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Recombinant human GMPR protein

CAT: 0112-ATGP1410-020Size: 20 µgDry Ice: NoHazardous: No
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CAT#:0112-ATGP1410-020Size:20 µg
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24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Description
GMPR, also known as guanosine monophosphate reductase, catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Recombinant human GMPR protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.
Product Name Alternative
Guanosine monophosphate reductase, GMPR1
Expression System
E.coli
Antigen Species
Human
Tag
His-Tag
Applications
SDS-PAGE
Concentration
1 mg/mL (determined by Bradford assay)
Purity
> 90% by SDS-PAGE
Molecular Weight
39.5 kDa (365aa) confirmed by MALDI-TOF
Additionnal Information
GMPR, Guanosine monophosphate reductase, GMPR1, ATGP1410-10 µg, ATGP1410-20 µg, ATGP1410-50 µg, ATGP1410-100 µg, ATGP1410-250 µg, ATGP1410-500 µg, ATGP1410-1 mg, ATGP1410-10, ATGP1410-20, ATGP1410-50, ATGP1410-100, ATGP1410-250, ATGP1410-500, ATGP1410-1
References & Citations
Yoshida A., et al. (1990) Cell. 62:11-12; ; Kanno H., et al. (1989) Cell. 58:595-606
Storage Conditions
Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
Formulation
Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 40% glycerol, 0.15M NaCl, 1mM DTT
Scientific Category
Redox Proteins
NCBI Accession Number
AAH08281
Uniprot Accession Number
P36959
Species
Human
AA Sequence
MGSSHHHHHH SSGLVPRGSH MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM LGGMFSGHTE CAGEVIERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS