Recombinant E.Coli Udp-3-O-Acyl-N-Acetylglucosamine Deacetylase (LPXC) Protein (His-SUMO)

Name: Recombinant E.Coli Udp-3-O-Acyl-N-Acetylglucosamine Deacetylase (LPXC) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02264P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) lpxC.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant E.Coli Udp-3-O-Acyl-N-Acetylglucosamine Deacetylase (LPXC) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P0A725
Target Symbol	LPXC
Synonyms	lpxC; asmB; envA; b0096; JW0094; UDP-3-O-acyl-N-acetylglucosamine deacetylase; UDP-3-O-acyl-GlcNAc deacetylase; EC 3.5.1.108; Protein EnvA; UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA
Expression Range	1-305aa
Protein Length	Full Length
Mol. Weight	49.8kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Protein Families	LpxC family
Database References	KEGG: ecj:JW0094 STRING: 316385.ECDH10B_0078

Gene Functions References

analysis of mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis PMID: 23316051
the active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions PMID: 20709752
The C-terminus of LpxC contains a signal sequence necessary for FtsH-dependent degradation. PMID: 16420369
potency of LpxC inhibitors in vitro can be altered by assay conditions and development of inhibitorsand that the metal ion status of LpxC in vivo may influence the effectiveness of LpxC inhibitors as antibiotics. PMID: 17144651
Functions of LpxC active site residues have been classified on the basis of changes in steady-state turnover and product binding affinity; side chains are identified that enhance and destabilize product affinity as well as enhance catalytic efficiency. PMID: 17176046
A C-terminal tail of about 20 amino acids length is required for proteolysis of LpxC by FtsH PMID: 17651755

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.