Succinyl-CoA synthetase

Succinyl-CoA synthetase
Item number Size Datasheet Manual SDS Delivery time Quantity Price
Cay22673-100 100 µg -

6 - 10 business days*

331.00€
Cay22673-1 1 mg -

6 - 10 business days*

1,322.00€
 
Succinyl-CoA synthetase from E. coli is responsible for the coupled hydrolysis of succinyl-CoA to... more
Product information "Succinyl-CoA synthetase"
Succinyl-CoA synthetase from E. coli is responsible for the coupled hydrolysis of succinyl-CoA to the production of ATP (or GTP) in the substrate-level phosphorylation step of the citric acid cycle (TCA). This enzyme complex is formed as a heterotetramer, alpha2beta2, where the two alpha subunits each contain the coenzyme A and phosphate binding sites, and the two beta subunits each contain the succinate binding sites and provide nucleotide binding specificity. This enzyme is Mg2+-dependent.Synonyms: SCS, Succinate Thiokinase, Succinyl Coenzyme A Synthetase. Purity: >85% estimated by SDS-PAGE. Source: Active E. coli (strain K12) C-terminal His-tagged Succinyl-CoA synthetase enzyme purified from E. coli. MW: 29.8 kDa (alpha), 41.4 kDa (beta). Formulation: (Request formulation change), 50 mM HEPES, pH 8.0, 150 mM sodium chloride, 20% glycerol. UniProt Accession #: P0A836, P0AGE9.
Keywords: b0729, SCS-alpha {ECO:0000255|HAMAP-Rule:MF_01988}, SCS-alpha {ECO:0000255|HAMAP-Rule:MF_01988}, Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988}, Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988}, Succinate--C
Supplier: Cayman Chemical
Supplier-Nr: 22673

Properties

Application: Enzyme assays
Conjugate: No
Purity: >85% estimated by SDS-PAGE
Format: Solution

Handling & Safety

Storage: -80°C
Shipping: -80°C (International: -80°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
You will get a certificate here
or to request a certificate of analysis.
Read, write and discuss reviews... more
Customer review for "Succinyl-CoA synthetase"
Write a review
or to review a product.
Viewed