| Catalog# |
C260 |
| Source |
E.coli |
| Description |
Recombinant Human Triosephosphate Isomerase/TIM is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Gln249) of Human TPI1 fused with a His tag at the N-terminus. |
| Names |
Triosephosphate Isomerase, TIM, Triose-Phosphate Isomerase, TPI1, TPI |
| Accession # |
P60174 |
| Formulation |
Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 1mM DTT, 10% Glycerol, pH 8.0 |
| Shipping |
The product is shipped on dry ice/ice packs. |
| Storage |
Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles. |
| Purity |
Greater than 95% as determined by reducing SDS-PAGE. |
| Endotoxin |
Less than 0.1 ng/µg (1 IEU/µg). |
| Amino Acid Sequence |
MGSSHHHHHHSSGLVPRGSHMAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPP TAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELI GQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGK TATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE FVDIINAKQ
|
| Background |
Triose-phosphate isomerase, also named Triose-phosphate isomerase, TPI and TIM, is an enzyme that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI deficiency is an autosomal recessive disorder and the most severe clinical disorder of glycolysis. Triose phosphate isomerase deficiency is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection and characterized by chronic hemolytic anemia. |
