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Recombinant Human NANS (E.coli, N-6His)

Cat. No. M21617
Recombinant Human NANS (E.coli, N-6His) Structure
Synonym:

N-Acetylneuraminate Synthase

Size Price Availability Quantity
10ug USD 185  USD185 In stock
50ug USD 455  USD455 In stock
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Quality Control & Documentation
  • Purity: >95%, Endotoxin < 1 EU/μg
  • COA
  • MSDS
Biological Activity

N-Acetylneuraminate Synthase (NANS) is an enzyme that contains one AFP-like domain. NANS is ubiquitous and plays a role in the biosynthetic pathways of sialic acids. Recombinant Human N-Acetylneuraminate Synthase is produced by E.coli expression system and the target gene encoding Met1-Ser359 is expressed with a 6His tag at the N-terminus. NANS produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). It also can use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

Chemical Information
Solubility (25°C) Water
Saline
PBS
Storage Store at ≤-70°C, stable for 6 months after receipt
Conversion of different model animals based on BSA (PMID: 27057123)
Species Mouse Rat Rabbit Guinea pig Hamster Dog
Weight (kg) 0.02 0.15 1.8 0.4 0.08 10
Body Surface Area (m2) 0.007 0.025 0.15 0.05 0.02 0.5
Km factor 3 6 12 8 5 20
Animal A (mg/kg) = Animal B (mg/kg) multiplied by  Animal B Km
Animal A Km

For example, to modify the dose of Compound A used for a mouse (20 mg/kg) to a dose based on the BSA for a rat, multiply 20 mg/kg by the Km factor for a mouse and then divide by the Km factor for a rat. This calculation results in a rat equivalent dose for Compound A of 10 mg/kg.

References

[1] S Feuerbaum, et al. Int J Med Microbiol. De-O-Acetylation of mucin-derived sialic acids by recombinant NanS-p esterases of Escherichia coli O157:H7 strain EDL933

[2] Nadja Saile, et al. Int J Med Microbiol. Growth advantage of Escherichia coli O104:H4 strains on 5-N-acetyl-9-O-acetyl neuraminic acid as a carbon source is dependent on heterogeneous phage-Borne nanS-p esterases

[3] Nadja Saile, et al. Appl Environ Microbiol. Escherichia coli O157:H7 Strain EDL933 Harbors Multiple Functional Prophage-Associated Genes Necessary for the Utilization of 5-N-Acetyl-9-O-Acetyl Neuraminic Acid as a Growth Substrate

[4] Chatchawal Phansopa, et al. Biochem J. Characterization of a sialate-O-acetylesterase (NanS) from the oral pathogen Tannerella forsythia that enhances sialic acid release by NanH, its cognate sialidase

[5] Michael John Aldape, et al. J Infect Dis. The leukemoid reaction in Clostridium sordellii infection: neuraminidase induction of promyelocytic cell proliferation

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Keywords: Recombinant Human NANS (E.coli, N-6His), N-Acetylneuraminate Synthase supplier, Recombinant Proteins, inhibitors, activators


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