GNPDA2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q8TDQ7 |
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Gene ID | 132789 |
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Other Names | Glucosamine-6-phosphate isomerase 2, Glucosamine-6-phosphate deaminase 2, GNPDA 2, GlcN6P deaminase 2, Glucosamine-6-phosphate isomerase SB52, GNPDA2, GNP2 |
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 | GNPDA2 {ECO:0000303|PubMed:26887390} |
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Synonyms | GNP2 |
Function | Catalyzes the reversible conversion of alpha-D-glucosamine 6- phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion, a regulatory reaction step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via hexosamine pathway. Deamination is coupled to aldo-keto isomerization mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high ammonium level can drive amination and isomerization of Fru-6P toward hexosamines and UDP-GlcNAc synthesis. Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on hyaluronan synthesis that occur during tissue remodeling. |
Cellular Location | Cytoplasm. |
Tissue Location | Ubiquitous, with highest expression detected in testis, ovary, placenta, and heart. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium (Arreola et al., 2003 [PubMed 12965206]).
References
He, M., et al. Arterioscler. Thromb. Vasc. Biol. 30(2):327-332(2010)Li, S., et al. Am. J. Clin. Nutr. 91(1):184-190(2010)Hotta, K., et al. J. Hum. Genet. 54(12):727-731(2009)
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