|Application ||WB, E|
|Calculated MW||37376 Da|
|Antigen Region||300-330 aa|
|Other Names||N-acetyl-D-glucosamine kinase, N-acetylglucosamine kinase, GlcNAc kinase, NAGK|
|Target/Specificity||This NAGK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 300-330 amino acids from the C-terminal region of human NAGK.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NAGK Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity.|
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Provided below are standard protocols that you may find useful for product applications.
N-acetylglucosamine kinase (NAGK) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine kinases and is a prominent salvage enzyme of amino sugar metabolism in mammals. The predicted 344-amino acid NAGK protein contains the 5 sequence motifs necessary for the binding of ATP by sugar kinases. NAGK shares 91.6% amino acid similarity with mouse Nagk, for which enzyme activity is detectable in all mouse tissues examined, with highest enzymatic activity in testis. It is hypothesized that NAGK has a general role in the catabolic pathways of GlcNAc as well as of ManNAc.
Hinderlich, S., et al., Eur. J. Biochem. 267(11):3301-3308 (2000).
Lowes, W., et al., Biochim. Biophys. Acta 1379(1):134-142 (1998).
Weidanz, J.A., et al., Br. J. Haematol. 95(4):645-653 (1996).
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