DNA nucleotidylexotransferase Recombinant Protein | TDT recombinant protein

Recombinant Human DNA nucleotidylexotransferase

Cat. Num. AAA949669

• Gene Names: DNTT; TDT
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: DNA nucleotidylexotransferase; Recombinant Human DNA nucleotidylexotransferase; Terminal addition enzyme Terminal deoxynucleotidyltransferase; TDT recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-509. Full Length
• Sequence: MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for TDT recombinant protein

template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

Product Categories/Family for TDT recombinant protein

Immunology

References

Expression of human terminal deoxynucleotidyl transferase in Escherichia coli.Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., Bollum F.J.J. Biol. Chem. 260:10495-10502(1985) Human terminal deoxyribonucleotidyltransferase molecular cloning and structural analysis of the gene and 5' flanking region.Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988) Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen.Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A., Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H., Koiwai O.Genes Cells 6:815-824(2001) Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. The DNA sequence and comparative analysis of human chromosome 10.Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.Nature 429:375-381(2004) Isolation of putative promoter region for human terminal deoxynucleotidyltransferase gene.Koiwai O., Morita A.Biochem. Biophys. Res. Commun. 154:91-100(1988) Molecular cloning of human terminal deoxynucleotidyltransferase.Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984) Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase.Yang B., Gathy K.N., Coleman M.S.J. Biol. Chem. 269:11859-11868(1994) Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65.Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.Genes Cells 6:641-652(2001) Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone.Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.Genes Cells 8:559-571(2003) Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase.Mahajan K.N., Mitchell B.S.Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) Direct binding of TReP-132 with TdT results in reduction of TdT activity.Fujisaki S., Sato A., Toyomoto T., Hayano T., Sugai M., Kubota T., Koiwai O.Genes Cells 11:47-57(2006) Solution structure of BRCT domain of terminal deoxynucleotidyltransferase.RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 63054852
• NCBI GeneID: 1791
• NCBI Accession #: NP_001017520.1
• NCBI GenBank Nucleotide #: NM_001017520.1
• UniProt Accession #: P04053; Q53FH1; Q5W103; Q96E50
• Molecular Weight: 62.5 kDa
• NCBI Official Full Name: DNA nucleotidylexotransferase isoform 2
• NCBI Official Synonym Full Names: DNA nucleotidylexotransferase
• NCBI Official Symbol: DNTT
• NCBI Official Synonym Symbols: TDT
• NCBI Protein Information: DNA nucleotidylexotransferase
• UniProt Protein Name: DNA nucleotidylexotransferase
• Protein Family: DNA nucleotidylexotransferase
• UniProt Gene Name: DNTT
• UniProt Synonym Gene Names: Terminal transferase
• UniProt Entry Name: TDT_HUMAN

NCBI Description

This gene is a member of the DNA polymerase type-X family and encodes a template-independent DNA polymerase that catalyzes the addition of deoxynucleotides to the 3'-hydroxyl terminus of oligonucleotide primers. In vivo, the encoded protein is expressed in a restricted population of normal and malignant pre-B and pre-T lymphocytes during early differentiation, where it generates antigen receptor diversity by synthesizing non-germ line elements (N-regions) at the junctions of rearranged Ig heavy chain and T cell receptor gene segments. Alternatively spliced transcript variants encoding different isoforms of this gene have been described. [provided by RefSeq, Jul 2008]

Uniprot Description

DNTT: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. Belongs to the DNA polymerase type-X family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Transferase; EC 2.7.7.31

Chromosomal Location of Human Ortholog: 10q23-q24

Cellular Component: cytoplasm; nucleoplasm; nucleus

Molecular Function: DNA binding; DNA nucleotidylexotransferase activity; DNA-directed DNA polymerase activity; metal ion binding; protein binding

Biological Process: DNA metabolic process; DNA modification