Code | CSB-RA797631A0HU |
Size | US$210 |
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Application | Recommended Dilution |
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IF | 1:20-1:200 |
ADAM17 antibody-producing hybridomas were formed by the fusion of myeloma cells to B lymphocytes. B cells were isolated from the animal that was immunized with a synthetic peptide derived from human ADAM17. The variable light and variable heavy domains of the hybridomas were sequenced to construct a vector for recombinant generation. The ADAM17 monoclonal antibody gene-containing vector was then transfected into cells for cultivation, and the ADAM17 recombinant monoclonal antibody was isolated and purified using affinity chromatography from the cell culture supernatant. The purified antibody's specificity was verified through ELISA and IF applications, where it only detected human ADAM17 protein.
ADAM17, also known as TACE, is involved in the proteolytic cleavage of a wide variety of cell surface proteins, including cytokines, growth factors, and adhesion molecules. ADAM17 has been implicated in various physiological and pathological processes, such as inflammation, cancer, and development. ADAM17 has also been implicated in the shedding of adhesion molecules such as E-cadherin and L-selectin, which can affect cell-cell interactions and migration. ADAM17 has also been shown to cleave the transmembrane protein Notch, which is involved in cell fate determination and differentiation.
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