Recombinant Human Thymidine Kinase 2, Mitochondrial (TK2) Protein (His&Myc)

Name: Recombinant Human Thymidine Kinase 2, Mitochondrial (TK2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-09157P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Thymidine Kinase 2, Mitochondrial (TK2) 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	O00142
Target Symbol	TK2
Synonyms	EC 2.7.1.21; KITM_HUMAN; mitochondrial; Mt TK ; Mt-TK; Thymidine kinase 2; Thymidine kinase 2 mitochondrial ; TK2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	VQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP
Expression Range	34-265aa
Protein Length	Full Length of Mature Protein
Mol. Weight	32.5 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	Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK. Widely used as target of antiviral and chemotherapeutic agents.
Subcellular Location	Mitochondrion.
Protein Families	DCK/DGK family
Database References	HGNC: 11831 OMIM: 188250 KEGG: hsa:7084 STRING: 9606.ENSP00000414334 UniGene: Hs.512619
Associated Diseases	Mitochondrial DNA depletion syndrome 2 (MTDPS2); Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 3 (PEOB3)
Tissue Specificity	Predominantly expressed in liver, pancreas, muscle, and brain.

Gene Functions References

We confirm the pathogenicity of the rare mitochondrial m.8340G>A variant the basis of single-fibre segregation studies and its association with an expanded clinical phenotype. Our case expands the phenotypic spectrum of diseases associated with mitochondrial tRNA point mutations, highlighting the importance of considering a mitochondrial diagnosis. PMID: 28729369
Severe deficiency of thymidine kinase 2 was associated with patients with mild forms of myopathy. PMID: 25948719
Data indicate that the thymidine kinase 2 enzyme kinetics of thymidine (dT) phosphorylation exhibits negative cooperativity, but deoxycytidine (dC) phosphorylation follows hyperbolic Michaelis-Menten kinetics. PMID: 25215937
thymidine kinase 2 but not deoxyguanosine kinase is up-regulated during the stationary growth phase of cultured cells PMID: 24940680
Clinically, hypotonia and proximal muscle weakness are the major phenotypes present in all subjects. In summary, our study expands the molecular and clinical spectrum associated with TK2 deficiency. PMID: 23932787
Thymidine kinase-2 mutations causing mtDNA deletions are linked to a case of late-onset respiratory failure. PMID: 24198295
Results strongly suggest that oxidative damage-induced S-glutathionylation and degradation of TK2 have significant impact on mitochondrial DNA precursor synthesis. PMID: 22661713
R225W and T230A mutation of TK2 leads to a significant reduction activity in autosomal recessive progressive external ophthalmoplegia patients. PMID: 21937588
TK2-deficient cells showed severe mtDNA depletion. PMID: 21382338
TK2 mutations have been identified in four patients from two families with myopathic mitochondrial DNA depletion and spinal muscular atrophy. PMID: 12391347
human thymidine kinase 2 has a role in mitochondrial DNA depletion myopathy as demonstrated by kinetic analysis PMID: 12493767
TK2 deficiency associated with myopathy and apparent reversion of mtDNA depletion noted in a 14-year-old patient in whom pathogenic mutations were identified in the TK2 gene PMID: 12682338
exon 5 is a "hot spot" for TK2 mutations in patients with myopathic mitochondrial DNA depletion syndrome PMID: 12873860
Long-term treatment of H9 human lymphoid cells in the presence of dideoxycytidine down-regulated TK2 gene expression and reduced the expression and activity of TK in resistant cells. PMID: 14659972
import of cytosolic dNTPs in mitochondria of proliferating cells can compensate a TK2 induced imbalance of the mitochondrial dNTP pool PMID: 17065084
Using (124)I-FIAU, (18)F-FIAU, or (18)F-FEAU, it should be possible to image DeltahTK2 reporter gene expression with PET in preclinical and clinical studies. PMID: 17468435
activity of TK2 is curbed by thymidine phosphorylase, which degrades thymidine in the cytoplasm, thus limiting the availability of thymidine for phosphorylation by TK2 in mitochondria PMID: 17913703
A 12-year-old patient with mitochondrial DNA (mtDNA) depletion syndrome due to TK2 gene mutations has been evaluated serially over the last 10 years. We observed progressive muscle atrophy with selective loss of type 2 muscle fibers. PMID: 18021809
FMAU is preferably phosphorylated by TK2 and can track TK2 activity and mitochondrial mass in cellular stress. FMAU may provide an early marker of treatment effects. PMID: 18265975
Mutations in TK2, necessary for mtDNA biogenesis, increased risk for defective mtDNA replication, leading to LV hypertrophy. PMID: 18446447
Novel mutations(p.Q87X and p.N100S) in the TK2 gene associated with fatal mitochondrial DNA depletion myopathy. PMID: 18508266
Normal fibroblasts apparently contain more TK2 than needed to maintain dTTP during quiescence, which would explain why TK2-mutated fibroblasts do not manifest mtDNA depletion despite their reduced TK2 activity. PMID: 19154348
Gene mutations in TK2 resulting in MDS syndrome was studied. PMID: 19265691
Sequence analysis of the TK2 gene revealed two novel heterozygous mutations: the frame shift mutation, c.255_c.258delAGAA, and the heterozygous missense mutation, c.515G>A, (p.R172Q). PMID: 19736010

FAQs

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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.