Purity ~ 85% (SDS-PAGE). Purified by using conventional chromatography techniques. GLRX5 is a small redox enzyme of approximately one hundred amino-acid residues which uses glutathione as a cofactor. This protein is oxidized by substrates, and reduced non-enzymatically by glutathione. It is involved in the biogenesis of iron-sulfur clusters, which are required for normal iron homeostasis. Recombinant human GLRX5 protein, fused to His-tag at N-terminus, was expressed in E. coli. Source: Recombinant corresponding to aa1-157 of human GLRX5 6x His tagged expressed in E. coli. AA Sequence: MGSSHHHHHH SSGLVPRGSH MSGSLGRAAA ALLRWGRGAG GGGLWGPGVR AAGSGAGGGG SAEQLDALVK KDKVVVFLKG TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK Enzyme Activity: Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein. Applications: Suitable for use in Western Blot.
Size
100ug
Concentration
n/a
Applications
WB
Other Names
Glutaredoxin-5, Recombinant, Human (Glutaredoxin 5, GLRX5, GRX5, C14orf87, FLB4739, Glutaredoxin-related Protein 5 Mitochondrial, Monothiol Glutaredoxin-5, PR01238, PRO1238, MGC14129)