FDPS Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 6
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | P14324 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 48275 Da |
Antigen Region | 389-419 aa |
Gene ID | 2224 |
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Other Names | Farnesyl pyrophosphate synthase, FPP synthase, FPS, (2E, 6E)-farnesyl diphosphate synthase, Dimethylallyltranstransferase, Farnesyl diphosphate synthase, Geranyltranstransferase, FDPS, FPS, KIAA1293 |
Target/Specificity | This FDPS antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 389-419 amino acids from the center region of human FDPS. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | FDPS Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | FDPS (HGNC:3631) |
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Synonyms | FPS, KIAA1293 |
Function | 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. |
Cellular Location | Cytoplasm. |
Provided below are standard protocols that you may find useful for product applications.
Background
The isoprene biosynthetic pathway supply the cell with cholesterol, ubiquinone, and various nonsterol metabolites. The farnesylpyrophosphate synthetase enzyme catalyzes the formation of geranyl and farnesylpyrophosphate from isopentenylpyrophosphate and dimethylallyl pyrophosphate. Analysis of FDPS activity and protein in rat liver, accompanied by immunofluorescence and immunoelectron microscopy studies, demonstrated that FDPS is predominantly localized in peroxisomes.1 Liver tissue from patients with the peroxisomal deficiency diseases Zellweger syndrome and neonatal adrenoleukodystrophy exhibit diminished activities of FDPS and subsequent isoprenoid synthesis.
References
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
Nomura, N., et al., DNA Res. 1(1):27-35 (1994).
Wilkin, D.J., et al., J. Biol. Chem. 265(8):4607-4614 (1990).
Sheares, B.T., et al., Biochemistry 28(20):8129-8135 (1989).
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