Anamorsin homolog 1 (H0403D02.15, OsI_17896), Recombinant Protein
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Anamorsin homolog 1 (H0403D02.15, OsI_17896), Recombinant Protein

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Cat: RP14098
Size: 0.02 mg (E-Coli)/ 0.1 mg (E-Coli)/ 0.02 mg (Yeast)/ 0.1 mg (Yeast)/ 0.02 mg (Baculovirus)/ 0.02 mg (Mammalian-Cell)/ 0.1 mg (Baculovirus)/ 1 mg (E-Coli)/ 1 mg (Yeast)/ 0.1 mg (Mammalian-Cell)/ 1 mg (Baculovirus)/ 0.5 mg (Mammalian-Cell)
Species: Oryza sativa subsp. indica (Rice)
Datasheet:

Product Info

Full Product Name
Recombinant Oryza sativa subsp. indica Anamorsin homolog 1 (H0403D02.15, OsI_17896)
Product Gene Name
H0403D02.15 recombinant protein
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Sequence
MAATAAAALA VTDELALPLR AVGDLAAAAG VSREEVVVIT QCASLGGKLP FADASVGSVL AVIKKVENLG NQFITEISRV LKAGGMVLVQ SSPSDQDPNN SIERKLLLGG FVDVQASAAS SQDNEHSVNI KAKKASWSMG SSFPLKKATK GLPKIQIDDD SELIDEDSLL TEDDLKKPEL PVVGDCEVGA TRKACKNCTC GRAEAEEKVE KLNLTSEQIN NPQSACGNCG LGDAFRCGTC PYRGLPAFKP GEKIALPGNF LAADM
Sequence Positions
1-265, Full length protein
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
27,661 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.

NCBI/Uniprot Data

NCBI Accession #
A2XYW4.1
NCBI GI #
292630655
NCBI Official Full Name
Anamorsin homolog 1
UniProt Gene Name
H0403D02.15
UniProt Protein Name
Anamorsin homolog 1
UniProt Synonym Protein Names
Fe-S cluster assembly protein DRE2 homolog 1
UniProt Primary Accession #
A2XYW4
UniProt Secondary Accession #
Q259R9
UniProt Comments
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.

For research use only, not for clinical use.