Log In Sign up
The largest database of trusted experimental protocols

Phgdh ab198455

Manufactured by Abcam
Visit Supplier

PHGDH (ab198455) is a recombinant protein that corresponds to a portion of the human phosphoglycerate dehydrogenase (PHGDH) protein. PHGDH is an enzyme involved in the serine biosynthesis pathway.

Automatically generated - may contain errors

Lab products found in correlation

Oxopentanoic acid, by Merck Group (2 mentions) Oxoadipic acid, by Merck Group (2 mentions) Pyruvate, by Merck Group (2 mentions) L lactate, by Merck Group (2 mentions) Alpha ketoglutarate, by Merck Group (2 mentions) Dimethyl alpha ketoglutarate, by Merck Group (2 mentions) Alpha ketobutyrate, by Merck Group (2 mentions) L2500, by Merck Group (2 mentions) D 2 hydroxyglutarate, by Merck Group (2 mentions) L malate, by Merck Group (2 mentions) D malate, by Merck Group (2 mentions) L 2 hydroxyglutarate, by Merck Group (2 mentions) D lactate, by Merck Group (2 mentions) Oxaloacetate, by Merck Group (2 mentions) Pcdna3.1 vector, by Addgene (2 mentions)

Spelling variants of this product

PHGDH (2 citations)

2 protocols using phgdh ab198455

1

Enzyme Purification and Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Purified enzymes were purchased from Sigma, including LDH from bovine heart (L2625), LDH from rabbit muscle (L2500), and MDH from porcine heart (M1567). Recombinant human enzymes were purchased from Abcam, including LDHA (ab93699), MDH1 (ab99244), MDH2 (ab99238), IDH1 (ab113858), and PHGDH (ab198455). Substrates, cofactors, and inhibitors were purchased from Sigma, including pyruvate, oxaloacetate, alpha-ketoglutarate, dimethyl-alpha-ketoglutarate, L-lactate, D-lactate, L-malate, D-malate, L-2-hydroxyglutarate, D-2-hydroxyglutarate, alpha-ketobutyrate, oxopentanoic acid, oxoadipic acid, ketohexanoic acid, phenylpyruvate, hydroxyphenylpyruvate, NADH, NADPH, and oxamate. FLAG-tagged wildtype and Q100R mutant LDHA constructs were cloned into the PCDNA3.1(+) vector (Addgene) by standard site-directed mutagenesis and verified by Sanger sequencing.
Intlekofer A.M., Wang B., Liu H., Shah H., Carmona-Fontaine C., Rustenburg A.S., Salah S., Gunner M.R., Chodera J.D., Cross J.R, & Thompson C.B. (2017). L-2-hydroxyglutarate production arises from non-canonical enzyme function at acidic pH. Nature chemical biology, 13(5), 494-500.
+ Open protocol
+ Expand
2

Enzyme Purification and Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Purified enzymes were purchased from Sigma, including LDH from bovine heart (L2625), LDH from rabbit muscle (L2500), and MDH from porcine heart (M1567). Recombinant human enzymes were purchased from Abcam, including LDHA (ab93699), MDH1 (ab99244), MDH2 (ab99238), IDH1 (ab113858), and PHGDH (ab198455). Substrates, cofactors, and inhibitors were purchased from Sigma, including pyruvate, oxaloacetate, alpha-ketoglutarate, dimethyl-alpha-ketoglutarate, L-lactate, D-lactate, L-malate, D-malate, L-2-hydroxyglutarate, D-2-hydroxyglutarate, alpha-ketobutyrate, oxopentanoic acid, oxoadipic acid, ketohexanoic acid, phenylpyruvate, hydroxyphenylpyruvate, NADH, NADPH, and oxamate. FLAG-tagged wildtype and Q100R mutant LDHA constructs were cloned into the PCDNA3.1(+) vector (Addgene) by standard site-directed mutagenesis and verified by Sanger sequencing.
Intlekofer A.M., Wang B., Liu H., Shah H., Carmona-Fontaine C., Rustenburg A.S., Salah S., Gunner M.R., Chodera J.D., Cross J.R, & Thompson C.B. (2017). L-2-hydroxyglutarate production arises from non-canonical enzyme function at acidic pH. Nature chemical biology, 13(5), 494-500.
+ 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!