Recombinant Human DCK Protein (N-6His-T7)

Name: Recombinant Human DCK Protein (N-6His-T7)
Brand: Beta LifeScience
SKU: BL-2055NP
Availability: InStock

BL-2055NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Deoxycytidine Kinase is produced by our E.coli expression system and the target gene encoding Met1-Leu260 is expressed with a 6His, T7 tag at the N-terminus.
Accession	P27707
Synonym	Deoxycytidine Kinase; dCK; DCK
Gene Background	Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localized to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.
Molecular Mass	34 KDa
Apmol Mass	30 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of PBS, 50% Glycerol, 1mM TCEP, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine. Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.
Subcellular Location	Nucleus.
Protein Families	DCK/DGK family
Database References	HGNC: 2704 OMIM: 125450 KEGG: hsa:1633 STRING: 9606.ENSP00000286648 UniGene: Hs.709

Gene Functions References

study suggests that DCK knockdown facilitates apoptosis while inhibiting proliferation and tumorigenicity in vivo of cervical cancer HeLa cells. PMID: 28820179
Phosphorylated and activated DCK can inhibit radiation-induced cell death including apoptosis and mitotic catastrophe, and promote radiation-induced autophagy through PI3K/Akt/mTOR pathway. PMID: 27879648
Low deoxycytidine kinase expression is associated with periampullary adenocarcinoma. PMID: 26362587
expression and A9846G AA genotype significantly associated with reduced mortality in pancreatic ductal adenocarcinoma PMID: 26962792
recently described a human deoxycytidine kinase mutant (G12) that sensitizes cancer cell lines to treatment with gemcitabine. Here, starting from the G12 variant, we identified a mutant that triggers even greater sensitisation to gemcitabine than G12. PMID: 26485161
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
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
results strongly suggest that (1) the E197K alteration in DCK causes inactivation of DCK, and that (2) loss of the normal E197 allele is the crucial mechanism in acquisition of gemcitabine resistance in the RMKN28 tumor cell line PMID: 26196746
DCK rs12648166 and DCK rs4694362 SNPs were associated with hematologic toxicity (OR = 2.63, CI 95% = 1.37-5.04, P = 0.0036 and OR = 2.53, CI 95% = 1.34-4.80, P = 0.0044, respectively). PMID: 25557962
These findings indicate that the decitabine metabolic pathway affects its therapeutic effects, lower hENT1 expression may induce primary resistance and down-regulated DCK expression may be related to secondary resistance. PMID: 25533931
induction after hypoxia plays a role in the progression of pulmonary fibrosis by contributing to alveolar epithelial cell proliferation PMID: 25358054
DCK expression levels are prognostic and had predictive value for sensitivity to 5-FU in pancreatic cancer. PMID: 24618665
DCK could regulate the migration and invasion of fibroblast-like synoviocytes through AKT pathway in rheumatoid arthritis patients. PMID: 24294360
PP2A constitutively dephosphorylates dCK in cells and negatively regulates its activity. PMID: 24462681
Report genetic variation in deoxycytidine kinase and subsequent gemcitabine metabolism. PMID: 23230131
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
Hematologic toxicity such as neutropenia, thrombocytopenia, and anemia were not associated with three tagged single-nucleotide polymorphisms of deoxycytidine kinase or haplotypes. Genetic variations did not affect survival of the patients. PMID: 23035362
High levels of dCK in pancreatic ductal adenocarcinoma predict longer survival times in patients treated with adjuvant gemcitabine. PMID: 22705007
These results indicate that the inactivation of DCK is one of the crucial mechanisms in acquisition of gemcitabine resistance. PMID: 22490663
Although dFdU increased the net intracellular radioactivity of [5-(3)H]dFdC at 24 h in control cells, this increase was abolished in the absence of dCK activity. PMID: 21832002
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
dCK expression level in fludarabine-sensitive patients was much higher than in Flud-resistant patients. PMID: 20137114
High deoxycytidine kinase is associated with response to pemetrexed-gemcitabine combination in patients with advanced non-small cell lung cancer. PMID: 21336182
Data show that dCK must make the transition between the open and closed states during the catalytic cycle. PMID: 21351740
Overexpressed dCK and knocked down p8 is associated with enhancement of gemcitabine sensitivity in pancreatic cancer. PMID: 21225236
Data indicate that variant C28624T showed a lower risk of lymphopenia (P=0.04), but a higher risk of neutropenia. PMID: 21030078
We show that ABCG2 influence on clofarabine cytotoxicity was markedly influenced by dCK activity PMID: 21245102
Data show that dCK-360G allele was found to increase the risk of mucositis after exposure to low-dose cytarabine in childhood ALL therapy. PMID: 20890066
Site-directed mutagenesis demonstrated that only Ser-74 phosphorylation was involved in dCK activation by casein kinase 1 delta, strengthening the key role of this residue in the control of dCK activity. PMID: 20637175
Data show that phosphorylation of the three other sites, located in the N-terminal extremity of the protein, does not significantly modify dCK activity, but phosphorylation of Thr-3 could promote dCK stability. PMID: 20544527
Data show that methylation was detected in one of the SP1 binding sites of the dCK promoter, in most tested cancer cell lines and in patient samples from brain tumors and leukemia. Methylation might therefore regulate transcription of dCK. PMID: 20544528
it is residue Asp133 of dCK that is most responsible for discriminating against the thymine base PMID: 20614893
Sensitivity of two pancreatic cancer cell lines transduced with deoxycytidine kinase to gemcitabine elevated dramatically in comparison with control cells. PMID: 20043109
alternatively spliced dCK forms found in acute myeloid leukemia cells play an important role in cytarabine resistance PMID: 11830489
Molecular basis of 2',3'-dideoxycytidine-induced drug resistance in human cells. PMID: 11952160
Data show that inorganic tripolyphosphate (PPP(i)) is a good donor for human ceoxycytidine kinase and deoxyguanosine kinase. PMID: 12535661
human deoxycytidine kinase promoter activity is regulated by USF and Sp1 PMID: 14514691
dCK can act as a phosphorylase, similar to the nucleoside phosphorylase family of enzymes PMID: 15561147
analysis of antitumor drug binding to deoxycytidine kinase PMID: 15571255
dCK expression varies between individual samples and between different types of malignancies and may play a role in resistance to ara-C in particular tumor types PMID: 15571257
deoxycytidine kinase activity is stimulated by 2-chlorodeoxyadenosine and aphidicolin in the cellular context PMID: 15571258
deoxycytidine kinase activity is regulated by reversible phosphorylation PMID: 15571259
an increased expression of mRNA, specific for thymidine kinase 1, dCK and thymidine phosphorylase, may be involved in carcinogenic processes in the human thyroid PMID: 15978330
dCK activity can be controlled by phosphorylation in intact cells, and Ser-74 is required for activity PMID: 16361699
Crystal structures of a deoxycytidine kinase variant lacking a flexible insert (residues 65-79) reveal major changes in the donor base binding loop (residues 240-247) between UDP-bound and ADP-bound forms, involving significant main-chain rearrangement. PMID: 16401075
an increase in activity of dCK, TK1 and 2 might be involved in an adaptive response of cultured human squamous lung carcinoma cells to radiation by facilitation of DNA repair PMID: 16969512
deoxycytidine kinase has a role in lymphoma cell sensitivity to cladribine PMID: 17065053
analysis of phosphorylation sites on human deoxycytidine kinase PMID: 17065079
analysis of deoxycytidine kinase reversible phosphorylation in normal human lymphocytes PMID: 17065080
deoxycytidine kinase activity is enhanced after pulsed low dose rate and single dose gamma irradiation PMID: 17065085

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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.

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