GPBB Human

Glycogen Phosphorylase Human Recombinant

Glycogen Phosphorylase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain. The Human GPBB mature chain: 2 - 843 aa; that is a total of 842 aa having a molecular mass of 96695.96 Dalton. The theoretical pI is 6.40.
The GPBB is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2208
Source
Escherichia Coli.
Appearance
Sterile Filtered colourless liquid formualtion.

PNP Human

Purine Nucleoside Phosphorylase Human Recombinant

PNP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 309 amino acids (1-289 a.a.) and having a molecular mass of 34.2kDa. The PNP is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2309
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PYGL Human

Phosphorylase, Glycogen, Liver Human Recombinant

PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.
PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2376
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

TYMP Human

Thymidine Phosphorylase Human Recombinant

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

UGP2 Human

UDP-Glucose Pyrophosphorylase 2 Human Recombinant

UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.
UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2497
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

UPP1 E.coli

Uridine Phosphorylase E.coli Recombinant

UPP1 E.Coli Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2570
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

UPP1 Human

Uridine Phosphorylase 1 Human Recombinant

UPP1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310) and having a molecular mass of 29.3 kDa.
UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2644
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

UPP1 Salmonella

Uridine Phosphorylase Salmonella Typhimurium Recombinant

Uridine phosphorylase Salmonella typhimurium Recombinantproduced in E.Coli is a non-glycosylated, polypeptide having a total molecular mass of 163068 Dalton.
Shipped with Ice Packs
Cat. No.
BT2701
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.
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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