Human Recombinant ASL protein, GST Tag (V2LY-0526-LY2167)

Name: Human Recombinant ASL protein, GST Tag
SKU: V2LY-0526-LY2167
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

Baculovirus-Insect Cells

Protein Species

Human

Tag

GST Tag

Protein Construction

This product is Human Recombinant ASL protein, GST Tag consist of Amino Acid: 1-464 and predicts a molecular mass of 79.5 kDa.

Molecule Mass

79.5 kDa

Sequence

Amino Acid: 1-464

Species

Human

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

Purity

>90% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile Tris, Glycerol

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

argininosuccinate lyase

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Alternative Versions

Rat Asl ELISA Kit (CAT#: V2LY-0626-LY1543)

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Isotype control

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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