STEAP1 Protein, Rat (Cell-Free, His)

The STEAP1 protein is classified as a member of the metal reductase family and cannot function as a functional metal reductase, mainly due to the lack of binding sites for the electron-donating substrate NADPH. This unique feature distinguishes STEAP1 from typical metal reductases, which are characterized by their ability to catalyze the reduction of metal ions using NADPH as an electron donor. STEAP1 Protein, Rat (Cell-Free, His) is the recombinant rat-derived STEAP1 protein, expressed by E. coli Cell-free , with C-10*His labeled tag.

STEAP1 (Six-Transmembrane Epithelial Antigen of the Prostate 1) protein, as indicated by available information, does not operate as a metalloreductase primarily because it lacks binding sites for the electron-donating substrate NADPH. Metalloreductases play a crucial role in cellular processes by reducing metal ions, but the absence of NADPH binding sites in STEAP1 suggests a distinct functional profile. This observation highlights the importance of understanding the structural and biochemical features of STEAP1 in elucidating its role within cellular pathways. Further research is necessary to uncover the specific functions and implications associated with STEAP1, both in normal cellular processes and potential connections to diseases or physiological conditions, as its distinctive characteristics may contribute to its unique role within the cellular environment. (

Rat

E. coli Cell-free

C-10*His

D3ZEK7 (M1-L339)

297738

Full Length

MEISKNITNPEELWKMKPKGNLEDDSYSTKDTGETSMLKRPVLSPLPHTVHVDAFDCPTELQHTQELFPNWQLPIKVAAVLSSLTFLYTLLREIIYPLVASREQYFYKIPILVVNKVLPMVSITLLALVYLPGEIAAVVQLRNGTKYKKFPPWLDRWMLARKQFGLLSFFFAVLHAIYSLSYPMRRSYRYKLLNWAYKQVQQSKEDAWVEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWREFHYIQSKLGIVSLLLGTVHASIFAWNKWVDISQFVWYMPPTFMIAVFLPTVVLICKIVLCLPCLRKKILKIRCGWEDVRKVNRTEMACRL

40.7 kDa

≥ 90%, as determined by reducing SDS-PAGE.