ALG12 Antibody (Q16): sc-100507

ALG12 Antibody (Q16) is a mouse monoclonal IgG1 kappa light chain antibody that detects ALG12 protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-ALG12 antibody (Q16) is available as the non-conjugated monoclonal isotype antibody. ALG12, also known as asparagine-linked glycosylation 12 homolog, ECM39, or membrane protein SB87, is a crucial 488 amino acid member of the glycosyltransferase 22 family, functioning primarily as a mannosyltransferase essential for proper protein glycosylation. ALG12 is predominantly located in the endoplasmic reticulum, where ALG12 plays a vital role in the addition of α1,6 mannose to dolichol-linked Man7GlcNAc2, a critical step in the N-glycosylation pathway. ALG12′s significance is underscored by the fact that defects can lead to congenital disorder of glycosylation type 1G (CDG1G), a multisystem disease characterized by under-glycosylated serum proteins, which can result in severe clinical manifestations such as coagulation disorders, psychomotor retardation, hypotonia, immunodeficiency, and dysmorphic features. Proper functioning of N-glycoproteins, which heavily rely on the glycosylation process facilitated by ALG12, is essential for various cellular processes, including cell maintenance, embryonic development, and differentiation, highlighting ALG12 monoclonal antibody (Q16)′s importance in research and diagnostic applications.

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ALG12 Antibody (Q16) References:

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2. The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols.  |  Grimme, SJ., et al. 2001. J Biol Chem. 276: 27731-9. PMID: 11356840
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7. The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases.  |  Samuelson, J., et al. 2005. Proc Natl Acad Sci U S A. 102: 1548-53. PMID: 15665075
8. Hydrophobic Man-1-P derivatives correct abnormal glycosylation in Type I congenital disorder of glycosylation fibroblasts.  |  Eklund, EA., et al. 2005. Glycobiology. 15: 1084-93. PMID: 16079417
9. Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.  |  Belanger, KD., et al. 2005. Genetics. 171: 935-47. PMID: 16118201