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Assay Range | 156 - 10,000 pg/mL |
Sensitivity | 10.0 pg/mL |
Size | 96T |
Storage | Store at 2 - 8ºC. Keep reconstituted standard and detection Ab at -20 ºC |
Assay Principle | Sandwich ELISA |
Sample volume | 100 µL final volume, dilution factor varies on samples. |
Detection Method | Chromogenic |
Kit Components
1. Recombinant Human ADAM12 standard: 2 vials.
2. One 96-well plate precoated with anti- Human ADAM12 Ab
3. Sample diluent buffer: 12 mL - 1
4. Detection antibody: 130 µL, dilution 1:100.
5. Streptavidin-HRP: 130 µL, dilution 1:100
6. Antibody diluent buffer: 12 mL x1
7. Streptavidin-HRP diluent buffer: 12 mL x1
8. TMB developing agent: 10 mL x1
9. Stop solution: 10 mL x1.
10. Washing solution (20x): 25 mL x1.
Background
A Disintegrin And Metalloproteinase domain-containing protein 12 (ADAM12), also known as Meltrin-alpha, is a member of the ADAM metalloproteinase family. It is a single chain polypeptide composed of a signal peptide, pro-peptide, metalloproteinase, disintegrin, cystein-rich, and EGF-like domains, as well as the transmembrane segment and cytoplasmic tail. Two alternatively spliced forms of ADAM12 have been described: a membrane-bound long form and a shorter secreted form. ADAM12 is initially synthesized as an inactive enzyme and is then activated by a furin-like protease in the trans-Golgi apparatus through cleavage of the pro-peptide before it is transported to the cell surface and secreted as the active form. Endogenous inhibitors for ADAM12 include TIMP-3 and α2-macroglobulin. The soluble form of ADAM12 is detectable in various body fluids, such as serum and urine.
ADAM12 may play important roles in cell adhesion and extracellular matrix degradation. It can cleave extracellular matrix proteins, such as gelatin, type IV collagen, and fibronectin. Overexpression of ADAM12 has been observed in various types of cancer. It is reported that, in mouse prostate cancer, ADAM12 is highly expressed in the carcinoma- associated stroma, and it is required for tumor progression. In breast cancer patients, ADAM12 is significantly increased in the urine compared to healthy controls. ADAM12 may also be involved in cell signal transduction. It has been shown that ADAM12 can facilitate the phosphorylation of Smad2 and the stabilization of the TGF-β receptor type II. Recently, it is reported that ADAM12 may play a role in skeletal muscle regeneration, specifically at the onset of cell fusion.