NT5C1A Protein, Human (P.pastoris, His)

The NT5C1A protein plays a key role in cellular nucleotide metabolism, catalyzing the hydrolysis of ribonucleotide and deoxyribonucleotide monophosphates and releasing inorganic phosphates and the corresponding nucleosides. Although AMP was identified as the primary substrate of NT5C1A, this versatile enzyme is also capable of hydrolyzing other nucleotides, such as dCMP and IMP. NT5C1A Protein, Human (P.pastoris, His) is the recombinant human-derived NT5C1A protein, expressed by P. pastoris , with N-His labeled tag. The total length of NT5C1A Protein, Human (P.pastoris, His) is 368 a.a., with molecular weight of ~43.0 kDa.

NT5C1A, also known as cytosolic purine 5'-nucleotidase, is an enzyme that catalyzes the hydrolysis of ribonucleotide and deoxyribonucleotide monophosphates. In this process, inorganic phosphate and the corresponding nucleoside are released. While adenosine monophosphate (AMP) is the primary substrate, NT5C1A can also hydrolyze other nucleotides, including deoxycytidine monophosphate (dCMP) and inosine monophosphate (IMP). This enzymatic activity is crucial for the regulation of nucleotide pools, contributing to the maintenance of cellular homeostasis by controlling the levels of nucleoside monophosphates. It has to highlight NT5C1A's versatility in hydrolyzing different substrates, emphasizing its role in nucleotide metabolism.

Human

P. pastoris

N-His

Q9BXI3 (1M-368Q)

84618  [NCBI]

MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRALFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDVFDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVREAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAHENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWGLETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAPAKQAPSAQ

Approximately 43.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.