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Mouse Anti-GPI (AA 1-558) Recombinant Antibody (AT22G2) (CBMAB-H1317-FY)

This product is mouse antibody that recognizes GPI. The antibody AT22G2 can be used for immunoassay techniques such as: WB, FC, ELISA, IF.
See all GPI antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
AT22G2
Antibody Isotype
IgG2a, κ
Application
WB, FC, ELISA, IF

Basic Information

Immunogen
Recombinant human GPI purified from E. coli
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-558

Target

Full Name
Glucose-6-Phosphate Isomerase
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.
Entrez Gene ID
2821
UniProt ID
P06744
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
Function
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808).

Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381).

Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:11004567).

It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745, PubMed:11004567).
Biological Process
Carbohydrate metabolic process Source: ProtInc
Erythrocyte homeostasis Source: Ensembl
Gluconeogenesis Source: GO_Central
Glucose 6-phosphate metabolic process Source: UniProtKB
Glucose homeostasis Source: Ensembl
Glycolytic process Source: GO_Central
Hemostasis Source: ProtInc
Humoral immune response Source: ProtInc
In utero embryonic development Source: Ensembl
Learning or memory Source: Ensembl
Mesoderm formation Source: Ensembl
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
Negative regulation of neuron apoptotic process Source: Ensembl
Positive regulation of endothelial cell migration Source: UniProtKB
Positive regulation of immunoglobulin production Source: CAFA
Response to cadmium ion Source: Ensembl
Response to estradiol Source: Ensembl
Response to immobilization stress Source: Ensembl
Response to morphine Source: Ensembl
Response to muscle stretch Source: Ensembl
Response to progesterone Source: Ensembl
Response to testosterone Source: Ensembl
Cellular Location
Secreted; Cytoplasm
Involvement in disease
Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID):
A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency.
PTM
Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway.
ISGylated.

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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