Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
ASPA encodes an enzyme that catalyzes the conversion of N-acetyl_L-aspartic acid (NAA) to aspartate and acetate. Additionally we are shipping ASPA Proteins (14) and ASPA Kits (5) and many more products for this protein.
Showing 10 out of 74 products:
Human Monoclonal ASPA Primary Antibody for ELISA, WB - ABIN393318
Joslyn, Ravindranathan, Brush, Schuckit, White: Human variation in alcohol response is influenced by variation in neuronal signaling genes. in Alcoholism, clinical and experimental research 2010
Show all 5 references for ABIN393318
Chicken Polyclonal ASPA Primary Antibody for WB - ABIN2786498
Le Coq, Pavlovsky, Malik, Sanishvili, Xu, Viola: Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue. in Biochemistry 2008
Human Polyclonal ASPA Primary Antibody for EIA, FACS - ABIN452768
Bitto, Bingman, Wesenberg, McCoy, Phillips: Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. in Proceedings of the National Academy of Sciences of the United States of America 2007
report of 2 Egyptian sibling patients suspected of Canavan disease (CD); study revealed homozygosity for substitution T530C (Ile177Thr) in exon 4 of the ASPA gene in both sibs; substitution T530C (Ile177Thr) results in a novel missense mutation causing a CD phenotype with severe clinical characteristics
Four ASPA missense mutations associated with Canavan disease are structurally characterized.
Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein.
This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent.
a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease.
Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver.
Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis.
We report on an Italian female patient with Canavan disease due to a missense mutation of the aspartoacylase gene and a 17p13.3 chromosomal microdeletion
the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found
Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene
Gata6 (show GATA6 Antibodies) regulates differentiation, metabolism, and survival of resident peritoneal macrophages through aspartoacylase.
aspartoacylase is proposed here to support lipid synthesis and energy metabolism via the provision of substrate for both cellular processes during early postnatal development
Intracellular vacuolisation in astrocytes coincides with axonal swellings in cerebellum and brain stem of aspa(lacZ/lacZ (show GLB1 Antibodies)) mutants indicating that astroglia may act as an osmolyte buffer in the aspa-deficient CNS
Aspa defects were associated with increased levels of acetylated histone H3 (show HIST3H3 Antibodies), decreased chromatin compaction and increased GFAP (show GFAP Antibodies) protein, a marker for astrogliosis. Early in postnatal development ASPA defic affects oligodendrocyte maturation and myelination
Death of OLs, neurons, and astrocytes was identified in every region of the aspartoacylase KO brain. These findings support involvement of ASPA in CNS development and function.
ASPA gene defect in the mouse leads to spinal cord pathology; these changes may be involved in the cause of the physiological/behavioral abnormalities seen in the knockout mouse.
normal hydrolysis of N-acetylaspartic acid is affected by aspartoacylase activity seen in the type 2 diabetes model mouse
we now present immunoblot, proteomic, and biochemical evidence that the membrane-bound form of ASPA is intrinsic to purified myelin membranes.
Nur7( Q193X) is a nonsense mutation in the mouse aspartoacylase gene that causes spongy degeneration of the CNS.
This gene encodes an enzyme that catalyzes the conversion of N-acetyl_L-aspartic acid (NAA) to aspartate and acetate. NAA is abundant in the brain where hydrolysis by aspartoacylase is thought to help maintain white matter. This protein is an NAA scavenger in other tissues. Mutations in this gene cause Canavan disease. Alternatively spliced transcript variants have been found for this gene.
aspartoacylase (Canavan disease)
, aspartoacylase (aminoacylase 2, Canavan disease)
, aminoacylase 2
, aspartoacylase (aminoacylase) 2