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C4780

Sigma-Aldrich

Coenzyme A sodium salt hydrate

BioReagent, suitable for cell culture

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Synonym(s):
CoA Na2
Empirical Formula (Hill Notation):
C21H36N7O16P3S · xNa+ · yH2O
CAS Number:
55672-92-9
Molecular Weight:
767.53 (anhydrous free acid basis)
EC Number:
259-747-8
PubChem Substance ID:
24892723
NACRES:
NA.75

biological source

yeast

Quality Level

200

description

cofactor for acyl transfer

product line

BioReagent

Assay

≥85% (HPLC)

form

powder

technique(s)

cell culture | mammalian: suitable

solubility

water: 50 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

[Na+].CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)([O-])=O)n2cnc3c(N)ncnc23)C(O)C(=O)NCCC(=O)NCCS

InChI key

SYTRWOCXZXQBPW-CLVRNSBASA-M

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Coenzyme A sodium salt hydrate BioReagent, suitable for cell culture

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assay

≥85% (HPLC)

assay

≥99% (HPLC)

assay

≥99% (HPLC)

assay

≥98% (HPLC)

form

powder

form

powder

form

powder

form

powder

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | insect: suitable, cell culture | mammalian: suitable

solubility

water: 50 mg/mL, clear, colorless to faintly yellow

solubility

H2O: 50 mg/mL, clear, colorless

solubility

H2O: 50 mg/mL

solubility

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Application

Coenzyme A sodium salt hydrate has been used:
  • in the branch chain aminotransferase enzymatic assay and protein determination
  • in the assay for halogenation of pyrrolyl-S-Bmp1 (an acyl carrier protein (ACP)-thioesterase (TE) di-domain protein) by Bmp2
  • as an extracellular coenzyme A (CoA) in in vitro and in vivo experiments to study alternative routes by which cells and organisms can obtain CoA

Biochem/physiol Actions

Coenzyme A (CoA) is a ubiquitous cofactor that plays an important role in many metabolic pathways, mainly as acyl-CoA. It is essential for the tricarboxylic acid cycle, and the synthesis and oxidation of fatty acids. CoA facilitates acyl group transfers, especially in fatty acid and lipid metabolism reactions. It is associated with neurodegeneration, autophagy, protein acetylation, and signal transduction.

Quality

Enzymatically assayed using phosphotransacetylase. Approx. 95% CoA-SH

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Balaji Srinivasan et al.
Nature chemical biology, 11(10), 784-792 (2015-09-01)
The metabolic cofactor coenzyme A (CoA) gained renewed attention because of its roles in neurodegeneration, protein acetylation, autophagy and signal transduction. The long-standing dogma is that eukaryotic cells obtain CoA exclusively via the uptake of extracellular precursors, especially vitamin B5
Yongzhong Wei et al.
World journal of gastroenterology, 14(2), 193-199 (2008-01-12)
Nonalcoholic fatty liver disease (NAFLD) includes hepatic steatosis, nonalcoholic steatohepatitis (NASH), fibrosis, and cirrhosis. NAFLD is the most common liver disorder in the United States and worldwide. Due to the rapid rise of the metabolic syndrome, the prevalence of NAFLD
Yao Rong et al.
eLife, 10 (2021-08-20)
TMEM120A, a member of the transmembrane protein 120 (TMEM120) family, has a pivotal function in adipocyte differentiation and metabolism, and may also contribute to sensing mechanical pain by functioning as an ion channel named TACAN. Here we report that expression
Krista Yang et al.
STAR protocols, 2(3), 100687-100687 (2021-08-18)
Carnitine palmitoyltransferase-1 (CPT-1) is a rate-controlling enzyme for long-chain fatty acid oxidation. This manuscript provides protocols for measuring CPT-1-mediated respiration in permeabilized, adherent cell monolayers and mitochondria freshly isolated from tissue, along with examples to assess the potency and specificity
Le Tran Phuc Khoa et al.
Cell stem cell, 27(3), 441-458 (2020-07-02)
Self-renewing embryonic stem cells (ESCs) respond to environmental cues by exiting pluripotency or entering a quiescent state. The molecular basis underlying this fate choice remains unclear. Here, we show that histone acetyltransferase MOF plays a critical role in this process

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