The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
ABHD10 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
ABHD10 cDNA ORF Clone in Cloning Vector, Human: Alternative Names
ABHD10 cDNA ORF Clone, Human
ABHD10 Background Information
Mycophenolic acid (MPA), the active metabolite of the immunosuppressant mycophenolate mofetil (MMF), is primarily metabolized by glucuronidation to a phenolic glucuronide (MPAG) and an acyl glucuronide (AcMPAG). It is known that AcMPAG, which may be an immunotoxic metabolite, is deglucuronidated in human liver. AcMPAG deglucuronidation activity was detected in both human liver cytosol (HLC) and microsomes (HLM). By purification from HLC with column chromatographic purification steps, the enzyme responsible for AcMPAG deglucuronidationis identified as α/β hydrolase domain containing 1 (ABHD1). Recombinant ABHD1 expressed in Sf9 cells efficiently deglucuronidated AcMPAG with a K(m) value of 1.7 ± 1.2 μM, which was similar to those in HLM, HLC, and human liver homogenates (HLH). Immunoblot analysis revealed ABHD1 protein expression in both HLC and HLM. The AcMPAG deglucuronidation by recombinant ABHD1, HLC, and HLH were potently inhibited by AgNO(3), CdCl(2), CuCl(2), PMSF, bis-p-nitrophenylphosphate, and DTNB. The CL(int) value of AcMPAG formation from MPA, which was catalyzed by human UGT2B7, in HLH was increased by 1.8-fold in the presence of PMSF. Thus, human ABHD1 would affect the formation of AcMPAG, the immunotoxic metabolite.
abhydrolase domain containing 10
Nardini M. et al., 1999, Curr Opin Struct Biol. 9 (6): 732-7.
Carr PD. et al., 2009, Protein Pept Lett. 16 (10): 1137-48.
Cheah E. et al., 1992, Protein Eng. 5 (3): 197-211.
Iwamura A. et al., 2012, J Biol Chem. 287 (12): 9240-9.
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