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Showing 1 to 5 of 5 found results for "43067"
1- (5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

Recombinant Ruthia magnifica subsp. Calyptogena magnifica 1- (5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

(#MBS1225230)

Gene Names:
hisA
Other Names:
1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
ATP phosphoribosyltransferase (hisG)

Recombinant Ruthia magnifica subsp. Calyptogena magnifica ATP phosphoribosyltransferase (hisG)

(#MBS1063651)

Gene Names:
hisG
Other Names:
ATP phosphoribosyltransferase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Phosphoribosyl-AMP cyclohydrolase (hisI)

Recombinant Ruthia magnifica subsp. Calyptogena magnifica Phosphoribosyl-AMP cyclohydrolase (hisI)

(#MBS1110724)

Gene Names:
hisI
Other Names:
phosphoribosyl-AMP cyclohydrolase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Phosphoribosyl-ATP pyrophosphatase (hisE)

Recombinant Ruthia magnifica subsp. Calyptogena magnifica Phosphoribosyl-ATP pyrophosphatase (hisE)

(#MBS1210259)

Gene Names:
hisE
Other Names:
phosphoribosyl-ATP pyrophosphatase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Imidazole glycerol phosphate synthase subunit HisF (hisF)

Recombinant Ruthia magnifica subsp. Calyptogena magnifica Imidazole glycerol phosphate synthase subunit HisF (hisF)

(#MBS1093234)

Gene Names:
hisF
Other Names:
imidazole glycerol phosphate synthase cyclase subunit
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.

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