ATP5D Human

ATP Synthase Subunit D, Mitochondrial Human Recombinant

This product consists of a non-glycosylated polypeptide chain of ATP5D, produced in E. coli. It encompasses amino acids 23 to 168 of the human ATP5D protein and has a molecular weight of 17.3 kDa. A 21 amino acid His-tag is fused to the N-terminus to facilitate purification. The protein has been purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23546
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

ATP5O Human

ATP Synthase Subunit O, Mitochondrial Human Recombinant

Recombinant human ATP5O, expressed in E. coli, is a purified protein with a His tag attached to its N-terminus. This non-glycosylated polypeptide chain consists of 211 amino acids (residues 24-213) and has a molecular weight of 23.1 kDa. Purification is achieved through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23631
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

CS Human

Citrate Synthase Human Recombinant

This product consists of the human CS enzyme, recombinantly produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain with 462 amino acids (specifically, amino acids 28 to 466) and a molecular weight of 51.4 kDa. For purification purposes, a 23 amino acid His-tag is attached to the N-terminus of the CS protein. The purification process utilizes proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23692
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

DHPS Human

Deoxyhypusine Synthase Human Recombinant

Recombinant human DHPS, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein, with a molecular weight of 43.1 kDa, comprises 389 amino acids, including a 20 amino acid His tag at the N-terminus (1-369 a.a. of the DHPS sequence). Purification is achieved through proprietary chromatographic techniques, ensuring high purity.
Shipped with Ice Packs
Cat. No.
BT23777
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

FARS2 Human

Phenylalanyl-tRNA Synthetase 2 Human Recombinant

This product consists of the FARS2 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain with 436 amino acids (specifically, amino acids 37 to 451). The molecular weight of the protein is 50.6 kDa. For purification and ease of use, a 21 amino acid His-tag is fused to the N-terminus. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23876
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NANS Human

N-acetylneuraminic acid synthase Human Recombinant

This product offers recombinant human NANS protein, modified with a 20 amino acid His tag at its N-terminus. Produced in E.Coli, it exists as a single, non-glycosylated polypeptide chain comprising 379 amino acids (residues 1-359) with a molecular weight of 42.4kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24277
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

OXSM Human

3-Oxoacyl-ACP Synthase, Mitochondrial Human Recombinant

Recombinantly produced in E.coli, OXSM Human is a non-glycosylated polypeptide chain devoid of any post-translational modifications. This protein comprises 455 amino acids, spanning from position 28 to 459, resulting in a molecular weight of 48.1kDa. For purification and ease of use, a 23 amino acid His-tag is fused to the N-terminus of OXSM. The purification process utilizes proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT24472
Source
Escherichia Coli.
Appearance
The product is a clear solution that has undergone sterile filtration.

PAPSS1 Human

3'-Phosphoadenosine 5'-Phosphosulfate Synthase 1 Human Recombinant

Recombinant human PAPSS1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 626 amino acids (residues 24-624) with a molecular weight of 70.9 kDa. This protein is engineered with a 25-amino acid His-tag at the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24545
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

SEPSECS Human

Selenocysteinyl-tRNA(Sec) synthase Human Recombinant

Produced in E. coli, our SEPSECS is a single, non-glycosylated polypeptide chain consisting of 521 amino acids (specifically, amino acids 1 through 501). It has a molecular weight of 57.9 kDa. For purification purposes, a 20 amino acid His-tag is attached to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24978
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized through filtration.

SEPSECS Mouse

Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant

Produced in E. coli, our SEPSECS is a single, non-glycosylated polypeptide chain consisting of 527 amino acids (with the mature protein encompassing amino acids 1-504). It has a molecular weight of 57.7 kDa. For purification and ease of use, SEPSECS is tagged with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25058
Source
Escherichia Coli.
Appearance
Clear, sterile solution.
Definition and Classification

Synthase is a type of enzyme that catalyzes the synthesis of molecules in biological systems. Unlike synthetases, synthases do not require energy from nucleoside triphosphates like ATP . Synthases are classified based on the type of reaction they catalyze, such as ATP synthase, citrate synthase, and fatty acid synthase .

Biological Properties

Synthases exhibit diverse biological properties depending on their specific type and function. For instance, ATP synthase is ubiquitous across all life forms and is essential for ATP production . Expression patterns and tissue distribution vary; for example, ATP synthase is found in mitochondria, chloroplasts, and bacterial plasma membranes . Other synthases, like nitric oxide synthase, have specific expression patterns in neuronal, endothelial, and immune cells .

Biological Functions

The primary function of synthases is to facilitate the synthesis of complex molecules. ATP synthase, for example, is crucial for producing ATP, the main energy currency of cells . Synthases also play roles in immune responses and pathogen recognition. Nitric oxide synthase, for instance, produces nitric oxide, a signaling molecule involved in immune responses and vasodilation .

Modes of Action

Synthases operate through various mechanisms. ATP synthase, for example, uses a proton gradient to drive the synthesis of ATP from ADP and inorganic phosphate . This process involves the movement of protons through the enzyme, which acts as a rotary motor . Nitric oxide synthase, on the other hand, catalyzes the conversion of L-arginine to nitric oxide and L-citrulline, involving multiple cofactors and binding partners .

Regulatory Mechanisms

The activity and expression of synthases are tightly regulated. ATP synthase activity is regulated by the availability of ADP and inorganic phosphate, as well as the proton gradient across the mitochondrial membrane . Nitric oxide synthase is regulated at the transcriptional level by various cytokines and growth factors, and its activity is modulated by post-translational modifications such as phosphorylation .

Applications

Synthases have numerous applications in biomedical research, diagnostics, and therapeutics. ATP synthase inhibitors are being explored as potential treatments for cancer and infectious diseases . Nitric oxide synthase is a target for drugs aimed at treating cardiovascular diseases and inflammatory conditions . Synthases are also used as biomarkers in diagnostic assays for various diseases .

Role in the Life Cycle

Synthases play critical roles throughout the life cycle, from development to aging and disease. ATP synthase is essential for energy production in all stages of life . Dysregulation of synthase activity is associated with various diseases, including metabolic disorders, neurodegenerative diseases, and cancer . Nitric oxide synthase, for example, is involved in developmental processes, immune responses, and aging .

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