GFPT1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q06210 |
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Clone Names | 90723045 |
Gene ID | 2673 |
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Other Names | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8887a was selected from the N-term region of human GFPT1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | GFPT1 |
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Synonyms | GFAT, GFPT |
Function | Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1 (By similarity). Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling (PubMed:26887390). |
Tissue Location | Isoform 1 is predominantly expressed in skeletal muscle. Not expressed in brain. Seems to be selectively expressed in striated muscle. |
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Provided below are standard protocols that you may find useful for product applications.
Background
GFPT1 is the first and rate-limiting enzyme of the hexosamine pathway and controls the flux of glucose into the hexosamine pathway. This protein catalyzes the formation of glucosamine 6-phosphate.
References
Eguchi,S., et.al., Genes Cells 14 (2), 179-189 (2009)Nakaishi,Y., et.al., FEBS Lett. 583 (1), 163-167 (2009)
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