NanA (AA 1-297) protein (His tag)
Origin: E. coli
Host: Escherichia coli (E. coli)
Recombinant
> 95 % by SDS - PAGE
SDS
1 image
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- Target
- NanA
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-297
- Origin
- E. coli
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Application
- SDS-PAGE (SDS)
- Characteristics
- nanA, 1-297aa, E.coli, His tag, E.coli
- Purity
- > 95 % by SDS - PAGE
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NanA (AA 1-297) protein (His tag)
Origin: E. coli Host: Escherichia coli (E. coli) Recombinant SDS
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- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/ml (determined by Bradford assay)
- Buffer
- Liquid. 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol
- Storage
- 4 °C
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- Target
- NanA
- Background
- NanA, also known as N-acetylneuraminate lyase, belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. This protein was inhibited by reduction with NaBH4 in the presence of the substrate, indicating that it belongs to the Schiff-base-forming Class I aldolases. NanA was strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, and also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde. Recombinant E.coli nanA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. Synonyms: N-acetylneuraminate lyase, npl. NCBI no.: NP_417692
- Molecular Weight
- 34.7 kDa (317aa) confirmed by MALDI-TOF
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