Synthetic peptide directed towards the C terminal region of human C3orf64
Application
Anti-C3ORF64 antibody produced in rabbit is suitable for western blotting at a concentration of 1.0μg/ml.
Biochem/physiol Actions
C3ORF64 is popular as EGF domain-specific O-linked N-acetylglucosamine (GlcNAc) transferase (EOGT; AOS4) is an O-GlcNAc transferase located in the endoplasmic reticulum. It catalyzes the addition of β-linked GlcNAc on Ser or Thr of EGF repeats. Mutations in EOGT gene reportedly result in genetic heterogeneity of Adams-Oliver Syndrome.
Sequence
Synthetic peptide located within the following region: GHHPTLGEHPKFTNYSFDVEEFMYLVLQAADHVLQHPKWPFKKKHDEL
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Proceedings of the National Academy of Sciences of the United States of America, 109(19), 7280-7285 (2012-04-21)
O-linked N-acetylglucosamine (O-GlcNAc) is a reversible posttranslational modification of Ser and Thr residues on cytosolic and nuclear proteins of higher eukaryotes catalyzed by O-GlcNAc transferase (OGT). O-GlcNAc has recently been found on Notch1 extracellular domain catalyzed by EGF domain-specific OGT.
American journal of human genetics, 92(4), 598-604 (2013-03-26)
Adams-Oliver syndrome (AOS) is a rare, autosomal-dominant or -recessive disorder characterized primarily by aplasia cutis congenita and terminal transverse limb defects. Recently, we demonstrated that homozygous mutations in DOCK6 cause an autosomal-recessive form of AOS. In this study, we sought
The O-GlcNAc transferase Eogt modifies EGF repeats in proteins that transit the secretory pathway, including Dumpy and Notch. In this paper, we show that the Notch ligands Delta and Serrate are also substrates of Eogt, that mutation of a putative
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