UPP1 E.coli

Uridine Phosphorylase E.coli Recombinant

Recombinant UPP1, derived from E. coli, is produced as a single, non-glycosylated polypeptide chain comprising 273 amino acids (residues 1-253) with a molecular weight of 29.3 kDa. The protein is expressed with a 20-amino acid His Tag fused at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT2570
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

UPP1 Human

Uridine Phosphorylase 1 Human Recombinant

Recombinant UPP1 protein, specifically the human variant, is produced in E.Coli. It exists as a single, non-glycosylated polypeptide chain composed of 330 amino acids (residues 1-310), resulting in a molecular weight of 29.3 kDa. This protein is engineered with a 20 amino acid His Tag at the N-terminus to facilitate purification, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2644
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

UPP1 Salmonella

Uridine Phosphorylase Salmonella Typhimurium Recombinant

Recombinant Uridine phosphorylase from Salmonella typhimurium, produced in E. coli, is a non-glycosylated polypeptide with a molecular weight of 163.068 kDa.
Shipped with Ice Packs
Cat. No.
BT2701
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.

GPBB Human

Glycogen Phosphorylase Human Recombinant

Glycogen Phosphorylase, Human Recombinant, produced in E. coli, is available as a single, non-glycosylated polypeptide chain. The mature human GPBB chain comprises amino acids 2 to 843, totaling 842 amino acids, with a molecular weight of 96,695.96 Daltons. The theoretical isoelectric point (pI) is 6.40. The purification of GPBB is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2208
Source
Escherichia Coli.
Appearance
Sterile, colorless liquid formulation.

PNP Human

Purine Nucleoside Phosphorylase Human Recombinant

Recombinant human PNP, expressed in E. coli, is a 34.2 kDa monomeric protein containing a 20 amino acid His-tag at the N-terminus. This non-glycosylated protein, spanning amino acids 1-289, is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2309
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

PYGL Human

Phosphorylase, Glycogen, Liver Human Recombinant

Recombinant human PYGL, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 879 amino acids (with a sequence spanning from amino acid position 1 to 847) and possessing a molecular weight of 100.7 kDa. For purification purposes, a 32 amino acid His-tag is attached to the N-terminus of the protein, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT2376
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TYMP Human

Thymidine Phosphorylase Human Recombinant

Recombinant human TYMP, fused with a 21 amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain contains 493 amino acids (11-482 a.a.) and has a molecular mass of 51.3 kDa. The TYMP protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2454
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

UGP2 Human

UDP-Glucose Pyrophosphorylase 2 Human Recombinant

Recombinant human UGP2, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a.) with a molecular mass of 59.3 kDa. It has a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2497
Source
Escherichia Coli.
Appearance
Sterile, colorless, and clear solution.
Definition and Classification

Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate to an acceptor molecule. This process is known as phosphorolysis. Phosphorylases are distinct from phosphatases, which remove phosphate groups, and kinases, which transfer phosphate groups from donor molecules like ATP . Phosphorylases are classified into several categories based on their substrate specificity:

  • Glycosyltransferases (EC 2.4): These enzymes break down glucans by removing a glucose residue. Examples include glycogen phosphorylase, starch phosphorylase, and maltodextrin phosphorylase.
  • Nucleotidyltransferases (EC 2.7.7): These enzymes have phosphorolytic 3’ to 5’ exoribonuclease activity. Examples include RNase PH and polynucleotide phosphorylase (PNPase) .
Biological Properties

Phosphorylases exhibit key biological properties, including their ability to catalyze the production of glucose-1-phosphate from glucans such as glycogen, starch, or maltodextrin . They are allosteric enzymes, meaning their activity can be regulated by molecules that bind to sites other than the active site. Phosphorylases are expressed in various tissues, with glycogen phosphorylase being present in the liver, muscle, and brain . The expression patterns and tissue distribution of phosphorylases are crucial for their role in energy metabolism and other cellular processes.

Biological Functions

The primary biological function of phosphorylases is to catalyze the breakdown of glycogen into glucose-1-phosphate, which is essential for maintaining blood glucose levels . In addition to their role in energy metabolism, phosphorylases are involved in immune responses and pathogen recognition. For example, polynucleotide phosphorylase (PNPase) plays a role in RNA metabolism and degradation, which is important for the immune response to viral infections .

Modes of Action

Phosphorylases interact with other molecules and cells through various mechanisms. Glycogen phosphorylase, for instance, binds to glycogen and catalyzes its breakdown into glucose-1-phosphate . This process involves the transfer of a phosphate group from an inorganic phosphate to the glycogen molecule. Phosphorylases also interact with other proteins and enzymes, forming complexes that regulate their activity and downstream signaling cascades .

Regulatory Mechanisms

The expression and activity of phosphorylases are regulated by several mechanisms, including transcriptional regulation and post-translational modifications. Phosphorylation is a key regulatory mechanism that controls the activity of glycogen phosphorylase. The enzyme exists in two forms: the active phosphorylase a and the less active phosphorylase b. Phosphorylase kinase phosphorylates phosphorylase b to convert it into the active form, while phosphoprotein phosphatase dephosphorylates phosphorylase a to convert it back to the less active form . Other regulatory mechanisms include allosteric regulation by molecules such as AMP, ATP, and glucose-6-phosphate .

Applications

Phosphorylases have various applications in biomedical research, diagnostic tools, and therapeutic strategies. In research, phosphorylases are used to study carbohydrate metabolism and energy production. They are also used in the synthesis of bioactive carbohydrates and glycosylated products . In diagnostics, phosphorylases can be used as biomarkers for certain diseases, such as glycogen storage diseases . Therapeutically, phosphorylases are being explored as targets for drug development, particularly in the treatment of metabolic disorders and cancer .

Role in the Life Cycle

Phosphorylases play a crucial role throughout the life cycle, from development to aging and disease. During development, phosphorylases are involved in the regulation of energy metabolism and cellular growth . In aging, changes in phosphorylase activity can affect metabolic processes and contribute to age-related diseases . In disease, mutations or dysregulation of phosphorylases can lead to metabolic disorders, such as glycogen storage diseases, and impact the immune response to infections .

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