Glucagon Human

Glucagon Human Recombinant
Cat. No.
BT14415
Source
Escherichia Coli.
Synonyms
GLP1, GLP2, GRPP.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek'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

Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton.
The Glucagon is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glucagon is a crucial hormone that plays a vital role in regulating carbohydrate metabolism. Produced and secreted by alpha cells within the islets of Langerhans in the pancreas, glucagon is released in response to low blood glucose levels (hypoglycemia). Its primary function is to stimulate the liver to break down stored glycogen into glucose, which is then released into the bloodstream, effectively raising blood glucose levels. This action counteracts the effects of insulin, which lowers blood glucose levels by promoting glucose uptake by cells. Glucagon is also employed in cell culture applications, particularly in studies investigating glycogenolysis in hepatocytes. Moreover, it has demonstrated the ability to induce DNA replication in primary cultures of adult rat hepatocytes when used in conjunction with EGF and insulin. Glucagon's effects extend to relaxing smooth muscles, such as those found in the gastrointestinal tract.
Description
Recombinant Human Glucagon, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 29 amino acids. With a molecular weight of 3483 Daltons, it is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Each milligram of recombinant Glucagon is formulated with 100 milligrams of lactose.
Solubility
To reconstitute the lyophilized Glucagon, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of not less than 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Glucagon remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it at 4°C. The addition of a carrier protein, such as 0.1% HSA or BSA, is also recommended for extended storage.
Purity
The purity of this product is greater than 98.0% as determined by: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis. (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of this product is determined by comparing its hyperglycemic effect to that of an international standard or a reference preparation calibrated in International Units (IU). The activity is found to be 1 IU/mg.
Synonyms
GLP1, GLP2, GRPP.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.

Product Science Overview

Structure and Production

Glucagon is a 29-amino acid polypeptide with the primary structure: NH₂-His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-COOH. It has a molecular mass of 3485 daltons . The hormone is synthesized and secreted from the alpha cells (α-cells) of the islets of Langerhans in the pancreas. It is produced from the preproglucagon gene (Gcg), which is first processed to form proglucagon and then cleaved to produce glucagon .

Mechanism of Action

Glucagon raises blood sugar levels by activating hepatic glucagon receptors, which stimulate glycogenolysis and the release of glucose. This process involves the activation of adenylate cyclase, increasing intracellular cyclic AMP and activating protein kinase A. This, in turn, leads to the breakdown of glycogen into glucose .

Medical Uses

Recombinant glucagon is used as a medication to treat severe hypoglycemia, particularly in patients with diabetes mellitus. It is also employed as a diagnostic aid in radiologic exams to temporarily inhibit the movement of the gastrointestinal tract . The recombinant form of glucagon is identical to the naturally occurring hormone and is produced using recombinant DNA technology.

Historical Context

Glucagon was first granted FDA approval on November 14, 1960 . Since then, it has become an essential tool in the management of hypoglycemia and in various diagnostic procedures. The recombinant form of glucagon has further enhanced its availability and utility in clinical settings.

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