Skip to Content
Merck
All Photos(1)

Key Documents

T6258

Sigma-Aldrich

Triosephosphate Isomerase from rabbit muscle

Type X, lyophilized powder, ≥3,500 units/mg protein

Synonym(s):

D-Glyceraldehyde-3-phosphate ketol-isomerase, TPI

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type X

Quality Level

form

lyophilized powder

specific activity

≥3,500 units/mg protein

mol wt

calculated mol wt 53.2 kDa

composition

Protein, 60-90% biuret

foreign activity

pyruvate kinase, lactic dehydrogenase, 3-phosphoglyceric phosphokinase, phosphoglucose isomerase, α-glycerophosphate dehydrogenase, aldolase and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

General description

Triosephosphate isomerase (TPI) gene is located on human chromosome 12p13. It is expressed in all tissues. This homodimer of two 27 kDa subunits is highly stable and is made up of 248 amino acids. TPI is catalytically active in its dimeric state.

Application

Triosephosphate Isomerase from rabbit muscle has been complexed with p-hydroxymercurybenzoate (PHMB) to denature the protein for hydrophobic interaction chromatography coupled online with chemical vapour atomic fluorescence spectrometry (HIC−CVGAFS).
Triosephosphate isomerase has been used in a study to assess changes in cardiac energy metabolic pathways in overweight rats fed a high-fat diet. Triosephosphate isomerase has also been used in a study to investigate proteomic identification of carbonylated proteins in F344 rat hippocampus after 1-bromopropane exposure.

Biochem/physiol Actions

Triosephosphate isomerase (TPI) is responsible for the catalysis of the triose phosphate isomers, dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. TPI deficiency is associated with glycolytic enzymopathy. Lack of TPI is also associated with chronic hemolytic anemia, enhanced exposure to bacterial infections, cardiomyopathy and neuromuscular disease.

Packaging

Package size based on protein content

Unit Definition

One unit will convert 1.0 μmole D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 at 25 °C.

Physical form

Sulfate-free, contains EDTA and borate buffer salts

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Hydrophobic interaction chromatography coupled with atomic fluorescence spectrometric detection: Effect of the denaturation on the determination of thiolic proteins
Bramanti E, et al.
Talanta, 63(2), 383-389 (2004)
Red blood cell enzymopathies
Hematology, 616-625 (2018)
Changes in cardiac energy metabolic pathways in overweighed rats fed a high-fat diet
Modrego, J., et al.
European Journal of Nutrition, DOI: 10-DOI: 10 (2012)
Zhenlie Huang et al.
Toxicology and applied pharmacology, 263(1), 44-52 (2012-06-12)
1-Bromopropane (1-BP) is neurotoxic in both experimental animals and humans. Previous proteomic analysis of rat hippocampus implicated alteration of protein expression in oxidative stress, suggesting that oxidative stress plays a role in 1-BP-induced neurotoxicity. To understand this role at the
Triosephosphate isomerase deficiency: new insights into an enigmatic disease
Orosz F, et al.
Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1792(12), 1168-1174 (2009)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service