AI Article Synopsis
- The study aimed to create monoclonal antibodies (mAbs) targeting the UDP-glucose pyrophosphorylase 2 (UGP2) enzyme in humans using hybridoma techniques.
- Human liver tissue was used to immunize mice, and the mAbs were identified through ELISA, Western blot, and immunohistochemistry methods, producing one specific mAb, BAD062.
- The BAD062 mAb was shown to specifically bind to UGP2 in liver cells with a molecular weight of 56 kD, and it is confirmed as a valuable tool for further UGP2 research.
Article Abstract
The study was aimed to generate monoclonal antibodies (mAbs) against homo sapiens UDP-glucose pyrophosphorylase 2 (UGP2). Normal human liver tissues homogenized, and cytosolic proteins isolated by centrifugation were used to immunize BALB/c mice to generate mAbs by hybridoma technique. The mAbs were identified by ELISA, Western blot, and immunohistochemistry assay. The antibody specificity was confirmed by Uni-ZAP expression library screening. The results indicated that one hybridoma BAD062 secreting specific mAb against UGP2 was established. The Ig subclass of this mAb was IgG(2b) (kappa), and it could be used in ELISA, Western blot, immunohistochemistry assay. The antigen recognized by BAD062 mAb was localized in the hepatocyte cytoplasm, with molecular weight of 56 kD in the cytosolic proteins of human liver tissue. The BAD062 mAb was further confirmed by immunoscreening of Uni-ZAP XR liver cDNA expression library. It is concluded that a hybridoma cell line stably secretes specific mAb against UGP2. This mAb reacted with UGP2 in ELISA, Western blot, immunohistochemistry assay, and would be very useful for the UGP2 studies.
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