INSR Human

Insulin Receptor Human Recombinant

Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.
The Human INSR is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18945
Source
HEK 293.
Appearance
Filtered White lyophilized (freeze-dried) powder.

Insulin Human

Insulin Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT19030
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Insulin Human, His

Insulin Human Recombinant, His Tag

Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT19124
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ProInsulin Human

ProInsulin C-Peptide Analogue Human Recombinant

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.
ProInsulin is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT19221
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Definition and Classification

Insulin is a peptide hormone produced by the beta cells of the pancreatic islets. It plays a crucial role in regulating blood glucose levels by facilitating the uptake of glucose into cells. Insulin is composed of two polypeptide chains, an A chain and a B chain, linked by disulfide bridges . It is classified based on its action duration into rapid-acting, short-acting, intermediate-acting, and long-acting types .

Biological Properties

Key Biological Properties: Insulin is a protein hormone with anabolic properties, promoting the synthesis of glycogen, fats, and proteins . It is derived from a precursor molecule called proinsulin, which is cleaved to form active insulin and C-peptide .

Expression Patterns and Tissue Distribution: Insulin is primarily produced in the beta cells of the islets of Langerhans in the pancreas . It is secreted in response to elevated blood glucose levels, such as after a meal .

Biological Functions

Primary Biological Functions: Insulin regulates the metabolism of carbohydrates, fats, and proteins by promoting the absorption of glucose from the blood into liver, fat, and skeletal muscle cells . It also inhibits the production of glucose by the liver .

Role in Immune Responses and Pathogen Recognition: While insulin’s primary role is metabolic regulation, it indirectly influences immune responses by maintaining glucose homeostasis, which is crucial for the proper functioning of immune cells .

Modes of Action

Mechanisms with Other Molecules and Cells: Insulin binds to specific receptors on the surface of target cells, triggering a cascade of intracellular events that facilitate glucose uptake . This binding activates the insulin receptor, which has intrinsic tyrosine kinase activity, leading to the phosphorylation of insulin receptor substrates (IRS) and subsequent activation of downstream signaling pathways .

Binding Partners and Downstream Signaling Cascades: The primary binding partner of insulin is the insulin receptor. Upon binding, the receptor undergoes autophosphorylation and activates several signaling pathways, including the PI3K-Akt pathway, which promotes glucose uptake and glycogen synthesis .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Insulin expression is regulated at both transcriptional and translational levels. Key transcription factors such as Pdx1, NeuroD, and MafA bind to regulatory sequences in the insulin gene promoter to modulate its transcription . Post-translational modifications, such as phosphorylation, also play a role in regulating insulin activity .

Transcriptional Regulation and Post-Translational Modifications: The insulin gene contains several regulatory elements that respond to glucose levels and other stimuli. Post-translational modifications, including phosphorylation and glycosylation, can affect insulin’s stability and activity .

Applications

Biomedical Research: Insulin is extensively studied in diabetes research to understand its role in glucose metabolism and develop new therapeutic strategies .

Diagnostic Tools: Insulin levels are measured to diagnose and monitor diabetes and other metabolic disorders .

Therapeutic Strategies: Insulin therapy is a cornerstone in the management of diabetes mellitus. Advances in insulin formulations and delivery methods, such as insulin pumps and inhaled insulin, have improved glycemic control and patient compliance .

Role in the Life Cycle

Role Throughout the Life Cycle: Insulin plays a vital role from development to aging. During development, it is essential for growth and energy storage. In adulthood, it maintains metabolic homeostasis. Dysregulation of insulin signaling is associated with aging and age-related diseases, such as type 2 diabetes and metabolic syndrome .

From Development to Aging and Disease: Insulin’s role evolves throughout life, from promoting growth and development in early life to maintaining energy balance and metabolic health in adulthood. Insulin resistance and impaired insulin signaling are key features of aging and contribute to the development of metabolic diseases .

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