lpxC polyclonal antibody CSB-PA358910HA01ENV was produced in the rabbit immunized by using the Recombinant Escherichia coli UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase protein (1-305AA) as the immunogen. The target protein lpxC plays a critical role in catalyzing the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. Due to its important role in lipid A synthesis, LpxC is an attractive target for the development of new antibacterial agents to treat Gram-negative infections.
This Rabbit anti-Escherichia coli (strain K12) lpxC Polyclonal antibody was tested in the ELISA. The non-conjugated IgG got purified by protein G and reached up to 95% in purity. It only reacts with the lpxC proteins of Escherichia coli-origin and may be used to detect the endogenous levels of lpxC protein.
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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Tested application: WB, IP Test sample&species: E.coli Primary antibody dilution ratio: 1:1000 Review: The experimental results are OK, but there are bands, which may be related to polyclonal antibodies. Also used for IP, although the manual is only ELISA.
靶點詳情
功能:
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.
基因功能參考文獻:
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