GOT1 Human

Glutamic-Oxaloacetic Transaminase 1 Human Recombinant

This recombinant GOT1 protein was produced in E. coli and is a single, non-glycosylated polypeptide chain. It consists of 433 amino acids, with amino acids 1-413 representing the GOT1 sequence, and has a molecular weight of 48.4 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT612
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

GOT1 Human, Active

Glutamic-Oxaloacetic Transaminase 1 Human Recombinant, Active

This product consists of the human recombinant GOT1 enzyme, which has been expressed in E. coli and purified to a high degree. The protein sequence includes amino acids 1 to 413 of the GOT1 protein with an additional 20 amino acid His-Tag fused at the N-terminus. The molecular weight of the recombinant protein is 48.4 kDa. Glycosylation is not present in this recombinant protein.
Shipped with Ice Packs
Cat. No.
BT682
Source
Escherichia Coli.
Appearance
The product is a clear and colorless solution that has been sterilized by filtration.

GOT2 Mouse, Active

Glutamic-Oxaloacetic Transaminase 2, Active Mouse Recombinant

Recombinant Mouse GOT2, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 422 amino acids (residues 30-430). The protein has a molecular mass of 46.8 kDa. For purification purposes, a 21 amino acid His tag is fused to the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1142
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless solution

GPT Human

Glutamic-Pyruvate Transaminase Human Recombinant

Recombinant Human GPT, expressed in E.coli, is a non-glycosylated polypeptide chain consisting of 516 amino acids (residues 1-496) with a molecular weight of 56.8 kDa. This protein is engineered with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1228
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

GPT Human, Active

Glutamic-Pyruvate Transaminase Human Recombinant, Active

Recombinant Human Alanine Aminotransferase is produced in E. coli. It is a homodimeric, non-glycosylated polypeptide chain consisting of 495 amino acids with a molecular weight of 54,479 Daltons. The amino acid sequence is identical to that of the native human liver ALT. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1288
Source
Escherichia Coli.
Appearance
Sterile Liquid

GPT Human, His Active

Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant

This product consists of recombinant human GPT, expressed in E. coli and purified to a high degree. It is a single polypeptide chain, lacking glycosylation, with 516 amino acids (residues 1-496). The protein has a molecular weight of 56.8 kDa. For purification and detection purposes, a 20 amino acid His-tag is fused to the N-terminus.
Shipped with Ice Packs
Cat. No.
BT1387
Source
E.coli.
Appearance
The product is a sterile, colorless solution.

GPT Mouse

Glutamic-Pyruvate Transaminase Mouse Recombinant

Recombinant GPT Mouse protein, expressed in E.Coli, is a single polypeptide chain lacking glycosylation. It consists of 519 amino acids, with amino acids 1-496 representing the main protein sequence, and has a molecular weight of 57.5kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1466
Source
Escherichia Coli.
Appearance
Sterile filtered solution, colorless in appearance.

BCAT1 Human

Branched Chain Amino-Acid Transaminase 1 Human Recombinant

Recombinant BCAT1, produced in E. coli, is a single chain protein consisting of 409 amino acids (1-386) with a molecular weight of 45.4kDa. It includes a 23 amino acid His-tag attached to the N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT365
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

BCAT2 Human

Branched Chain Amino-Acid Transaminase 2 Human Recombinant

Recombinant human BCAT2 protein was expressed in E. coli and purified to greater than 90% purity. The protein is a single, non-glycosylated polypeptide chain containing 390 amino acids (residues 28-392) with a His-tag on the N-terminus. The molecular weight of the protein is 43.9 kDa.
Shipped with Ice Packs
Cat. No.
BT419
Source
Escherichia Coli.
Appearance
Clear, colorless and sterile-filtered solution.

GFPT1 Human

Glutamine--Fructose-6-Phosphate Transaminase 1 Human Recombinant

Recombinant human GFPT1 protein has been produced in E. coli. This non-glycosylated polypeptide chain consists of 391 amino acids (residues 332-699) and has a molecular weight of 43.7 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT514
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Transaminases, also known as aminotransferases, are enzymes that catalyze the transfer of an amino group from an amino acid to a keto acid. This process is known as transamination. Transaminases are crucial for the synthesis of amino acids, which are the building blocks of proteins . They are classified based on the specific amino/keto acid pairs they act upon. For example, alanine transaminase (ALT) and aspartate transaminase (AST) are two well-known types .

Biological Properties

Transaminases exhibit several key biological properties:

  • Expression Patterns: Transaminases are expressed in various tissues, with high concentrations in the liver, heart, and muscles .
  • Tissue Distribution: ALT is predominantly found in the liver, while AST is present in both the liver and heart .
Biological Functions

Transaminases play a vital role in:

  • Amino Acid Metabolism: They facilitate the conversion of amino acids to keto acids, which can enter metabolic pathways like the citric acid cycle .
  • Immune Responses and Pathogen Recognition: Transaminases are involved in the synthesis of amino acids necessary for the production of immune cells and antibodies .
Modes of Action

Transaminases operate through a mechanism involving the coenzyme pyridoxal phosphate (PLP). The process can be divided into two half-reactions:

  1. The amino group from an amino acid is transferred to PLP, forming pyridoxamine phosphate.
  2. Pyridoxamine phosphate then transfers the amino group to a keto acid, forming a new amino acid .
Regulatory Mechanisms

The expression and activity of transaminases are regulated through:

  • Transcriptional Regulation: Gene expression of transaminases is controlled by various transcription factors in response to cellular needs .
  • Post-Translational Modifications: Phosphorylation and other modifications can alter the activity of transaminases .
Applications

Transaminases have several applications in biomedical research and clinical practice:

  • Diagnostic Tools: Elevated levels of ALT and AST in the blood are used as biomarkers for liver and heart diseases .
  • Therapeutic Strategies: Transaminases are explored for their potential in developing treatments for metabolic disorders .
Role in the Life Cycle

Throughout the life cycle, transaminases are involved in:

  • Development: They are essential for the synthesis of amino acids required for growth and development .
  • Aging and Disease: Changes in transaminase activity are associated with aging and various diseases, including liver and cardiovascular conditions .
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