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Showing 1 to 5 of 5 found results for "31315"
1- (5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)

Recombinant Novosphingobium aromaticivorans 1- (5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)

(#MBS1402143)

Gene Names:
hisA
Other Names:
MULTISPECIES: 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 Novosphingobium aromaticivorans ATP phosphoribosyltransferase (hisG)

(#MBS1437731)

Gene Names:
hisG
Other Names:
MULTISPECIES: 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.
Histidinol-phosphate aminotransferase (hisC)

Recombinant Novosphingobium aromaticivorans Histidinol-phosphate aminotransferase (hisC)

(#MBS1331607)

Gene Names:
hisC
Other Names:
MULTISPECIES: histidinol-phosphate aminotransferase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Imidazoleglycerol-phosphate dehydratase (hisB)

Recombinant Novosphingobium aromaticivorans Imidazoleglycerol-phosphate dehydratase (hisB)

(#MBS1353406)

Gene Names:
hisB
Other Names:
MULTISPECIES: imidazoleglycerol-phosphate dehydratase
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 Novosphingobium aromaticivorans Phosphoribosyl-ATP pyrophosphatase (hisE)

(#MBS1367526)

Gene Names:
hisE
Other Names:
MULTISPECIES: 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.

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