Log In Sign up
The largest database of trusted experimental protocols

Rabbit aldolase

Manufactured by Merck Group
Visit Supplier

Rabbit aldolase is a laboratory enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-bisphosphate into glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. It is commonly used as a standard in biochemical assays and enzyme activity measurements.

Automatically generated - may contain errors

Lab products found in correlation

Yeast alcohol dehydrogenase, by Merck Group (2 mentions) Glycogen phosphorylase b from rabbit muscle, by Merck Group (2 mentions) Glutamate dehydrogenase from bovine liver, by Merck Group (2 mentions) Horse liver alcohol dehydrogenase, by Merck Group (2 mentions) Pyruvate kinase, by Merck Group (2 mentions) Beta galactosidase from escherichia coli, by Merck Group (2 mentions) Groes, by Merck Group (2 mentions)

2 protocols using rabbit aldolase

1

Preparation of Protein Complexes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein complex samples, including glycogen phosphorylase b from rabbit muscle (195 kDa), glutamate dehydrogenase from bovine liver (334 kDa), beta-galactosidase from Escherichia coli (464 kDa), horse liver alcohol dehydrogenase (80 kDa), yeast alcohol dehydrogenase (147 kDa), rabbit aldolase (158 kDa), GroES (84 kDa), and pyruvate kinase (232 kDa) were purchased from Sigma-Aldrich (St. Louis, MO). GroEL from Escherichia coli (802 kDa) was prepared57 and provided by Dr. I.D.G.C.; human superoxide dismutase (32 kDa) was provided by Dr. Y. Sheng and human transferrin receptor (157 kDa) was provided by Dr. M. Penichet.
Li H., Nguyen H.H., Ogorzalek Loo R.R., Campuzano I.D, & Loo J.A. (2018). An Integrated Native Mass Spectrometry and Top-Down Proteomics Method that Connects Sequence to Structure and Function of Macromolecular Complexes. Nature chemistry, 10(2), 139-148.
+ Open protocol
+ Expand
2

Preparation of Protein Complexes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein complex samples, including glycogen phosphorylase b from rabbit muscle (195 kDa), glutamate dehydrogenase from bovine liver (334 kDa), beta-galactosidase from Escherichia coli (464 kDa), horse liver alcohol dehydrogenase (80 kDa), yeast alcohol dehydrogenase (147 kDa), rabbit aldolase (158 kDa), GroES (84 kDa), and pyruvate kinase (232 kDa) were purchased from Sigma-Aldrich (St. Louis, MO). GroEL from Escherichia coli (802 kDa) was prepared57 and provided by Dr. I.D.G.C.; human superoxide dismutase (32 kDa) was provided by Dr. Y. Sheng and human transferrin receptor (157 kDa) was provided by Dr. M. Penichet.
Li H., Nguyen H.H., Ogorzalek Loo R.R., Campuzano I.D, & Loo J.A. (2018). An Integrated Native Mass Spectrometry and Top-Down Proteomics Method that Connects Sequence to Structure and Function of Macromolecular Complexes. Nature chemistry, 10(2), 139-148.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!