Anti-FPGT monoclonal antibody (DCABH-11614) Made to order

Rabbit anti-Human FPGT monoclonal antibody for WB, ELISA

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Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
Human
Immunogen
A synthetic peptide of human FPGT is used for rabbit immunization.
Conjugate
Unconjugated

Target


Alternative Names
FPGT; fucose-1-phosphate guanylyltransferase; GFPP; GDP-L-fucose diphosphorylase; GDP-beta-L-fucose pyrophosphorylase; fucose-1-phosphate guanyltransferase
Entrez Gene ID
UniProt ID

Product Background


Gene summary
FPGT (Fucose-1-Phosphate Guanylyltransferase) is a Protein Coding gene. Among its related pathways are Metabolism and Transport to the Golgi and subsequent modification. GO annotations related to this gene include transferase activity, transferring phosphorus-containing groups and fucose-1-phosphate guanylyltransferase activity. L-fucose is a key sugar in glycoproteins and other complex carbohydrates since it may be involved in many of the functional roles of these macromolecules, such as in cell-cell recognition. The fucosyl donor for these fucosylated oligosaccharides is GDP-beta-L-fucose. There are two alternate pathways for the biosynthesis of GDP-fucose; the major pathway converts GDP-alpha-D-mannose to GDP-beta-L-fucose. The protein encoded by this gene participates in an alternate pathway that is present in certain mammalian tissues, such as liver and kidney, and appears to function as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. This pathway involves the phosphorylation of L-fucose to form beta-L-fucose-1-phosphate, and then condensation of the beta-L-fucose-1-phosphate with GTP by fucose-1-phosphate guanylyltransferase to form GDP-beta-L-fucose. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream TNNI3 interacting kinase (TNNI3K) gene.
Antigen Description
L-fucose is a key sugar in glycoproteins and other complex carbohydrates since it may be involved in many of the functional roles of these macromolecules, such as in cell-cell recognition. The fucosyl donor for these fucosylated oligosaccharides is GDP-beta-L-fucose. There are two alternate pathways for the biosynthesis of GDP-fucose; the major pathway converts GDP-alpha-D-mannose to GDP-beta-L-fucose. The protein encoded by this gene participates in an alternate pathway that is present in certain mammalian tissues, such as liver and kidney, and appears to function as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. This pathway involves the phosphorylation of L-fucose to form beta-L-fucose-1-phosphate, and then condensation of the beta-L-fucose-1-phosphate with GTP by fucose-1-phosphate guanylyltransferase to form GDP-beta-L-fucose. Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. Fucose-1-phosphate guanylyltransferase is an enzyme that in humans is encoded by the FPGT gene. 0The function about FPGT antigen include GTP binding; catalytic activity; fucose-1-phosphate guanylyltransferase activity; nucleotide binding; nucleotidyltransferase activity.
Pathway
Amino sugar and nucleotide sugar metabolism, organism-specific biosystem; Amino sugar and nucleotide sugar metabolism, conserved biosystem; Fructose and mannose metabolism, organism-specific biosystem; Fructose and mannose metabolism, conserved biosystem; GDP-L-fucose biosynthesis II (from L-fucose), organism-specific biosystem; Metabolic pathways, organism-specific biosystem.

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References


Koffuor, GA; Woode, E; et al. Hypoglycaemic Activity of Tragia tennifolia (Euphorbiaceae) Extract in Rats. INTERNATIONAL JOURNAL OF PHARMACOLOGY 7:704-709(2011).
Wiltshire, SA; Leiva-Torres, GA; et al. Quantitative Trait Locus Analysis, Pathway Analysis, and Consomic Mapping Show Genetic Variants of Tnni3k, Fpgt, or H28 Control Susceptibility to Viral Myocarditis. JOURNAL OF IMMUNOLOGY 186:6398-6405(2011).

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