Insulin Human

Insulin Human Recombinant
Cat. No.
BT19030
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by RP-HPLC analysis.
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

Insulin Human Recombinant produced in E.Coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Insulin is a hormone that regulates blood sugar levels. It facilitates the entry of glucose into cells, thereby lowering blood glucose concentration. Additionally, insulin promotes the uptake of amino acids and fatty acids into cells. It also accelerates key metabolic processes such as glycolysis, the pentose phosphate pathway, and glycogen synthesis in the liver.
Description
Recombinant Human Insulin, produced in E. coli, is a non-glycosylated polypeptide composed of two chains. It consists of 51 amino acids and has a molecular weight of 5807 Daltons. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile white powder obtained by freeze-drying.
Formulation
The protein was freeze-dried from a solution containing 1mg/ml protein and no additional components.
Solubility
To reconstitute the lyophilized Insulin, it is recommended to dissolve it in sterile 0.005N HCl at a concentration not exceeding 1 mg/ml.
Stability
Lyophilized Insulin remains stable for up to 3 weeks at room temperature. However, for extended storage, it is recommended to store it desiccated below -18°C. Once reconstituted, Insulin should be stored at 4°C for a maximum of 2-7 days. For long-term storage after reconstitution, it is advisable to store it below -18°C. To ensure stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be higher than 98% based on RP-HPLC analysis.
Biological Activity
The measured biological activity is 28 units per milligram of protein.
Source
Escherichia Coli.

Product Science Overview

Introduction

Insulin is a crucial hormone for regulating blood glucose levels, and its deficiency or resistance leads to diabetes mellitus. The advent of recombinant DNA technology has revolutionized the production of human insulin, making it more accessible and effective for diabetes management.

Historical Context

Before the development of recombinant insulin, diabetes was managed using animal-derived insulin, primarily from pigs and cows. While effective, these insulins often caused allergic reactions and other side effects due to slight differences in amino acid sequences compared to human insulin .

Development of Recombinant Insulin

The breakthrough in recombinant insulin production came in the early 1980s. Eli Lilly and Company launched the first human insulin of recombinant DNA origin in 1982, followed by Novo Nordisk in 1988 . This development was made possible by inserting the human insulin gene into the genetic material of bacteria, such as Escherichia coli (E. coli), or yeast. These genetically modified microorganisms could then produce insulin identical to that produced by the human pancreas .

Production Process

The production of recombinant human insulin involves several critical steps:

  1. Gene Cloning: The human insulin gene is inserted into a plasmid vector, which is then introduced into a host microorganism like E. coli or yeast.
  2. Expression: The host microorganisms are cultured in large fermentation tanks, where they express the insulin protein.
  3. Purification: The insulin protein is extracted and purified through various techniques, including chromatography and crystallization .
  4. Formulation: The purified insulin is formulated into a stable, injectable form suitable for medical use .
Advantages of Recombinant Insulin

Recombinant insulin offers several advantages over animal-derived insulin:

  • Reduced Allergic Reactions: Being identical to human insulin, recombinant insulin minimizes the risk of allergic reactions.
  • Scalability: The production process can be scaled up to meet the growing demand for insulin worldwide.
  • Consistency: Recombinant insulin ensures a consistent and reliable supply, crucial for managing diabetes effectively .
Impact on Diabetes Management

The introduction of recombinant insulin has significantly improved the quality of life for people with diabetes. It has enabled better glycemic control, reduced complications, and provided more flexible treatment options. Additionally, the development of insulin analogs, which are modified forms of insulin with altered pharmacokinetic properties, has further enhanced diabetes management .

Future Prospects

The demand for insulin continues to rise, driven by the increasing prevalence of diabetes globally. Ongoing research aims to develop more efficient and cost-effective production methods, as well as new insulin analogs with improved therapeutic properties .

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