Human Recombinant PGI protein-1 (V2LY-0526-LY6109)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Protein Construction
This product is Human Recombinant PGI protein consist of Please contact us for more information. and predicts a molecular mass of 41.28 kDa.
Molecule Mass
41.28 kDa
Sequence
Please contact us for more information.
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, NaCl, Glutathione, EDTA, DTT, PMSF, 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
Glucose-6-Phosphate Isomerase
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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