Recombinant Human Glutamate Dehydrogenase His Protein Summary
Description |
A denatured recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 54-558 of Human Glutamate Dehydrogenase Source: E.coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
GLUD1 |
Purity |
>80%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Application Notes |
Denatured protein is most likely not the best option for functional studies. It is better suited for Western Blot (WB) or imaging assays. |
Theoretical MW |
58.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
20 mM Tris-HCl buffer (pH 8.0), 0.4M UREA, 10% glycerol |
Preservative |
No Preservative |
Concentration |
1 mg/ml |
Purity |
>80%, by SDS-PAGE |
Alternate Names for Recombinant Human Glutamate Dehydrogenase His Protein
Background
One enzyme central to the metabolism of glutamate is glutamate dehydrogenase (GDH1; EC 1.4.1.3), that catalyzes the reversible deamination of L-glutamate to 2-oxoglutarate using NAD+ or NADP+. Mammalian GDH is composed of six identical subunits, and the regulation of GDH is very complex. It has been a major goal to identify the substrate and regulatory binding sites of GDH. It is only in recent years that the three-dimensional structure of GDH from microorganisms is available. Very recently, crystallization of bovine liver GDH was reported for the first time from the mammalian sources. However, remarkably little is known about the detailed structure of mammalian GDH, especially the brain enzymes.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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