Human Recombinant ADSL protein, His Tag (V2LY-0526-LY1950)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant ADSL protein, His Tag consist of Amino Acid: 1-484 and predicts a molecular mass of 57 kDa.
Molecule Mass
57 kDa
Sequence
Amino Acid: 1-484
Species
Human

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

Purity
>95% 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 PBS
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
Adenylosuccinate Lyase
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.

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