ASPA Antibody

Code CSB-PA002223ZA01HU
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Product Details

Full Product Name Rabbit anti-Homo sapiens (Human) ASPA Polyclonal antibody
Uniprot No. P45381
Target Names ASPA
Alternative Names ACY 2 antibody; ACY-2 antibody; ACY2 antibody; ACY2_HUMAN antibody; Aminoacylase 2 antibody; Aminoacylase-2 antibody; Aminoacylase2 antibody; ASP antibody; ASPA antibody; Aspartoacylase (aminoacylase 2; Canavan disease) antibody; Aspartoacylase (Canavan disease) antibody; Aspartoacylase antibody; NUR 7 antibody; NUR7 antibody; OTTMUSP00000006437 antibody; RP23-213I10.1 antibody; Small lethargic antibody
Raised in Rabbit
Species Reactivity Homo sapiens
Immunogen Recombinant Human Aspartoacylase (ASPA) (1-313AA)
Immunogen Species Homo sapiens (Human)
Conjugate Non-conjugated
Clonality Polyclonal
Isotype IgG
Purification Method Protein A/G
Concentration It differs from different batches. Please contact us to confirm it.
Buffer Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form Liquid
Tested Applications ELISA, WB (ensure identification of antigen)
Protocols ELISA Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time Made-to-order

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Target Data

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.
Gene References into Functions
  1. 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 PMID: 24036223
  2. Four ASPA missense mutations associated with Canavan disease are structurally characterized. PMID: 25003821
  3. Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein. PMID: 24632142
  4. This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent. PMID: 22878930
  5. a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease. PMID: 22468686
  6. Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver. PMID: 22750302
  7. Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis. PMID: 22219087
  8. 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 PMID: 22019069
  9. the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found PMID: 12638939
  10. Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene PMID: 16437572
  11. molecular weight of the purified enzyme is higher than predicted, suggesting the presence of post-translational modifications. Deglycosylation of aspartoacylase or mutation at glycosylation site causes decreased enzyme stability and catalytic activity PMID: 16669630
  12. a green fluorescent protein-human ASPA fusion protein larger than the permissible size for the nuclear pore complex was enzymatically active and showed mixed nuclear-cytoplasmic distribution. PMID: 16935940
  13. The finding that wild-type and Glu178Asp have the same K(m) but different k(cat) values confirms the idea that the carboxylate group contributes importantly to the enzymatic activity of aspartoacylase. PMID: 17027983
  14. the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A PMID: 17194761
  15. These results show that aspartoacylase is a member of the caboxypeptidase A family and offer novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease. PMID: 17391648
  16. New structure of human aspartoacylase complexed with a catalytic intermediate analogue, N-phosphonomethyl- l-aspartate, supports a carboxypeptidase-type mechanism for hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate. PMID: 18293939

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Involvement in disease Canavan disease (CAND)
Subcellular Location Cytoplasm, Nucleus
Protein Families AspA/AstE family, Aspartoacylase subfamily
Tissue Specificity Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver.
Database Links

HGNC: 756

OMIM: 271900

KEGG: hsa:443

STRING: 9606.ENSP00000263080

UniGene: Hs.171142

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