Products

Enzymes for Research, Diagnostic and Industrial Use

Glutamate dehydrogenase, Recombinant

Cat No.
NATE-1145
Description
Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.
Abbr
GLDH, Recombinant
Alias
GLDH
Applications
Except glutamate dehydrogenation, GLDH can also catalytic the deaminase of other amino acids such as L-valine, L-2-aminobutyric acid and L-leucine. The main measuring method is continuous monitoring. Moreover, GLDH catalyzes the reaction of α-ketoglutarate, H+,ammonia and NADH to generating glutamic. Since NADH is the color source of many biochemical assays, therefore the reaction catalyzed by the corresponding GLDH is widely used to detect the final step of biochemical detection reagent.
Appearance
White powder, lyophilized
Product Overview
Glutamate dehydrogenase (GLDH, EC 1.4.1.2) is the enzyme present in the mitochondrial matrix of the cell. It can convert glutamic acid to α-ketoglutarate and catalyze the reverse reaction as well. GLDH is one of the allosteric enzymes which generated in the body through oxidative dehydrogenation, aminotransferase, combined dehydrogenation, non-oxidative dehydrogenation reaction and so on. The combined dehydrogenation is the most important reaction in the body. GLDH is an important molecular in the assimilation and alienation pathway. It is rich in the liver lobule cells followed by the kidney, pancreas, brain, small intestine and heart. Since GLDH is a kind of liver-specific enzyme, the change of GLDH activity in the peripheral blood reflects the changes of the liver function to some extent.
Enzyme Commission Number
EC 1.4.1.2
Activity
>400U/mg
CAS No.
9001-46-1
Molecular Weight
About 65kDa (SDS-PAGE detection)
Purity
>90% (SDS-PAGE test)
Unit Definition
One unit will convert 1µmol NADH per min at pH 8.3and at 37°C.
Storage
4°C, store at -20°C for long-term preservation.
Buffer
20mM Tris, PH8.0
Synonyms
glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehydrogenase; NAD+-glutamate dehydrogenase; NAD+-linked glutamate dehydrogenase; NAD+-linked glutamic dehydrogenase; NAD+-specific glutamic dehydrogenase; NAD+-specific glutamate dehydrogenase; NAD+:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase; GLDH; EC 1.4.1.2
Download Datasheet:


“GLDH” Total Products Page

Inquiry
Related Products
Catalog
ProductName
EC No.
CAS No.
Source
Price
CatalogNATE-1701
EC No.EC 1.4.1.2
CAS No.9001-46-1
SourceE. coli
CatalogNATE-1802
EC No.EC 1.4.1.2
CAS No.9001-46-1
SourceE. coli
CatalogDIA-146
EC No.EC 1.4.1.3
CAS No.9001-46-1
SourceBovine liver
CatalogDIA-196
EC No.EC 1.4.1.4
CAS No.2604121
SourceProteus sp.
+ See More >>
Related Services
Related Protocols
L-PHENYLALANINE DEHYDROGENASE -Enzymatic Assay Protocol
Online Inquiry
Name:
*Phone:
*E-mail Address:
Country:
Company/Institution:
*Products or Services Interested:
Quantity:
Project Description:
Our Products are Not Intended for Private Therapeutic Use!
*Verification Code:
Please input "enzymes"(case insensitive) as verification code.

Welcome! For price inquiries, please feel free to contact us through the form below through the form on the left side. We will get back to you as soon as possible.

Sitemap  Privacy Policy
Copyright ©2011 - 2017 Creative Enzymes.
Contact Us 45-1 Ramsey Road, Shirley, NY 11967, USA
Email: info@creative-enzymes.com
Tel: 1-631-562-8517 1-631-448-7888
Fax: 1-631-938-8127
Distributors To view the contact information for a specific location, select the desired country: