Recombinant Human Cytidine Deaminase (CDA) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01853P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Cytidine Deaminase (CDA) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01853P
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Product Overview

Description Recombinant Human Cytidine Deaminase (CDA) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P32320
Target Symbol CDA
Synonyms Cytidine aminohydrolase
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ
Expression Range 1-146aa
Protein Length Full Length
Mol. Weight 23.6 kDa
Research Area Epigenetics And Nuclear Signaling
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Protein Families Cytidine and deoxycytidylate deaminase family
Database References
Tissue Specificity Highly expressed in granulocytes while expression is very low in fibroblasts, chondrocytes, monocytes, and T- as well as B-cell lines.

Gene Functions References

  1. SNPs in CDA and CES2 were associated with benefit from the addition of capecitabine to chemotherapy in metastatic breast cancer patients PMID: 28827188
  2. The observed incomplete sister chromatid disjunction may be due to the accumulation of unreplicated DNA during mitosis in CDA-deficient cells, as reflected in the changes in centromeric DNA structure associated with the decrease in basal PARP-1 activity. PMID: 28463527
  3. Intracerebral microdialysis revealed that clonal NSC line to stably express cytosine deaminase (CD-NSCs) produced 5-FU locally in the brain in a 5-FC dose-dependent manner. Collectively, our results from this first-in-human study demonstrate initial safety and proof of concept regarding the ability of NSCs to target brain tumors and locally produce chemotherapy. PMID: 27979915
  4. results indicate that rs2072671 in CDA may be an important prognostic marker in NK-AML patients. PMID: 26354033
  5. tumor cell lines that are susceptible to epigenetic nucleosides overexpress cytidine deaminase (CDA); CDA converts 5hmdC and 5fdC into variants of uridine that are incorporated into DNA, resulting in accumulation of DNA damage, and ultimately, cell death PMID: 26200337
  6. RNA expression of deoxycytidine kinase (DCK), human equilibrative nucleoside transporter-1 (ENT1) and ribonucleotide reductase M1 (RRM1) were significantly higher and cytidine deaminase (CDA) was significantly lower in ex vivo Ara-C sensitive samples. PMID: 26083014
  7. stimulation of PARP-1 activity in CDA-deficient cells restores replication and, thus, chromosome segregation. Moreover, increasing intracellular dCTP levels generates under-replication-induced sister-chromatid bridges as efficiently as PARP-1 knockdown PMID: 26181065
  8. n the multivariate Cox regression analysis, we found that age at diagnosis, wild-type genotype of the CDA A79C polymorphism, and wild-type genotype of the dCK C360G polymorphism were the most significant prognostic factors for predicting the risk of death PMID: 26090398
  9. Single nucleotide polymorphisms in cytidine deaminase gene were associated with the efficacy of gemcitabine in Biliary Tract Cancer. PMID: 26418006
  10. Polymorphisms in ABCB1, CDA, ENOSF1,and TYMS could help to predict specific and overall severe adverse reactions to capecitabine. PMID: 25691056
  11. miR-484-modulated cytidine deaminase has a dual impact in promoting chemoresistance and suppressing cell proliferation in breast cancer PMID: 25643696
  12. This case report calls for further prospective studies investigating the exact role that CDA status plays in the clinical outcome of patients treated with azacytidine. PMID: 25850965
  13. The A79C CDA polymorphism did not show a significant impact on the response rate to gemcitabine in NSCLC patients, while the wild type CDA genotype was indeed correlated to a lower rate of incidence of severe anemia in patients taking gemcitabine. PMID: 24557790
  14. These results suggest that CDA 79A>C polymorphisms is a potential biomarker for toxicity of gemcitabine-based chemotherapy and a CDA testing before gemcitabine administration is preferred. PMID: 25582275
  15. These results provide suggestive evidence of a favorable effect for the XPD 312Asp/Asp and XPD 751Lys/Lys genotypes with respect to overall survival rates in platinum-treated NSCLC patients PMID: 24841663
  16. Macrophages mediate gemcitabine resistance of pancreatic adenocarcinoma by upregulating cytidine deaminase. PMID: 23995783
  17. The T70 variant has a lower catalytic efficiency toward the analyzed substrates when compared to the A70 variant, suggesting that patients carrying the 208G>A SNP may have a greater exposure to cytosine based pro drugs PMID: 24183806
  18. Carriers of the CDA*2B haplotype displayed higher CDA activity. PMID: 23651026
  19. ultrarapid metabolizer patients are nearly five-times more likely to have progressive disease than patients with normal or low CDA activities. PMID: 23837479
  20. Studied human CDA using site-directed mutagenesis: through these studies it was possible to understand the role exerted by specific amino acid residues in CDA active site and in the contacts between subunits. PMID: 23033855
  21. Variation in the DPYD, TYMS, CDA and MTHFR genes are clinically significant predictors of fluoropyrimidine toxicity. PMID: 23736036
  22. Data indicate cytidine deaminase rapid expression upon doxycycline application in mouse haematopoietic system. PMID: 22592598
  23. In conclusion, in this prospective randomized adjuvant study of patients with pancreatic cancer, the cytidine deaminase polymorphism is validated as a predictive marker of gemcitabine hematological toxicity, but not with treatment response or survival PMID: 21625252
  24. It is evident that the DCK and CDA polymorphisms might be the important markers for the AML patients' therapy outcomes in a Chinese population. PMID: 22884143
  25. Chinese patients carrying A79C variant C allele of CDA were found to be at higher risk of developing severe neutropenia after gemcitabine-based chemotherapy. PMID: 22546611
  26. CDA RNA expression as well as Ara-C IC showed wide variation in AML samples and normal controls. PMID: 22304580
  27. cytidine deaminase enzymatic activity appears to be the strongest candidate biomarker of activity and efficacy of platinum-gemcitabine-based chemotherapy in advanced non-small-cell lung cancer patients PMID: 21652582
  28. Cytidine deaminase (CDA) 435 T/T genotype was significantly associated with better response to treatment and the CDA 435 C/T genotype was associated with a significantly increased risk of nonhematological toxicity. PMID: 22052224
  29. Data show that the CDA/DCK ratio was 3 fold higher in non-responders than responders (P<.05), suggesting that this could be a mechanism of primary resistance. PMID: 21858090
  30. Aberrant activation-induced cytidine deaminase expression is correlated with persistent inflammatory condition induced by H. pylori infection and may contribute to the development of gastric cancer through an inflammatory condition and intestinalization. PMID: 21538122
  31. the deleted allele of rs3215400 in the promoter of cytidine deaminase shows an increased allele-specific expression and is significantly associated with an increased risk of capecitabine-induced hand-foot syndrome PMID: 21325291
  32. Single nucleotide polymorphisms in cytidine deaminase is associated with the pharmacological advantage of prolonged dose rate gemcitabine. PMID: 21332653
  33. Compared with their parental cells, the expressions of CDA, RRM1, PTEN and ERCC1 increase in human gemcitabine-resistant non-small cell lung cancer cell lines. PMID: 20211060
  34. These investigations reinforced the hypothesis that in human CDA the side chain of Y33 is involved in intersubunit interactions with four glutamate residues forming a double latch that connects each of the two pairs of monomers of the tetrameric CDA. PMID: 20637228
  35. The aim of this study was also to assess the distribution of genotypic variants of CDA in a central Italy population. PMID: 19941076
  36. The cytidine deaminase 208A genotype is shown to be more sensitive to cytosine arabinoside than the 208G genotype in childhood acute leukemia. PMID: 19035178
  37. Activation-induced cytidine deaminase expression suggests diffuse large B-cell lymphoma may arise from a putative interfollicular large B cell. PMID: 20196672
  38. Curcumin downregulated Helicobacter pylori induced cytidine deaminase expression in gastric epithelial cells. PMID: 19889077
  39. serum adenosine deaminase and cytidine deaminase levels were significantly higher in systemic lupus erythematosus patients PMID: 12113294
  40. This enzyme can act on deoxycytidine in single-stranded DNA, but requires the action of RNase A. PMID: 12651944
  41. The level of CDD mRNA expression varies at the different stage of acute leukemia. The expression level of CDD seems not to be a prognostic factor. PMID: 12844405
  42. Intersubunit interactions in human cytidine deaminase using wild and recombinant, amino acid-substituted enzymes PMID: 14565460
  43. Understanding the catalytic mechanism by crystallization of the E. coli homolog PMID: 14565461
  44. Presence of several GATA1 binding sites in the CDAsf promoter and the uniform detection of GATA1 mutations in DS megakaryocytic leukemia suggested the potential role of GATA1 in regulating CDA transcription. PMID: 14744791
  45. analysis of isoenzymatic forms of human cytidine deaminase PMID: 15713780
  46. Molecular model of cytidine deaminase. PMID: 16303324
  47. Gene transfer increased the resistance of CDD-transduced cord blood and peripheral blood-derived progenitor cells for 20-100 nM cytarabine and 8-10 nM gemcitabine. Protection was observed for progenitors of erythroid as well as myeloid differentiation. PMID: 16304576
  48. 6 SNPs ( -92A>G, -205C>G, -451C>T, -897C>A, -1075A>G and -1181G>A) in promoter of CDA may influence Ara-C chemosensitivity. PMID: 16446974
  49. Described the identification and characterization of HSCD, which is the product of alternative splicing of the HCD gene PMID: 17464349
  50. After gene trasfer of CDA, this enzyme plus 5-fluorocytosine with TRAIL may be useful for the therapy of tumors resistant to TRAIL. PMID: 17479107

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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