{"product_id":"terminal-deoxynucleotidyl-transferase-tdt-bhp13700139","title":"Terminal Deoxynucleotidyl Transferase (TdT)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDT\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e DNA nucleotidylexotransferase; Terminal addition enzyme; Terminal deoxynucleotidyltransferase; Terminal transferase; TdT.\u003c\/p\u003e\u003cp\u003eTerminal Deoxynucleotidyl Transferase (TdT), expressed in Null\u003c\/p\u003e\u003cp\u003eTerminal deoxynucleotidyl transferase (TdT), also known as terminal transferase, is a specialized DNA polymerase expressed in immature, pre-B, pre-T lymphoid cells, and acute lymphoblastic leukemia\/lymphoma cells. Generally, TdT catalyses the addition of nucleotides to the 3' terminus of a DNA molecule. Unlike most DNA polymerases, it does not require a template. The preferred substrate of this enzyme is a 3'-overhang, but it can also add nucleotides to blunt or recessed 3' ends.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDT\u003c\/strong\u003e supports biochemical transformations that can be read out as changes in substrate\/product balance, metabolic intermediates, or signaling-relevant small molecules. Defined recombinant enzymes help enable mechanistic dissection and quantitative reconstitution studies. This target is frequently investigated in research themes such as \u003cstrong\u003eMetabolism \u0026amp; Enzymology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 58.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant bovine TdT consists of 520 amino acids and migrates with an apparent molecular mass of 58.3 kDa as estimated in SDS-PAGE under reducing conditions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Bovine TdT (X04122) (Mer1-Ala520) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 90 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Liquid in sterile 50 mM K2HPO4, 100 mM NaCl, 1 mM DTT, 0.1% Tween20, 1% BSA, 50% Glycerol, pH 6.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"40 ug","offer_id":52997740036461,"sku":"PRP3002-40UG","price":99.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740069229,"sku":"PRP3002-100UG","price":189.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP3002.png?v=1770191178","url":"https:\/\/www.ebiohippo.com\/products\/terminal-deoxynucleotidyl-transferase-tdt-bhp13700139","provider":"BioHippo","version":"1.0","type":"link"}