Human Recombinant FDPS protein, His Tag (V2LY-0526-LY4044)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant FDPS protein, His Tag consist of Amino Acid: 1-353 and predicts a molecular mass of 42.4 kDa.
Molecule Mass
42.4 kDa
Sequence
Amino Acid: 1-353
Species
Human

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

Purity
>85% 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
farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)
Research Area
Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Biological Process
Cholesterol biosynthetic process Source: ProtInc
Farnesyl diphosphate biosynthetic process Source: GO_Central
Geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
Cellular Location
Cytoplasm
Involvement in disease
Porokeratosis 9, multiple types (POROK9):
A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported.

Oike, A., Iwata, S., Hirayama, A., Ono, Y., Nagasato, Y., Kawabata, Y., ... & Shigemura, N. (2022). Bisphosphonate affects the behavioral responses to HCl by disrupting farnesyl diphosphate synthase in mouse taste bud and tongue epithelial cells. Scientific Reports, 12(1), 1-15.

Jin, T., Lu, J., Lv, Q., Gong, Y., Feng, Z., Ying, H., ... & Jiang, D. (2022). Farnesyl diphosphate synthase regulated endothelial proliferation and autophagy during rat pulmonary arterial hypertension induced by monocrotaline. Molecular Medicine, 28(1), 1-16.

Tang, H. V., Berryman, D. L., Mendoza, J., Yactayo‐Chang, J. P., Li, Q. B., Christensen, S. A., ... & Block, A. K. (2022). Dedicated farnesyl diphosphate synthases circumvent isoprenoid‐derived growth‐defense tradeoffs in Zea mays. The Plant Journal, 112(1), 207-220.

Lin, P., Yan, Z. F., & Li, C. T. (2020). Effects of Exogenous Elicitors on Triterpenoids Accumulation and Expression of Farnesyl Diphosphate Synthase Gene in Inonotus obliquus. Biotechnology and Bioprocess Engineering, 25(4), 580-588.

Wang, X., Sun, T., Sun, J., Wang, S., Ma, Y., Liu, Z., ... & Zou, L. (2020). Molecular cloning, characterisation, and heterologous expression of farnesyl diphosphate synthase from Sanghuangporus baumii. Molecular Biotechnology, 62(2), 132-141.

Fei, Y., Li, N., Zhang, D. H., & Xu, J. W. (2019). Increased production of ganoderic acids by overexpression of homologous farnesyl diphosphate synthase and kinetic modeling of ganoderic acid production in Ganoderma lucidum. Microbial cell factories, 18(1), 1-9.

Wang, Z., Guo, H., Zhang, Y., Lin, L., Cui, M., Long, Y., & Xing, Z. (2019). DNA methylation of farnesyl pyrophosphate synthase, squalene synthase, and squalene epoxidase gene promoters and effect on the saponin content of Eleutherococcus Senticosus. Forests, 10(12), 1053.

Kim, H. Y., Kim, D. K., Bae, S. H., Gwak, H., Jeon, J. H., Kim, J. K., ... & Jang, H. (2018). Farnesyl diphosphate synthase is important for the maintenance of glioblastoma stemness. Experimental & molecular medicine, 50(10), 1-12.

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

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