Triosephosphate Isomerase (TPI)

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Description

Product name: Triosephosphate Isomerase (TPI)

Product description: Recombinant Human TPI enzyme (active) produced in Nicotiana benthamiana by Agrobacterium-mediated transient expression.

Host species: Nicotiana benthamiana

Molecular weight: 54 kDa dimer (2x 27 kDa subunits)

Tag: N-terminal His-tag

Uses: For research use only. Examples include SDS-PAGE, Western Blot, functional assays.

Relevance: Involved in gluconeogenesis (carbohydrate biosynthesis) and glycolysis (carbohydrate degradation). TPI catalyses the reversible conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate D-glyceraldehyde. TPI deficiency (TPID) is an autosomal recessive disorder which is characterized by several traits including progressive neuromuscular dysfunction, cardiomyopathy, susceptibility to bacterial infection and congenital haemolytic anaemia.1,2.

Specification:

Purity: >99 % as shown by SDS-PAGE.

 

 

 

 

 

 

 

 

 

Figure 1: reducing 4-20% SDS-PAGE analysis of 5 µg TPI.

 

 

 

 

 

 

 

 

 

 

 

 

 

Figure 2: Latter stage of TPI activity assay showing linear change in absorption (450 nm) over 15 minutes up until reaction saturation.

Biological activity: Active. >1000 mU/mg. Measuring the conversion of dihydroxyacetone phosphate (DHAP) to glyceradehyde-3-phosphate (GAP).

Endotoxin: Not tested.

Storage

Formulation: Lyophilized from 20 mM Tris-HCl, pH 7.5, 175 mM Trehalose Dihydrate and 0.9 mM DTT.

Shipped: Recombinant proteins are sterile-filtered and provided as lyophilized powder which are shipped at ambient temperature.

Stability & Storage: See COA for detailed storage instructions. Lyophilized materials are stable for up to twelve months from date of receipt at -70℃.

It is recommended that reconstituted protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Reconstitution: A hardcopy of COA with reconstitution instructions is included with the product.

References:

  1. https://www.uniprot.org/uniprot/P60174
  2. Orosz F, Olàh J, Ovádi J. Triosephosphate isomerase deficiency: new insights into an enigmatic disease. 1792(12):1168-74 (2009)