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Human Aspartate Aminotransferase

 Product Information

Cat #
MBS-1170
CAS No.
9000-97-9
Enzyme Commission Number
EC 2.6.1.1
Product Overview
High-quality enzyme products. Well-defined strains can be also provided for our clients to manufacture fermented products in a cost-effective way.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminotransferase; aspartyl aminotransferase; AST (ambiguous); glutamate-oxalacetate aminotransferase; glutamate-oxalate transaminase; glutamic-aspartic aminotransferase; glutamic-oxalacetic transaminase; glutamic oxalic transaminase; GOT (enzyme) [ambiguous]; L-aspartate transaminase; L-aspartate-α-ketoglutarate transaminase; L-aspartate-2-ketoglutarate aminotransferase; L-aspartate-2-oxoglutarate aminotransferase; L-aspartate-2-oxoglutarate-transaminase; L-aspartic aminotransferase; oxaloacetate-aspartate aminotransferase; oxaloacetate transferase; aspartate:2-oxoglutarate aminotransferase; glutamate oxaloacetate transaminase
Type
Function
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis, some EC 2.6.1.57 activity can be found in this enzyme from other sources; indeed the enzymes are identical in Trichomonas vaginalis.
Applications
Research Use
Storage
Store at -20°C
Storage Buffer
Shelf Life
Strains
Source
Human Heart
Appearance
Molecular Weight
~92,000
Color / Form
Instruction
Enzyme Class
Transferases
Production Methods
Fermentation
Activity
> 5 U/mg
Specific Enzyme Activity
Purity
Purified (Control Grade)
Unit Definition
One unit will catalyze the transamination of one micromole of L-aspartate to alpha-ketoglutarate forming L-glutamate and oxaloacetate per minute at 37°C and pH 7.8. Measured at 340 nm as one equimolar amount of NAD produced by a coupled reaction.
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage

 Description

AST is found in many tissues throughout the body, including the liver, heart, muscles, kidney, and brain. If any of these organs or tissues is affected by disease or injury, AST is released into the bloodstream. This means that AST isn't as specific an indicator of liver damage as ALT (also known as alanine aminotransferase, another type of enzyme found almost entirely in the liver).

For Research Use Only.
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