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AIPL1 Matched Antibody Pair (043) (APMAB-043LY)


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Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Rabbit anti-AIPL1 polyclonal antibody, 100 ug
Detection Antibody
Anti-AIPL1 Mouse monoclonal, IgG2a antibody, 20 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
Leber congenital amaurosis (LCA) is the most severe inherited retinopathy with the earliest age of onset and accounts for at least 5% of all inherited retinal diseases. Affected individuals are diagnosed at birth or in the first few months of life with nystagmus, severely impaired vision or blindness and an abnormal or flat electroretinogram. The photoreceptor/pineal-expressed gene, AIPL1, encoding aryl-hydrocarbon interacting protein-like 1, is located within the LCA4 candidate region. The encoded protein contains three tetratricopeptide motifs, consistent with chaperone or nuclear transport activity. Mutations in this gene may cause approximately 20% of recessive LCA. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Alternative Names
Aryl Hydrocarbon Receptor Interacting Protein Like 1; AIPL2; Aryl Hydrocarbon Receptor-Interacting Protein-Like 1; Aryl Hydrocarbon Receptor Interacting Protein-Like 1; Aryl-Hydrocarbon-Interacting Protein-Like 1; LCA4;
Entrez Gene ID
23746
UniProt ID
Q9NZN9
More Infomation

Lukovic, D., Castro, A. A., Kaya, K. D., Munezero, D., Gieser, L., Davó-Martínez, C., ... & Erceg, S. (2020). Retinal Organoids derived from hiPSCs of an AIPL1-LCA Patient Maintain Cytoarchitecture despite Reduced levels of Mutant AIPL1. Scientific reports, 10(1), 1-13.

Yadav, R. P., Boyd, K., Yu, L., & Artemyev, N. O. (2019). Interaction of the TPR-domain of aryl hydrocarbon receptor-interacting protein-like 1 with the regulatory P [gamma] subunit of phosphodiesterase 6. J. Biol. Chem., 294(43); 10, 2019).

Yadav, R. P., Boyd, K., Yu, L., & Artemyev, N. O. (2019). Interaction of the tetratricopeptide repeat domain of aryl hydrocarbon receptor–interacting protein–like 1 with the regulatory Pγ subunit of phosphodiesterase 6. Journal of Biological Chemistry, 294(43), 15795-15807.

Yu, L., Yadav, R. P., & Artemyev, N. O. (2019). NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1). Biomolecular NMR assignments, 13(1), 79-83.

Sacristan-Reviriego, A., & van der Spuy, J. (2018). The leber congenital amaurosis-linked protein AIPL1 and its critical role in photoreceptors. Retinal Degenerative Diseases, 381-386.

Lukovic, D., Castro, A. A., León, M., del Buey Furió, V., Cortón, M., Ayuso, C., & Erceg, S. (2018). Generation of a human iPSC line from a patient with Leber congenital amaurosis caused by mutation in AIPL1. Stem cell research, 33, 151-155.

Yu, L., Yadav, R. P., & Artemyev, N. O. (2017). NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand. Biomolecular NMR assignments, 11(1), 111-115.

Yadav, R. P., & Artemyev, N. O. (2017). AIPL1: A specialized chaperone for the phototransduction effector. Cellular signalling, 40, 183-189.

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For research use only. Not intended for any clinical use.

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