Technical Data
Citrate Synthase
The enzyme citrate synthase exists in nearly all living cells and stands as a pace-making enzyme in the first step of the Citric Acid Cycle (or Krebs Cycle). Citrate synthase is localized within eukaryotic cells in the mitochondrial matrix, but is encoded by nuclear DNA rather than mitochondrial. It is synthesized using cytoplasmic ribosomes, then transported into the mitochondrial matrix. Citrate synthase is commonly used as a quantitative enzyme marker for the presence of intact mitochondria.
Citrate synthase catalyzes the condensation reaction of the two-carbon acetate residue from acetyl coenzyme A and a molecule of four-carbon oxaloacetate to form the six-carbon citrate. Oxaloacetate will be regenerated after the completion of one round of the Krebs Cycle.

Suitable for use in ELISA, Western Blot, Dot Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Dot Blot: Non-reducing conditions only
Immunohistochemistry: Formaldehyde-fixed, paraffin embedded sections
Optimal dilution to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IcePorcineMouse
Porcine heart citrate synthase.
Supplied as a liquid in PBS, pH 7.6, 0.09% sodium azide.
Recognizes porcine citrate synthase. Shows intense intracellular granular reactivity with human muscle and liver when tested by IHC on formaldehyde-fixed, paraffin embedded tissue sections. In the case of anaerobic damage/necrosis, the affected cells showed characteristic loss of reactivity compared to normal tissue. Species Crossreactivity: human
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Hu, Q., et al., Am. J. Physiol. Heart Circ. Physiol. 291: H648-H657 (2006). General Reference: 1. Nemeth, P., et al., J. Mol. Recogn. 4: 77-83 (1991). 2. ICSU Short Reps. 10: 11 (1990). 3. Alter, G.M., et al., Biochemistry 29: 7557-7563 (1990).