Saltar al contenido
Merck

C3260

Sigma-Aldrich

Citrate Synthase from porcine heart

ammonium sulfate suspension, ≥100 units/mg protein

Sinónimos:

Citrate condensing enzyme, Citrate oxaloacetate lyase (CoA-acetylating)

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine heart

Quality Level

form

ammonium sulfate suspension

specific activity

≥100 units/mg protein

mol wt

98 kDa ( 49 kDa monomer)

solubility

H2O: soluble 1.0 mg/mL, clear

foreign activity

isocitrate dehydrogenase and aconitase ≤0.01%
malic dehydrogenase ≤0.1%

storage temp.

2-8°C

Application

Citrate Synthase from porcine heart has been used:
  • to inject newt egg for determining its importance in egg activation at fertilization
  • in the preparation of reaction mix to determine pyruvate carboxylase enzyme activity
  • to examine whether it can induce a [Ca2+] increase and egg activation in unfertilized eggs

Biochem/physiol Actions

Citrate synthase catalyses the conversion of citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine.

Unit Definition

One unit will form 1.0 μmole of citrate from oxalacetate and acetyl CoA per min at pH 8.0 at 37 °C.

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 7.0.

Preparation Note

Dissolves in water to form a clear solution at 1 mg/mL concentration.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

Oded Rimon et al.
Antioxidants & redox signaling, 27(15), 1252-1267 (2017-04-11)
A recently discovered group of conditionally disordered chaperones share a very unique feature; they need to lose structure to become active as chaperones. This activation mechanism makes these chaperones particularly suited to respond to protein-unfolding stress conditions, such as oxidative
Skylar Xantus Kim et al.
eLife, 7 (2018-07-17)
Anhydrobiotes are rare microbes, plants and animals that tolerate severe water loss. Understanding the molecular basis for their desiccation tolerance may provide novel insights into stress biology and critical tools for engineering drought-tolerant crops. Using the anhydrobiote, budding yeast, we
Hairui Yuan et al.
PloS one, 8(1), e53887-e53887 (2013-01-18)
Aerobic exercise has beneficial effects on both weight control and skeletal muscle insulin sensitivity through a number of specific signaling proteins. To investigate the targets by which exercise exerts its effects on insulin resistance, an approach of proteomic screen was
Alterations in Cytosolic and Mitochondrial [U-13C] Glucose Metabolism in a Chronic Epilepsy Mouse Model
McDonald TS, et al.
eNeuro, 4(1), 266-276 (2017)
Adam Begeman et al.
EMBO reports, 21(10), e49735-e49735 (2020-09-19)
Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico