Recombinant Human DNTT/TDT Protein (N-6His)

Name: Recombinant Human DNTT/TDT Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-2609NP
Availability: InStock

BL-2609NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human DNA Nucleotidylexotransferase is produced by our E.coli expression system and the target gene encoding Met1-Ala509 is expressed with a 6His tag at the N-terminus.
Accession	P04053
Synonym	DNA nucleotidylexotransferase; Terminal addition enzyme; Terminal deoxynucleotidyltr; Terminal deoxynucleotidyltransferase; Terminal transferase; DNTT; TDT
Gene Background	Terminal deoxynucleotidyl transferase (TdT) is a highly conserved vertebrate enzyme that possesses the unique ability to catalyze the random addition of deoxynucleoside 5'-triphosphates onto the 3'-hydroxyl group of a single-stranded DNA. It plays an important role in the generation of immunoglobin and T-cell receptor diversity. 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.
Molecular Mass	60.7 KDa
Apmol Mass	62 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 0.1M KH2PO4, 200mM KCl, 1mM 2-Mercaptoethanol, 50% Glycerol, pH 7.2.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% 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	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.
Subcellular Location	Nucleus.
Protein Families	DNA polymerase type-X family
Database References	HGNC: 2983 OMIM: 187410 KEGG: hsa:1791 STRING: 9606.ENSP00000360216 UniGene: Hs.534206

Gene Functions References

TdT protein can be found in cells of epithelial origin and specifically sebaceous cells, both benign and malignant. PMID: 28677299
Structural basis for a new templated activity by terminal deoxynucleotidyl transferase and implications for V(D)J recombination have been described. PMID: 27499438
TdT-positive cells may be part of the inflammatory milieu in infant kidneys. PMID: 28248816
Absence of TdT expression identifies a subset of high-risk T-acute lymphoblastic leukemia/lymphoma that overlaps with, but is not identical to, the ETP leukemia, providing additional prognostic value. PMID: 23702731
Our study confirms that PAX5 and TdT expression can be expressed in a high percentage of Merkel cell carcinomas and so when positive are not diagnostic of lymphoblastic leukemia/lymphoma. PMID: 23329999
role in DNA repair PMID: 11974916
Overexpression of newly discovered alternatively spliced short or long human TdT isoforms greatly reduces the efficiency of recombination, which is reverted to normal levels by the simultaneous expression of both enzymes. PMID: 15356150
In spleen, appendix and branchial cleft cysts the range of TdT-positivity was 0-13, 0-96 and 0-6 TdT+ cells per high-power field. PMID: 16885057
The TdT binding, DNA binding and dimerization regions, and nuclear localization signal (NLS) in TdIF1, were identified. PMID: 17663723

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.