S1826
Sialic Acid Aldolase from Escherichia coli K12
recombinant, expressed in E. coli BL21, ≥3.0 units/mg protein
Sinônimo(s):
N-Acetylneuraminate lyase, N-Acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
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About This Item
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
recombinante
expressed in E. coli BL21
Nível de qualidade
Formulário
lyophilized powder
atividade específica
≥3.0 units/mg protein
peso molecular
33.4 kDa
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
Descrição geral
Sialic acid aldolases, or N-acetylneuraminate lyases, catalyze the reversible aldol cleavage of N-acetylneuraminic acid to form pyruvate and N-acetyl-D-mannosamine. In nature, N-acetylneuraminate lyase mainly occurs in pathogens.
Aplicação
Sialic acid aldolase can be used to synthesize unnatural sugars of C(6) to C(10) for the design of antagonists and inhibitors of glycoenzymes.
Definição da unidade
One unit will catalyze the formation of 1.0 μmol Neu-5-Ac from Man-N-Ac and pyruvate per minute at 37°C at pH 8.0.
forma física
Lyophilized powder containing Tris-HCl and NaCl
Nota de análise
Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 7.5) containing Neu-5-Ac (10 mM) at 37 °C for 15 min and analyzed using capillary electrophoresis with UV detection at 200 nm.
Palavra indicadora
Warning
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251.
Chien-Yu Chou et al.
The Journal of biological chemistry, 286(16), 14057-14064 (2011-01-29)
In a recent directed-evolution study, Escherichia coli D-sialic acid aldolase was converted by introducing eight point mutations into a new enzyme with relaxed specificity, denoted RS-aldolase (also known formerly as L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase), which showed a preferred selectivity toward
Guiomar Sánchez-Carrón et al.
Applied and environmental microbiology, 77(7), 2471-2478 (2011-02-15)
N-Acetylneuraminate lyases (NALs) or sialic acid aldolases catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-d-mannosamine (ManNAc). In nature, N-acetylneuraminate lyase occurs mainly in pathogens. However, this paper describes how an N-acetylneuraminate lyase was cloned
Jozef Nahálka et al.
Organic & biomolecular chemistry, 7(9), 1778-1780 (2009-07-11)
Active inclusion bodies of polyphosphate kinase 3 and cytidine 5'-monophosphate kinase were combined with whole cells that co-express sialic acid aldolase and CMP-sialic acid synthetase. The biocatalytic mixture was used for the synthesis of CMP-sialic acid, which was then converted
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