OGT antibody

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935106861
info@markelab.com
name
OGT antibody
category
Primary Antibodies
provider
FineTest
reference
FNab05981
tested applications
ELISA, WB, IHC
Description
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) (OGT) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | WB: 1:500 - 1:2000; IHC: 1:50 - 1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 117 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IHC |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months (Avoid repeated freeze / thaw cycles.) |
UniProt ID | O15294 |
Gene ID | 8473 |
Alias | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit,O-GlcNAc transferase subunit p110,O-linked N-acetylglucosamine transferase 110 kDa subunit (OGT),OGT |
Background | Antibody anti-OGT |
Status | RUO |
Note | Mol. Weight 117 kDa |
Descripción
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Human OGT (UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit) ELISA Kit
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OGT antibody
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Ver Producto