LpxC Protein, E.coli (His)
Based on 1 Customer Validation
LpxC protein serves as a key enzyme in lipid A biosynthesis by catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine, marking a key and crucial step in this important pathway. Through this enzymatic process, LpxC promotes the conversion of its substrate into UDP-3-O-myristoylglucosamine and acetate, making a significant contribution to lipid A biosynthesis. LpxC Protein, E.coli (His) is the recombinant E. coli-derived LpxC protein, expressed by E. coli , with N-His labeled tag.
- Species: E.coli
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
LpxC protein serves as a key enzyme in lipid A biosynthesis by catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine, marking a key and crucial step in this important pathway. Through this enzymatic process, LpxC promotes the conversion of its substrate into UDP-3-O-myristoylglucosamine and acetate, making a significant contribution to lipid A biosynthesis. LpxC Protein, E.coli (His) is the recombinant E. coli-derived LpxC protein, expressed by E. coli , with N-His labeled tag.
LpxC is an enzyme that plays a crucial role in lipid A biosynthesis by catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine. This reaction results in the formation of UDP-3-O-myristoylglucosamine and acetate, representing the committed step in the biosynthesis of lipid A, a key component of bacterial lipopolysaccharides. Lipid A is an essential structural element in the outer membrane of Gram-negative bacteria, contributing to membrane integrity and playing a role in host-pathogen interactions. LpxC's catalytic activity is pivotal for the production of lipid A, and the enzyme serves as a potential target for the development of antibacterial agents aimed at disrupting the synthesis of crucial bacterial cell wall components.
The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.
Technical Parameters
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Species E.coli
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Source E. coli
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Tag N-His
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Accession
P0A725 (M1-A305)
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Gene ID944816 [NCBI]
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Molecular Construction
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N-term
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His
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LpxC (M1-A305)
Accession # P0A725 -
C-term
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Protein Length
Full Length
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Synonyms
UDP-3-O-acyl-N-acetylglucosamine deacetylase; EC:3.5.1.108; UDP-3-O-acyl-GlcNAc deacetylase; Protein EnvA; UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase; lpxC; asmB; envA; b0096; JW0094
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AA Sequence
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA
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Predicted Molecular Mass
38 kDa
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.22 μm filtered solution of 10 mM Tris-HCl, 1 mM EDTA, 6% trehalose, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (237 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)