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GPI Matched Antibody Pair (496) (APMAB-496LY)

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Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Rabbit anti-GPI polyclonal antibody, 100 ug
Detection Antibody
Anti-GPI Mouse polyclonal 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
This gene encodes a member of the glucose phosphate isomerase protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In the cytoplasm, the gene product functions as a glycolytic enzyme (glucose-6-phosphate isomerase) that interconverts glucose-6-phosphate and fructose-6-phosphate. Extracellularly, the encoded protein (also referred to as neuroleukin) functions as a neurotrophic factor that promotes survival of skeletal motor neurons and sensory neurons, and as a lymphokine that induces immunoglobulin secretion. The encoded protein is also referred to as autocrine motility factor based on an additional function as a tumor-secreted cytokine and angiogenic factor. Defects in this gene are the cause of nonspherocytic hemolytic anemia and a severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2016]
Alternative Names
Glucose-6-Phosphate Isomerase; Autocrine Motility Factor; Phosphoglucose Isomerase; Phosphohexose Isomerase; Neuroleukin; EC 5.3.1.9; SA-36; PGI; AMF; NLK; PHI;
Entrez Gene ID
UniProt ID
More Infomation

Li, T., Ge, C., Krämer, A., Sareila, O., Agelii, M. L., Johansson, L., ... & Holmdahl, R. (2023). Pathogenic antibody response to glucose-6-phosphate isomerase targets a modified epitope uniquely exposed on joint cartilage. Annals of the Rheumatic Diseases, 82(6), 799-808.

Guo, Y., Wu, J., Wang, M., Wang, X., Jian, Y., Yang, C., & Guo, W. (2022). The metabolite saccharopine impairs neuronal development by inhibiting the neurotrophic function of glucose-6-phosphate isomerase. Journal of Neuroscience, 42(13), 2631-2646.

Zu, Y., Wang, H., Lin, W., & Zou, C. (2022). Hereditary nonspherocytic hemolytic anemia caused by glucose-6-phosphate isomerase (GPI) deficiency in a Chinese patient: a case report. BMC pediatrics, 22(1), 1-6.

Velmurugan, R., & Incharoensakdi, A. (2021). Overexpression of glucose-6-phosphate isomerase in Synechocystis sp. PCC 6803 with disrupted glycogen synthesis pathway improves exopolysaccharides synthesis. Algal Research, 57, 102357.

Matsumoto, I., Kurata, I., Ohyama, A., Kawaguchi, H., Ebe, H., Osada, A., ... & Sumida, T. (2020). Revisit of autoimmunity to glucose-6-phosphate isomerase in experimental and rheumatoid arthritis. Modern Rheumatology, 30(2), 232-238.

Xu, J., Zhang, X. Y., Li, R., Liu, J., Ye, H., Zhang, X. W., & Li, Z. G. (2020). Glucose-6-phosphate isomerase is associated with disease activity and declines in response to infliximab treatment in rheumatoid arthritis. Chinese Medical Journal, 133(08), 886-891.

Guo, Y., Jiang, W., Yu, W., Niu, X., Liu, F., Zhou, T., ... & Chen, D. (2019). Proteomics analysis of asthenozoospermia and identification of glucose-6-phosphate isomerase as an important enzyme for sperm motility. Journal of proteomics, 208, 103478.

Fermo, E., Vercellati, C., Marcello, A. P., Zaninoni, A., Aytac, S., Cetin, M., ... & Bianchi, P. (2019). Clinical and molecular spectrum of glucose-6-phosphate isomerase deficiency. Report of 12 new cases. Frontiers in Physiology, 10, 467.

Ma, Y. T., Xing, X. F., Dong, B., Cheng, X. J., Guo, T., Du, H., ... & Ji, J. F. (2018). Higher autocrine motility factor/glucose-6-phosphate isomerase expression is associated with tumorigenesis and poorer prognosis in gastric cancer. Cancer management and research, 10, 4969.

Mojzikova, R., Koralkova, P., Holub, D., Saxova, Z., Pospisilova, D., Prochazkova, D., ... & Divoky, V. (2018). Two novel mutations (p.(Ser160Pro) and p.(Arg472Cys)) causing glucose-6-phosphate isomerase deficiency are associated with erythroid dysplasia and inappropriately suppressed hepcidin. Blood Cells, Molecules, and Diseases, 69, 23-29.

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

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