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Human IDI2 / IPPI2 Protein  pdf  pdf  pdf


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Synonym

IDI2,IPPI2,IPP isomerase 2

Source

Human IDI2, His Tag (ID2-H5142) is expressed from E.coli cells. It contains AA Ser 2 - Val 227 (Accession # AAH17778).

Predicted N-terminus: Met

Molecular Characterization

Poly-his
IDI2(Ser 2 - Val 227)AAH17778

This protein carries a polyhistidine tag at the N-terminus.

The protein has a calculated MW of 27.6 kDa. The protein migrates as 28 kDa under reducing (R) condition (SDS-PAGE).

Endotoxin

Less than 1.0 EU per μg by the LAL method.

 

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in 150 mM NaCl, 50 mM Tris, pH7.5, 0.1 mM PMSF, 1 mM DTT. Normally trehalose is added as protectant before lyophilization.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Storage

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

No activity loss is observed after storage at:

  1. 4-8°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.
 

SDS-PAGE

Human IDI2, His Tag (Cat. No. ID2-H5142) SDS-PAGE gel

Human IDI2, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

 

Background

Isopentenyl-diphosphate delta-isomerase 2 (IDI2) is also known as Isopentenyl pyrophosphate isomerase 2 (IPPI2 or IPP isomerase 2),which belongs to the IPP isomerase type 1 family and contains one nudix hydrolase domain. IDI2 catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).Recently, it indicates that, in humans, IDI2 is expressed only in skeletal muscle. Expression constructs of human IDI2 in Saccharomyces cerevisiae can complement isomerase function in an idi1-deficient yeast strain. Both isozymes, IDI1 and IDI2 are localized to the peroxisome by a PTS1-dependent pathway. IDI2 is regulated independently from IDI1, by a mechanism that may involve PPARalpha.

References

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