Human GCDH Recombinant Protein N-6 His Tag

Human GCDH Recombinant Protein N-6 His Tag from Innovative Research has been recombinantly produced in E. coli. This is a Liquid protein buffered in Supplied as a 0.2 um filtered solution of 20mM HEPES, 150mM NaCl, pH 7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: GCDH Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli Storage Conditions: Store at -20░C, stable for 6 months after receipt.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

Additional Information:

Glutaryl-CoA Dehydrogenase Mitochondrial (GCDH) is an enzyme that acts upon glutaryl-coenzyme A, creating crotonyl-coenzyme A. It plays a role in the metabolism of lysine, hydroxylysine and tryptophan. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive Glutaryl-CoA and electron-transfer flavoprotein to (E)-but-2-enoyl-CoA, CO2 and reduced electron-transfer flavoprotein. A defect in this enzyme is associated with neurological condition glutaric acidemia type 1 and cause a progressive form of early-onset generalized dystonia.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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This material is sold for in-vitro use only for research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herein are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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