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Key Documents

SRP0288

Sigma-Aldrich

ATP Citrate Lyase Active human

recombinant, expressed in baculovirus, ≥90% (SDS-PAGE)

Synonyme(s) :

ACLY, ATP-citrate synthase, ATPCL, CLATP

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About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in baculovirus

Pureté

≥90% (SDS-PAGE)

Forme

aqueous solution

Activité spécifique

≥1.2 pmol/min-μg

Poids mol.

147 kDa

Numéro d'accès NCBI

NM_001096

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

mouse ... ACLY(47)

Description générale

Human ATP citrate lyase (ACLY) (GenBank Accession No. NM_001096), full length, with N-terminal GST tag, MW = 147 kDa, expressed in baculovirus expression system.

Application

Active human ATP citrate lyase is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Active human ATP citrate lyase has been used in a study to ascertain the nature of the catalytic phosphorylation that initiates the ACL reaction, and to identity the active site residues involved. Active human ATP citrate lyase has also been used in a study to analyze tumor metabolism to reveal mitochondrial glucose oxidation in genetically diverse human glioblastomas.

Actions biochimiques/physiologiques

ATP citrate lyase is an enzyme involved in fatty acid synthesis that generates cytosolic acetyl-CoA and oxaloacetate from citrate and CoA. ATP citrate lyase is often upregulated in cancer.

Définition de l'unité

One unit is defined as the amount of enzyme required to convert 1 pmol of ADP to ATP/min at 37°C.

Forme physique

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 10% glycerol.

Notes préparatoires

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Fabiola Márquez et al.
Critical reviews in food science and nutrition, 52(7), 585-594 (2012-04-26)
Several studies have shown that Garcinia cambogia plays an important role in the regulation of endogenous lipid biosynthesis. This effect is specially attributed to (-)-hydroxycitric acid (HCA) inhibiting the enzyme ATP-dependent citrate lyase, which catalyzes the cleavage of citrate to
Isaac Marin-Valencia et al.
Cell metabolism, 15(6), 827-837 (2012-06-12)
Dysregulated metabolism is a hallmark of cancer cell lines, but little is known about the fate of glucose and other nutrients in tumors growing in their native microenvironment. To study tumor metabolism in vivo, we used an orthotopic mouse model
Fan Fan et al.
Biochemistry, 51(25), 5198-5211 (2012-06-05)
ATP citrate lyase (ACL) catalyzes an ATP-dependent biosynthetic reaction which produces acetyl-coenzyme A and oxaloacetate from citrate and coenzyme A (CoA). Studies were performed with recombinant human ACL to ascertain the nature of the catalytic phosphorylation that initiates the ACL

Articles

Fatty Acid Synthesis in Cancer Cells

Fatty acid synthesis supports cancer cell proliferation, essential for membrane generation, protein modification, and bioenergetics.

Fatty Acid Synthesis in Cancer Cells

Fatty acid synthesis supports cancer cell proliferation, essential for membrane generation, protein modification, and bioenergetics.

Fatty Acid Synthesis in Cancer Cells

Fatty acid synthesis supports cancer cell proliferation, essential for membrane generation, protein modification, and bioenergetics.

Fatty Acid Synthesis in Cancer Cells

Fatty acid synthesis supports cancer cell proliferation, essential for membrane generation, protein modification, and bioenergetics.

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