescence (Immunocytochemistry): 1:800
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody.
Protocol
Available protocols: Western Blotting, Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
ADAM12 (F9J1B) Rabbit Monoclonal Antibody recognizes endogenous levels of total ADAM12 protein. This antibody detects a 25 kDa protein of unknown identity in some cell lines. Knockdown of ADAM12 with siRNA elicits a decrease in the 25 kDa band, suggesting it may be target-related.
Species Reactivity: Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro896 of human ADAM12 protein.
Background
A disintegrin and metalloprotease (ADAM) family of multidomain membrane proteins influences cell signaling and adhesion by shedding cell surface proteins, such as cytokines and growth factors, influencing cell adhesion to the extracellular matrix (ECM), and directly remodeling the ECM. Conserved domains in ADAM family members include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2). The prodomain is thought to aid in protein folding, and disintegrin and cysteine-rich domains mediate adhesion, at least in part, through binding to integrins. Phosphorylation of the cytoplasmic tail and its interaction with other signaling proteins may influence intra- and extracellular signaling (1). ADAM12, an important member of the ADAM family, was initially identified as meltrin-alpha due to its expression in muscle cells. It is unique among many ADAMs for its complex role in organ development and its association with aggressive tumor phenotypes (2,3). ADAM12 is synthesized as an approximately 100 kDa precursor protein that undergoes post-translational processing by furin-like proteases to remove its prodomain, generating a mature, catalytically active enzyme. Notably, the gene generates two major alternatively spliced isoforms that dictate its cellular function and location: ADAM12-L (long form) and ADAM12-S (short/secreted form). ADAM12-L is the membrane-anchored form that contains all the conserved domains, including the transmembrane and cytoplasmic tails. It is the primary form involved in mediating cell-matrix interactions and direct cellular signaling. ADAM12-S is the secreted form, which lacks the transmembrane and cytoplasmic domains. It can circulate in the extracellular space and influence distant cells or act as a local regulator of the ECM (4). ADAM12 has been shown to be essential for developmental processes, such as muscle development, involving significant tissue remodeling, and in the cleavage of various ECM components and cell surface receptors, involving the protein's metalloprotease activity (5,6). The misregulation of ADAM12's normal functions drives several pathological states, making it a valuable cancer and disease target. ADAM12 is frequently overexpressed in various human malignancies, including pancreatic, breast, and colorectal cancer, where its presence is often associated with poor prognosis, and ADAM12-S in particular, promotes tumor growth and metastasis by enhancing the tumor cell's ability to migrate and invade, in part by stimulating angiogenesis (7,8). Through its role in regulating the synthesis and degradation of ECM components, aberrant ADAM12 activity has also been linked to the progression of fibrotic diseases in various organs (8).
Alternate Names
ADA12; ADAM 12; ADAM metallopeptidase domain 12; ADAM12; ADAM12-OT1; CAR10; Disintegrin and metalloproteinase domain-containing protein 12; MCMP; MCMPMltna; Meltrin-alpha; metalloprotease-disintegrin 12 transmembrane; MLTN; MLTNA
