Anti-Lin28 Antibody

Lin28 is a transcription factor that was first identified through its key role in the pathway of developmental timing in C. elegans. The role of Lin28 in development suggested that it might be useful in the creation of stem cells that might be beneficial in cell replacement therapies in the treatment of several degenerative diseases. Artificial stem cells, termed induced pluripotent stem (iPS) cells, can be created by expressing Lin28 in addition to the transcription factors POU5F1, Sox2, and NANOG in mouse fibroblasts. More recently, experiments have demonstrated that iPS cells could be generated using expression plasmids expressing Lin28, Sox2, POU5F1 and c-Myc, eliminating the need for virus introduction, thereby addressing a safety concern for potential use of iPS cells in regenerative medicine.

Lin28 antibody was raised against a 15 amino acid synthetic peptide near the carboxy terminus of human Lin28. The immunogen is located within the last 50 amino acids of Lin28.

RNA-binding protein that inhibits processing of pre-let- 7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876) . Seems to recognize a common structural G- quartet (G4) feature in its miRNA and mRNA targets (Probable) . 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let- 7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984) . Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity) .