TKT Human

Transketolase Human Recombinant
Cat. No.
BT27154
Source
E.coli.
Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.
TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Transketolase (TKT) is a thiamine-dependent enzyme that plays a crucial role in the pentose phosphate pathway, channeling excess sugar phosphates into glycolysis. Multiple alternatively spliced variants exist, all of which encode the same protein.
Description
Recombinant human TKT, expressed in E. coli, is a single polypeptide chain consisting of 643 amino acids (residues 1-623) with a molecular weight of 70.0 kDa. The protein features a 20 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Colorless, sterile-filtered solution.
Formulation
The TKT solution is supplied at a concentration of 0.25 mg/ml in a buffer composed of 20 mM Tris-HCl (pH 8.0), 100 mM NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeds 85% as determined by SDS-PAGE analysis.
Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.

Product Science Overview

Genetic and Structural Information

The TKT gene is located on chromosome 3 at position 3p21.1 . It encodes a homodimeric enzyme with two active sites situated at the monomer contact surfaces . In addition to TKT, there are two other transketolase-like proteins in humans: TKTL1 and TKTL2, located on the X chromosome at Xq28 and chromosome 4 at 4q32.2, respectively . These proteins share structural similarities with TKT and are believed to be functional transketolases .

Biological Function

Transketolase is pivotal in generating sugar phosphates necessary for intracellular nucleotide metabolism and the production of nicotinamide adenine dinucleotide phosphate (NADPH), a crucial reducing agent and antioxidant . The enzyme’s activity is vital for maintaining cellular redox balance and supporting anabolic reactions.

Clinical Significance

Altered TKT functionality has been implicated in various diseases, including diabetes and cancer . For instance, hyperglycemic individuals often exhibit reduced TKT activity, which can be ameliorated by thiamine treatment, suggesting potential therapeutic applications for type 2 diabetes . Additionally, TKT activity and its nuclear localization have been linked to the progression of hepatocellular carcinoma (HCC), highlighting its role in both metabolic and non-metabolic pathways in cancer development .

Recombinant Transketolase

Recombinant transketolase is produced using genetic engineering techniques to express the human TKT gene in suitable host cells, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant TKT retains the functional properties of the native enzyme, making it a valuable tool for studying its role in cellular metabolism and disease.

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