Recombinant ADAM12 Monoclonal Antibody (AN300106P)
For research use only.
| Verified Samples | Verified Samples in WB: A431 |
| Dilution | WB 1:500-1:1000, |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Rabbit Monoclonal |
| Immunogen | Recombinant Human ADAM12 protein |
| Abbre | ADAM12 |
| Synonyms | CAR, UNQ, PRO, ADAM, ADAM12-OT, ADAM12, ADAM12-OT1, CAR10, MCMP, MCMPMltna, MLTN, MLTNA, UNQ346, PRO545, A disintegrin and metalloproteinase domain 12, ADA12, ADAM 12, ADAM metallopeptidase domain 12, Disintegrin and metalloproteinase domain-containing protein 12, Meltrin alpha, Meltrin-alpha, Metalloprotease disintegrin 12 transmembrane, OTTHUMP00000046766 |
| Swissprot | |
| Calculated MW | 100 kDa |
| Observed MW |
100 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cancer, Cell Biology |
| Clone No. | 11G10 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported. |
Other Clones
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Unconjugated
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