ECHS1
Reactivité: Humain, Souris, Rat, Chien, Lapin, Boeuf (Vache), Cobaye, Mouton, Porc
WB
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
ECHS1 antibody can be used for detection of ECHS1 by ELISA at 1:312500. ECHS1 antibody can be used for detection of ECHS1 by western blot at 5.0 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Add 100 ?L of distilled water. Final antibody concentration is 1 mg/mL.
Concentration
1 mg/mL
Buffer
Antibody is lyophilized in PBS buffer with 2 % sucrose.
Conseil sur la manipulation
As with any antibody avoid repeat freeze-thaw cycles.
Stock
4 °C/-20 °C
Stockage commentaire
For short periods of storage (days) store at 4 °C. For longer periods of storage, store ECHS1 antibody at -20 °C.
Antigène
ECHS1
(Enoyl CoA Hydratase, Short Chain, 1, Mitochondrial (ECHS1))
anticorps SCEH, anticorps cOR6not, anticorps fj55e05, anticorps si:zc217g15.1, anticorps wu:fj55e05, anticorps C80529, anticorps enoyl-CoA hydratase, short chain, 1, mitochondrial L homeolog, anticorps enoyl-CoA hydratase, short chain 1, anticorps enoyl CoA hydratase, short chain, 1, mitochondrial, anticorps enoyl Coenzyme A hydratase, short chain, 1, mitochondrial, anticorps echs1.L, anticorps ECHS1, anticorps Echs1, anticorps echs1
Sujet
ECHS1 functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. ECHS1 is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix.The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix. Transcript variants utilizing alternative transcription initiation sites have been described in the literature.