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ASPA Matched Antibody Pair (110) (APMAB-110LY)

This antibody pair set can be used for detecting and quantifying protein level of human ASPA.
See all ASPA antibodies

Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Rabbit anti-ASPA polyclonal antibody, 100 ug
Detection Antibody
Anti-ASPA Mouse monoclonal, IgG2b antibody, 20 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
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. [provided by RefSeq, Jul 2008]
Alternative Names
Aspartoacylase; Aminoacylase 2; EC 3.5.1.15; ACY-2; ACY2; ASP; Aspartoacylase (Aminoacylase 2, Canavan Disease); Canavan Disease; Aminoacylase-2;
Entrez Gene ID
443
UniProt ID
P45381

Gersing, S. K., Wang, Y., Grønbæk-Thygesen, M., Kampmeyer, C., Clausen, L., Willemoës, M., ... & Hartmann-Petersen, R. (2021). Mapping the degradation pathway of a disease-linked aspartoacylase variant. PLoS Genetics, 17(4), e1009539.

Gersing, S. K., Wang, Y., Grønbæk-Thygesen, M., Kampmeyer, C., Clausen, L., Andréasson, C., ... & Hartmann-Petersen, R. (2020). Evolutionarily conserved chaperone-mediated proteasomal degradation of a disease-linked aspartoacylase variant. bioRxiv.

Kots, E. D., Khrenova, M. G., Nemukhin, A. V., & Varfolomeev, S. D. (2019). Aspartoacylase: a central nervous system enzyme. Structure, catalytic activity and regulation mechanisms. Russian Chemical Reviews, 88(1), 1.

Kuwamura, M., Tanimura, S., Hasegawa, Y., Hoshiai, R., Moriyama, Y., Tanaka, M., ... & Serikawa, T. (2019). Downregulation of aspartoacylase during the progression of myelin breakdown in the dmy mutant rat with mitochondrial magnesium channel MRS2 defect. Brain research, 1718, 169-175.

Bannerman, P., Guo, F., Chechneva, O., Burns, T., Zhu, X., Wang, Y., ... & Pleasure, D. (2018). Brain Nat8l knockdown suppresses spongiform leukodystrophy in an aspartoacylase-deficient canavan disease mouse model. Molecular Therapy, 26(3), 793-800.

Starling, S. (2018). Targeted aspartoacylase gene therapy reverts Canavan disease. Nature Reviews Neurology, 14(1), 4-4.

Doss, C. G. P., & Zayed, H. (2017). Comparative computational assessment of the pathogenicity of mutations in the Aspartoacylase enzyme. Metabolic brain disease, 32(6), 2105-2118.

Mendes, M. I., Smith, D. E., Pop, A., Lennertz, P., Fernandez Ojeda, M. R., Kanhai, W. A., ... & Salomons, G. S. (2017). Clinically distinct phenotypes of Canavan disease correlate with residual aspartoacylase enzyme activity. Human mutation, 38(5), 524-531.

Varfolomeev, S. D., Kots, E. D., Khrenova, M. G., Lushchekina, S. V., & Nemukhin, A. V. (2017, June). Supercomputer technologies for structural-kinetic study of mechanisms of enzyme catalysis: A quantum-chemical description of aspartoacylase catalysis. In Doklady Physical Chemistry (Vol. 474, No. 2, pp. 89-92). Pleiades Publishing.

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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