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Alanine Transaminase Active Protein

Alanine Transaminase, Recombinant, Human (ALT, Alanine Aminotransferase, Serum Glutamic Pyruvic Transaminase, SGPT)

Purity
Highly Purified
95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.
Synonyms
Alanine Transaminase; Recombinant; Human (ALT; Alanine Aminotransferase; Serum Glutamic Pyruvic Transaminase; SGPT); Alanine Transaminase active protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Highly Purified
95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.
Form/Format
Supplied as a liquid in 40mM sodium acetate buffer, pH 5.5, 1mM DTT, 1mM EDTA, 5mM 2-oxoglutarate, 0.1mM pyridoxal-5'-phosphate.
Concentration
1720 U/ml (varies by lot)
Biological Activity
~1020 U/mg.
Preparation and Storage
May be stored at 4 degree C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Aliquots are stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Related Product Information for Alanine Transaminase active protein
The enzyme alanine aminotransferase (AL T) was previously known as serum glutamic pyruvic transaminase (SGPT). This enzyme also is correctly referred to as alanine transaminase. ALT is a cytoplasmic enzyme that catalyzes the transamination of alpha-ketoglutarate and L-alanine forming glutamate and pyruvate.The highest activities of ALT are found in hepatocytes and striated (skeletal and cardiac) muscle cells. Therefore, increased serum ALT activity can accompany hepatocellular injury or necrosis of striated muscle. With cell injury or death, ALT (a "leakage" enzyme) escapes from the cytosol. Determination of ALT activity is a relatively sensitive indicator of hepatic damage in certain animal species and can help determine whether further tests. Recombinant ALT is a single, non-glycosylated, polypeptide chain containing 495 amino acids and having a molecufar mass of 54.4kD.
Product Categories/Family for Alanine Transaminase active protein

NCBI and Uniprot Product Information

NCBI GI #
Molecular Weight
54.4kD
NCBI Official Full Name
alanine transaminase

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Product Notes

The Alanine Transaminase (Catalog #AAA637359) is an Active Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Alanine Transaminase, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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