|Other Names||Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, UDP-GlcNAc-2-epimerase/ManAc kinase, UDP-N-acetylglucosamine 2-epimerase (hydrolyzing), UDP-GlcNAc-2-epimerase, Uridine diphosphate-N-acetylglucosamine-2-epimerase, N-acetylmannosamine kinase, ManAc kinase, GNE, GLCNE|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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.|
|Function||Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development (By similarity). Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells.|
|Tissue Location||Highest expression in liver and placenta. Also found in heart, brain, lung, kidney, skeletal muscle and pancreas Isoform 1 is expressed in heart, brain, kidney, liver, placenta, lung, spleen, pancreas, skeletal muscle and colon. Isoform 2 is expressed mainly in placenta, but also in brain, kidney, liver, lung, pancreas and colon. Isoform 3 is expressed at low level in kidney, liver, placenta and colon.|
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Provided below are standard protocols that you may find useful for product applications.
GNE is a bifunctional enzyme that initiates and regulates the biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It is a rate-limiting enzyme in the sialic acid biosynthetic pathway. Sialic acid modification of cell surface molecules is crucial for their function in many biologic processes, including cell adhesion and signal transduction. Differential sialylation of cell surface molecules is also implicated in the tumorigenicity and metastatic behavior of malignant cells.
Reinke, S.O., et al. Glycoconj. J. 26(4):415-422(2009)Tong, Y., et al. PLoS ONE 4 (10), E7165 (2009) Klootwijk, R.D., et al. FASEB J. 22(11):3846-3852(2008)
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