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Mouse Anti-ASL Recombinant Antibody (14C7) (CBMAB-A3784-YC)

Provided herein is a Mouse monoclonal antibody against Human Argininosuccinate Lyase. The antibody can be used for immunoassay techniques, such as WB.
See all ASL antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
14C7
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Full length human recombinant protein of human ASL (NP_001020114) produced in HEK293T cell
Specificity
Human
Antibody Isotype
IgG1
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.

Target

Full Name
argininosuccinate lyase
Introduction
ASL is a member of the lyase 1 family. The encoded protein forms a cytosolic homotetramer and primarily catalyzes the reversible hydrolytic cleavage of argininosuccinate into arginine and fumarate, an essential step in the liver in detoxifying ammonia via
Entrez Gene ID
435
UniProt ID
P04424
Alternative Names
Argininosuccinate Lyase; Arginosuccinase; EC 4.3.2.1; ASAL; Argininosuccinase;
Biological Process
Arginine biosynthetic process via ornithine Source: GO_Central
Urea cycle Source: Reactome
Cellular Location
Cytosol; Extracellular exosome; Cytoplasm
Involvement in disease
Argininosuccinic aciduria (ARGINSA): An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.
PTM
Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity.

Burrage, L. C., Madan, S., Li, X., Ali, S., Mohammad, M., Stroup, B. M., ... & Urea Cycle Disorders Consortium. (2020). Chronic liver disease and impaired hepatic glycogen metabolism in argininosuccinate lyase deficiency. JCI insight, 5(4).

Ali, E. Z., Yakob, Y., & Ngu, L. H. (2019). Identification of mutations in Malaysian patients with argininosuccinate lyase (ASL) deficiency. Molecular genetics and metabolism reports, 21, 100525.

Zhao, M., Hou, L., Teng, H., Li, J., Wang, J., Zhang, K., & Yang, L. (2019). Whole-Exome Sequencing Identified a Novel Compound Heterozygous Genotype in ASL in a Chinese Han Patient with Argininosuccinate Lyase Deficiency. BioMed research international, 2019.

Wang, Y., Sun, Y., Liu, M., Zhang, X., & Jiang, T. (2019). Functional characterization of argininosuccinate lyase gene variants by mini-gene splicing assay. Frontiers in genetics, 10, 436.

Kho, J., Tian, X., Wong, W. T., Bertin, T., Jiang, M. M., Chen, S., ... & Lee, B. H. (2018). Argininosuccinate lyase deficiency causes an endothelial-dependent form of hypertension. The American Journal of Human Genetics, 103(2), 276-287.

Kim, D., Ko, J. M., Kim, Y. M., Seo, G. H., Kim, G. H., Lee, B. H., & Yoo, H. W. (2018). Low prevalence of argininosuccinate lyase deficiency among inherited urea cycle disorders in Korea. Journal of human genetics, 63(8), 911-917.

Hung, Y. H., Huang, H. L., Chen, W. C., Yen, M. C., Cho, C. Y., Weng, T. Y., ... & Lai, M. D. (2017). Argininosuccinate lyase interacts with cyclin A2 in cytoplasm and modulates growth of liver tumor cells. Oncology reports, 37(2), 969-978.

Huang, H. L., Chen, W. C., Hsu, H. P., Cho, C. Y., Hung, Y. H., Wang, C. Y., & Lai, M. D. (2017). Silencing of argininosuccinate lyase inhibits colorectal cancer formation. Oncology reports, 37(1), 163-170.

Rostami, P., Häberle, J., Setoudeh, A., Zschocke, J., & Sayarifard, F. (2017). Two novel mutations in the argininosuccinate lyase gene in Iranian patients and literature review. Iranian Journal of Pediatrics, 27(3).

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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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