Description
IDI1 Antibody | 26-918 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse
Homology: N/A
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human IDI1.
Research Area: Other
Tested Application: E, WB
Application: IDI1 antibody can be used for detection of IDI1 by ELISA at 1:1562500. IDI1 antibody can be used for detection of IDI1 by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50, 000 - 100, 000.
Specificiy: N/A
Positive Control 1: Cat. No. 1201 - HeLa Cell Lysate
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 32 kDa
Validation: N/A
Isoform: N/A
Purification: Antibody is purified by peptide affinity chromatography method.
Clonality: Polyclonal
Clone: N/A
Isotype: N/A
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Concentration: batch dependent
Storage Condition: For short periods of storage (days) store at 4˚C. For longer periods of storage, store IDI1 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Alternate Name: IDI1, IPP1, IPPI1
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: IDI1 is a peroxisomally-localized enzyme that catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP) , which are the substrates for the successive reaction that results in the synthesis of farnesyl diphosphate and, ultimately, cholesterol. It has been shown in peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy that there is reduction in IPP isomerase activity.IDI1 encodes a peroxisomally-localized enzyme that catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP) , which are the substrates for the successive reaction that results in the synthesis of farnesyl diphosphate and, ultimately, cholesterol. It has been shown in peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy that there is reduction in IPP isomerase activity.