SMS Human

Spermine Synthase Human Recombinant

Recombinant human SMS protein is produced in E.coli. It is a single, non-glycosylated polypeptide chain consisting of 390 amino acids (residues 1-366) with a molecular weight of 43.8kDa. A 24 amino acid His-tag is fused to the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25155
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

SRM Human

Spermidine Synthase Human Recombinant

Recombinant human spermidine synthase (SRM) is a purified protein produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 322 amino acids (with a 20 amino acid His tag at the N-terminus) and has a molecular weight of 36 kDa. The protein is purified using proprietary chromatographic techniques and is greater than 95% pure as determined by SDS-PAGE.
Shipped with Ice Packs
Cat. No.
BT25224
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution.

ASNS Mouse

Asparagine Synthetase Mouse Recombinant

Mouse ASNS, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain comprising 568 amino acids (1-562 a.a.) with a molecular weight of 65.2 kDa. It includes a 6-amino acid His tag at the C-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT23375
Source

Sf9, Insect cells.

Appearance
Sterile Filtered colorless solution.

ASS1 Human

Argininosuccinate Synthase 1 Human Recombinant

Recombinant Human ASS1, synthesized in E. coli, is a single, non-glycosylated polypeptide chain comprising 432 amino acids (specifically, amino acids 1 to 412). It possesses a molecular weight of 48.6 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus of ASS1, followed by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23474
Source
Escherichia Coli.
Appearance
The product is provided as a sterile, colorless solution that has been filtered for clarity.

GGPS1 Human

Geranylgeranyl Diphosphate Synthase 1 Human Recombinant

Recombinant Human GGPS1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 320 amino acids, with a sequence spanning from 1 to 300 a.a., and has a molecular weight of 37 kDa. The GGPS1 protein is fused to a 20 amino acid His-Tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23943
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

HMBS Human

Hydroxymethylbilane Synthase Human Recombinant

Recombinant human HMBS, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 385 amino acids (residues 1-361) and possessing a molecular weight of 41.9 kDa. This protein is expressed with an N-terminal 24-amino acid His-tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24022
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

HMGCS1 Human

3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 Human Recombinant

Recombinant human HMGCS1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 543 amino acids (residues 1-520) with a molecular weight of 59.7 kDa. The protein includes an N-terminal His-tag of 23 amino acids and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24123
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

HPGDS Human

Hematopoietic Prostaglandin D Synthase Human Recombinant

Recombinant human HPGDS, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 25.9 kDa. It consists of 223 amino acids, comprising the HPGDS sequence (amino acids 1-199) and a 24 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24190
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PTGDS Human

Prostaglandin D2 Synthase Human Recombinant

The PTGDS produced in E. coli is a single polypeptide chain that lacks glycosylation. It comprises 189 amino acids (specifically, amino acids 23 to 190) and has a molecular weight of 20.9 kDa. The protein includes a 21 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT24615
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PTGES2 Human

Prostaglandin E Synthase 2 Human Recombinant

The PTGES2 protein produced in E. coli is a single, non-glycosylated polypeptide chain. It consists of 206 amino acids, with 186 amino acids forming the active protein (1-186 a.a.), and has a molecular weight of 23.5 kDa. A 20 amino acid His-tag is fused to the N-terminus of PTGES2 to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24681
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.
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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