POMT1- selective antibodies were generated against a peptide taken from the N-terminal region of the human protein. The POMT1-selective antibodies are affinity purified on an immobilized antigen based affinity matrix, the isolated antibodies were then stabilized in antibody stabilization buffer for long-term storage. The anti- POMT1-selective antibodies are fully characterized for applications in western blotting and ELISA at the recommended dilutions. antibodies-online.com provides POMT1 Western blot positive control samples in SDS-PAGE sample buffer.
Aufreinigung
Affinity Purified
Immunogen
Synthetic peptide taken within amino acid region 400-460 on human POMT1 protein.
Antibodies were tested in ELISA and western blotting applications at 1:500 dilution using ABIN1686541 samples. Antibody dilutions for these antibodies are for reference only, investigators are expected to determine the optimal conditions.Application of this antibody in other protocols has not yet tested. WB: > 1:500 IMM & IP pull-down assays: n.d. IHC: n.d. Investigators using this antibody in protocols other than listed above can request a complimentary sample of this antibody. n.d. not necessarily means the antibody is not suitable for that application, it simply means we have not yet characterized the antibody for that application. The antibody labels a strong band of POMT1 at 57 kDa in ABIN1686541 samples and in other cancer cell lines.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
0.55-0.75 μg/μL
Lagerung
-20 °C
Informationen zur Lagerung
Storage of very dilute antibody solutions is not recommended.
Protein O mannosylation is initiated in the endoplasmic reticulum by protein O-mannosyl transferases (POMT proteins). They play an important role in the secretion, localization, and function of many proteins, as well as in cell wall integrity and morphogenesis in fungi. On the molecular level, the O-mannosylation pathway and the function of O-mannosyl glycans are characterized best in the eukaryotic model yeast Saccharomyces cerevisiae. O-mannosylation defects interfere with cell wall integrity and ER homeostasis in yeast, resulting in severe neuromuscular diseases in humans. Transfer of this knowledge from yeast to mammals could lead to the development of novel antifungal drugs by diagnostic and therapeutic approaches in the frame of neuromuscular diseases. The POMT family is classified into POMT1, POMT2 and POMT4 subfamilies. Protein-O-Mannosyl Transferase 1 (POMT1) is a glycosyltransferase involved in α-dystroglycan (α-DG) glycosylation. The POMT1 (protein O-mannosyl transferase 1) protein consists of 747 amino acids with seven to twelve transmembrane regions and a C-terminal ER membrane retention signal. RT-PCR reveals several mRNA splice variants. RNA dot blot analysis indicates ubiquitous expression of POMT1, with maximum levels in testis and high levels in fetal brain and pituitary tissues. Walker-Warburg syndrome (WWS), a severe, recessive, congenital muscular dystrophy associated with defects in neuronal migration that produce complex brain and eye abnormalities, is caused by mutations in the POMT1 gene. A defect in this gene also causes limb-girdle muscular dystrophy type 2K (LGMD 2K). POMT1 is an O-mannosyl transferase that requires interaction with the product of the POMT2 gene for enzymatic function. Several transcript variants encoding different isoforms exist for this gene. In yeast, cell morphology and cell-cell separation are affected by lack of O-mannosylation resulting in abnormal cell wall and septum formation. The gene for POMT1 is present on chromosome 9q34.1