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SRP6372

Sigma-Aldrich

Cytidine deaminase human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Synonym(s):

CDA, CDD, Cytidine aminohydrolase, Cytosine nucleoside deaminase

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥90% (SDS-PAGE)

form

liquid

mol wt

18.3 kDa (166 aa, 1-146 aa + His Tag.)

packaging

pkg of 100 μg

concentration

0.5 mg/mL

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... CDA(978)

General description

Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2′-deoxycytidine for UMP synthesis. This protein is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as arabinofuranosyl cytidine (Ara-C) and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function.

Biochem/physiol Actions

Cytidine deaminase (CDA) is mainly expressed in granulocytes and can form homotetramers. Recombinant human CDA protein, fused to His-tag at N-terminus, was expressed in Escherichia coli and purified by using conventional chromatography.

Physical form

0.5 mg/mL in 20 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl, 1 mM DTT, 2 mM EDTA and 40% glycerol.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Jia-Ling Ruan et al.
Ultrasound in medicine & biology, 47(6), 1596-1615 (2021-03-13)
In this study we compared three different microbubble-based approaches to the delivery of a widely used chemotherapy drug, gemcitabine: (i) co-administration of gemcitabine and microbubbles (Gem+MB); (ii) conjugates of microbubbles and gemcitabine-loaded liposomes (GemlipoMB); and (iii) microbubbles with gemcitabine directly
Twana Alkasalias et al.
Cell death discovery, 8(1), 464-464 (2022-11-25)
Highly specific and potent inhibitors of dihydroorotate dehydrogenase (DHODH), an essential enzyme of the de novo pyrimidine ribonucleotide synthesis pathway, are in clinical trials for autoimmune diseases, viral infections and cancer. However, because DHODH inhibitors (DHODHi) are immunosuppressants they may

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