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  |  

Mouse Anti-ASPA Recombinant Antibody (3G7) (CBMAB-A3802-YC)

Provided herein is a Mouse monoclonal antibody against Human Aspartoacylase. The antibody can be used for immunoassay techniques, such as IHC-P, WB.
See all ASPA antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
3G7
Antibody Isotype
IgG2b
Application
WB

Basic Information

Immunogen
Human recombinant protein fragment corresponding to amino acids 77-313 of human ASPA (NP_000040) produced in E.coli.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:2,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 77-313

Target

Full Name
Aspartoacylase
Introduction
ASPA is 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
Entrez Gene ID
443
UniProt ID
P45381
Alternative Names
Aspartoacylase; Aminoacylase 2; EC 3.5.1.15; ACY-2; ACY2; ASP; Aspartoacylase (Aminoacylase 2, Canavan Disease); Canavan Disease; Aminoacylase-2;
Function
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids.
Biological Process
Aspartate catabolic process Source: ProtInc
Aspartate family amino acid metabolic process Source: Reactome
Central nervous system myelination Source: Ensembl
Positive regulation of oligodendrocyte differentiation Source: Ensembl
Cellular Location
Cytoplasm; Nucleus
Involvement in disease
Canavan disease (CAND): A rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demyelination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average.

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.

Custom Antibody Labeling

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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