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Mouse Anti-ADSL Recombinant Antibody (V2-180027) (CBMAB-A1429-YC)

Provided herein is a Mouse monoclonal antibody against Human Adenylosuccinate Lyase. The antibody can be used for immunoassay techniques, such as WB, FC, ELISA, ICC, IF.
See all ADSL antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-180027
Antibody Isotype
IgG1, κ
Application
WB, IHC-F, ELISA, ICC, IF

Basic Information

Immunogen
Recombinant human ADSL(1-484aa) purified from E. coli
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IF(ICC)1:100
FC1:10-1:1,000

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

Buffer
PBS pH7.4, 10% 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.

Target

Full Name
Adenylosuccinate Lyase
Introduction
ADSL belongs to the lyase 1 family. It is an essential enzyme involved in purine metabolism, and catalyzes two non-sequential reactions in the de novo purine biosynthetic pathway: the conversion of succinylaminoimidazole carboxamide ribotide (SAICAR) to a
Entrez Gene ID
158
UniProt ID
P30566
Alternative Names
Adenylosuccinate Lyase; Adenylosuccinase; EC 4.3.2.2; ASASE; AMPS; ASL; EC 4.3.2;
Function
Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.
Biological Process
de novo' AMP biosynthetic process
'de novo' IMP biosynthetic process
AMP biosynthetic process
Purine nucleotide biosynthetic process
Purine ribonucleoside monophosphate biosynthetic process
Cellular Location
Cytosol; Protein-containing complex
Involvement in disease
Adenylosuccinase deficiency (ADSLD): An autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present.

Taha-Mehlitz, S., Bianco, G., Coto-Llerena, M., Kancherla, V., Bantug, G. R., Gallon, J., ... & Piscuoglio, S. (2021). Adenylosuccinate lyase is oncogenic in colorectal cancer by causing mitochondrial dysfunction and independent activation of NRF2 and mTOR-MYC-axis. Theranostics, 11(9), 4011.

Mastrogiorgio, G., Macchiaiolo, M., Buonuomo, P. S., Bellacchio, E., Bordi, M., Vecchio, D., ... & Bartuli, A. (2021). Clinical and molecular characterization of patients with adenylosuccinate lyase deficiency. Orphanet journal of rare diseases, 16(1), 1-10.

Macchiaiolo, M., Buonuomo, P. S., Mastrogiorgio, G., Bordi, M., Testa, B., Weber, G., ... & Bartuli, A. (2020). Very mild isolated intellectual disability caused by adenylosuccinate lyase deficiency: a new phenotype. Molecular genetics and metabolism reports, 23, 100592.

Andelman-Gur, M. M., Saitsu, H., Matsumoto, N., Spiegel, R., Yosovich, K., Lev, D., ... & Blumkin, L. (2020). Myoclonic tremor status as a presenting symptom of adenylosuccinate lyase deficiency. European journal of medical genetics, 63(12), 104061.

Zurlo, G., Liu, X., Takada, M., Fan, C., Simon, J. M., Ptacek, T. S., ... & Zhang, Q. (2019). Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer. Nature communications, 10(1), 1-15.

Oduselu, G. O., Ajani, O. O., Ajamma, Y. U., Brors, B., & Adebiyi, E. (2019). Homology modelling and molecular docking studies of selected substituted Benzo [d] imidazol-1-yl) methyl) benzimidamide scaffolds on Plasmodium falciparum adenylosuccinate lyase receptor. Bioinformatics and biology insights, 13, 1177932219865533.

Park, H., Ohshima, K., Nojima, S., Tahara, S., Kurashige, M., Hori, Y., ... & Morii, E. (2018). Adenylosuccinate lyase enhances aggressiveness of endometrial cancer by increasing killer cell lectin-like receptor C3 expression by fumarate. Laboratory Investigation, 98(4), 449-461.

Mao, X., Li, K., Tang, B., Luo, Y., Ding, D., Zhao, Y., ... & Guo, J. (2017). Novel mutations in ADSL for Adenylosuccinate Lyase deficiency identified by the combination of trio-WES and constantly updated guidelines. Scientific reports, 7(1), 1-7.

Macchiaiolo, M., Barresi, S., Cecconi, F., Zanni, G., Niceta, M., Bellacchio, E., ... & Bartuli, A. (2017). A mild form of adenylosuccinate lyase deficiency in absence of typical brain MRI features diagnosed by whole exome sequencing. Italian journal of pediatrics, 43(1), 1-7.

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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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