Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
The remaining five patients were diagnosed with neonatal intrahepatic cholestasis due to citrin deficiency, and have respectively carried mutations of the SLC25A13 gene including [c.851-854delGTAT+c.851-854delGTAT], [c.851-854delGTAT+IVS6+5G>A], [c.851-854delGTAT+IVS16ins3kb], [c.851-854delGTAT+IVS6-11A>G] and [c.851-854delGTAT+c.1638-1660dup23]
Overexpression of ASL may be a contributing factor in drug resistance for arginine deprivation therapy.
ASL-targeting shRNA-induced growth inhibition is associated with decreased cyclin A2 expression and Nitric oxide content in colon cancer.
the mechanism induced by ASL shRNA which occurred in human breast cancer may be attributed to a decrease in cyclin A2 and NO.
The clinical and biochemical course in variant forms of ASL deficiency is associated with relevant residual levels of ASL activity as well as instability of mutant ASL proteins.
Point mutation of ASS1, ASL and SLC25A13 is associated with citrullinemia.
Data show that in patients with Argininosuccinate lyase deficiency, the ASl gene is subject to several mutations, the majority are missense; some more frequent then others.
Our results suggest that ASL transcripts can contribute to the highly variable phenotype in ASA patients if expressed at high levels.
Cox regression analysis showed that ASL is an independent prognostic marker for HCC. Therefore, reduced ASL expression may be a novel maker for poor prognosis in HCC patients
analysis of mutant argininosuccinate lyase in argininosuccinic aciduria
extent of protection of ASL and delta-crystallin at different ratios of alphaA-crystallin
MDR analysis provided evidence of interaction between the genes for ASS1 and SLC25A13 on the risk of CL/P.
Structural studies of the ASL frequently complementing allele Q286R suggest that the mutation may hinder a conformational change in the 280's loop (residues 270-290) and domain 3 that may be important for catalysis.
Complementation can occur at the ASL locus between thermolabile mutants and stable mutants by stabilization of the active oligomeric form of the hybrid enzyme, which may be sufficiently stable for catalysis to occur.
complete sequence of the human ASL gene and a complete ASL homologue on chromosome 22
argininosuccinic aciduria patients of different ethnic backgrounds who are characterized by residual activity of argininosuccinate lyase and who present with less severe clinical courses.
This unique mutation causes an elongation of fifty amino acids in the C-terminal region of the ASL protein, and is likely related to a milder phenotype compared with previously reported mutations.
a novel ASL pseudogene located in the centromeric region of chromosome 7, 14 novel mutations in the ASL gene, and a novel intronic polymorphism found in a cohort of Italian patients with argininosuccinic aciduria
analysis of human missense argininosuccinate lyase mutations in yeast
Enterocyte-derived ASL has a protective role in necrotizing enterocolitis.
In the case of NIT1, overall efficiency of recombination was 10 to 100 fold lower than with ARG7.
This gene encodes a member of the lyase 1 family. The encoded protein forms a cytosolic homotetramer and primarily catalyzes the reversible hydrolytic cleavage of argininosuccinate into arginine and fumarate, an essential step in the liver in detoxifying ammonia via the urea cycle. Mutations in this gene result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency. A nontranscribed pseudogene is also located on the long arm of chromosome 22. Alternatively spliced transcript variants encoding different isoforms have been described.
, argininosuccinate lyase