GPBB Human

Glycogen Phosphorylase Human Recombinant
Cat. No.
BT2208
Source
Escherichia Coli.
Synonyms
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
Appearance
Sterile Filtered colourless liquid formualtion.
Purity
Greater than 85.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Glycogen phosphorylase, an enzyme categorized under phosphorylases (EC 2.4.1.1), plays a crucial role in glycogen breakdown. It facilitates the release of glucose subunits from glycogen molecules. During this process, glycogen loses a glucose molecule, which transforms into glucose-1-phosphate. For metabolic utilization, this glucose-1-phosphate needs conversion to glucose-6-phosphate, a step carried out by the enzyme phosphoglucomutase. The action of glycogen phosphorylase is limited to the linear chains of glycogen, specifically the α-1,4 glycosidic linkages. It encounters an obstacle four residues away from α-1,6 branch points, which are prevalent in glycogen. To overcome this, a debranching enzyme comes into play, straightening the chain in that region. Additionally, an α-1,6-glucosidase enzyme is required to cleave the remaining α-1,6 residue in the newly linearized chain. Once these steps are completed, glycogen phosphorylase can resume its activity. Insulin, a key hormone, stimulates the enzyme phosphoprotein phosphatase (PP-1), which in turn deactivates glycogen phosphorylase, thereby preventing glycogen breakdown. GPBB serves as a highly sensitive marker for diagnosing acute myocardial infarction (AMI) within 4 hours of chest pain onset. Studies have revealed elevated GPBB levels in a significant portion of AMI patients within 2-3 hours of experiencing chest pain. This elevation is also observed early on in patients with unstable angina. Furthermore, GPBB acts as a sensitive indicator for detecting perioperative myocardial ischemia and infarction in patients undergoing coronary artery bypass grafting.
Description
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.
Physical Appearance
Sterile, colorless liquid formulation.
Formulation
The protein concentration is 1 mg/mL, and the formulation contains 50% glycerol as a stabilizing agent.
Stability
While GPBB remains stable at 10°C for up to 7 days, storage at or below -18°C is recommended for long-term preservation. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of GPBB is greater than 85.0%, as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis. (b) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Applications
Glycogen Phosphorylase, Human Recombinant, is suitable for use in various applications, including: - Immunoassays - Western blot analysis
Synonyms
Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.
Source
Escherichia Coli.

Product Science Overview

Structure and Forms

Glycogen Phosphorylase exists in two main forms:

  1. Phosphorylase A: The active, phosphorylated form.
  2. Phosphorylase B: The inactive, unphosphorylated form.

Both forms exist as homodimers and are found in various tissues, including muscle, liver, and brain .

Function

The primary function of Glycogen Phosphorylase is to catalyze the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate. This reaction is essential for the mobilization of glucose from glycogen stores, especially during periods of fasting or intense physical activity .

Clinical Significance

Glycogen Phosphorylase has significant clinical applications:

  • Acute Myocardial Infarction (AMI): It serves as a sensitive marker for AMI diagnosis within 4 hours after the onset of chest pain. Elevated levels of Glycogen Phosphorylase isoform BB (GPBB) can be detected in a considerable proportion of AMI patients within 2-3 hours from chest pain onset .
  • Unstable Angina: GPBB levels are also increased early in patients with unstable angina .
  • Peri-operative Myocardial Ischemia: It can be used as a marker for detecting myocardial ischemia and infarction in patients undergoing coronary artery bypass grafting .
Recombinant Human Glycogen Phosphorylase

Recombinant Human Glycogen Phosphorylase is produced in E. coli and is a single, non-glycosylated polypeptide chain with a molecular mass of 97 kDa . This recombinant form is used in various research and diagnostic applications, including immunoassays and western blotting .

Mechanism

The enzyme breaks down glycogen into glucose subunits through the following reaction:

(α1,4 glycogen chain)n+Pi(α1,4 glycogen chain)n1+αDglucose-1-phosphate(\alpha-1,4 \text{ glycogen chain})_n + Pi \leftrightarrow (\alpha-1,4 \text{ glycogen chain})_{n-1} + \alpha-D-\text{glucose-1-phosphate}

This reaction leaves glycogen with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate .

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