Thrombin Human

Thrombin Human Recombinant

Recombinant human thrombin, produced in E. coli, is a single-chain polypeptide that is not glycosylated. It comprises 296 amino acids (spanning positions 328 to 622 of the full-length protein) and has a molecular weight of 33.9 kDa.
Shipped with Ice Packs
Cat. No.
BT30088
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

Thrombin Human, HEK

Thrombin Human Recombinant, HEK

This product is a recombinant form of human Thrombin, produced in HEK cells. It has a molecular weight of 36kDa and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT30133
Source
HEK
Appearance
A clear, colorless solution that has been sterilized by filtration.

Thrombin Porcine

Porcine Thrombin

Shipped with Ice Packs
Cat. No.
BT30195
Source
Porcine Blood.
Appearance
Sterile filtered white lyophilized powder.

THBD Human

Thrombomodulin Human Recombinant

Recombinant human THBD, expressed in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein consists of 500 amino acids (residues 22-515) with an approximate molecular weight of 52.6 kDa. For purification purposes, a 6-amino acid Histidine tag is fused to the C-terminus. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT29862
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

Thrombin

Human Thrombin

Thrombin was extracted and purified from human plasma.
Shipped with Ice Packs
Cat. No.
BT29957
Source
Human Plasma.
Appearance
The product is provided as a sterile, filtered liquid solution.

Thrombin Bovine

Bovine Thrombin

Shipped with Ice Packs
Cat. No.
BT30005
Source
Bovine Blood.
Appearance

Sterile Filtered, lyophilized powder with a beige color.

Definition and Classification

Thrombin, also known as coagulation factor IIa, is a serine protease that plays a crucial role in the blood coagulation process. It is derived from its inactive precursor, prothrombin, through enzymatic cleavage by the prothrombinase complex . Thrombin is classified as a serine protease due to its mechanism of action involving a serine residue at its active site .

Biological Properties

Key Biological Properties: Thrombin is a Na±activated, allosteric enzyme that exists in multiple forms, including E*, E, and E:Na+, which interconvert based on ligand binding . It is involved in various physiological processes, including blood coagulation, cell-mediated immunity, and cell death .

Expression Patterns and Tissue Distribution: Thrombin is produced in the liver and is present in the blood as an inactive precursor, prothrombin . It is abundantly expressed in all arterial vessel wall constituents, including endothelial cells, smooth muscle cells, and leukocytes .

Biological Functions

Primary Biological Functions: Thrombin’s primary function is to convert fibrinogen into fibrin, forming a blood clot . It also activates other coagulation factors, including factors V, VIII, XI, and XIII . Additionally, thrombin plays a role in platelet activation and aggregation .

Role in Immune Responses and Pathogen Recognition: Thrombin is involved in immune responses by promoting leukocyte recruitment into atherosclerotic plaques and enhancing oxidative stress . It also plays a role in inflammation and angiogenesis .

Modes of Action

Mechanisms with Other Molecules and Cells: Thrombin interacts with various molecules and cells through its specific cell membrane receptors, known as protease-activated receptors (PARs), including PAR-1, PAR-3, and PAR-4 . These interactions lead to various cellular responses, including inflammation, cell migration, and proliferation .

Binding Partners and Downstream Signaling Cascades: Thrombin binds to fibrinogen, thrombomodulin, and other coagulation factors through its anion-binding exosites . These interactions trigger downstream signaling cascades that regulate coagulation, inflammation, and cell proliferation .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Thrombin activity is regulated by the prothrombinase complex, which includes activated Factor X (Xa) and Factor V (Va) . The presence of calcium ions and phospholipid bilayers also enhances thrombin activity .

Transcriptional Regulation and Post-Translational Modifications: Thrombin is co-translationally modified in a vitamin K-dependent reaction that converts glutamic acids to gamma-carboxyglutamic acid . This modification is essential for its binding to phospholipid surfaces .

Applications

Biomedical Research: Thrombin is extensively studied for its role in coagulation and its potential therapeutic applications . It is used in various research models to understand coagulation disorders and develop anticoagulant therapies .

Diagnostic Tools: Thrombin generation assays are used to assess coagulation status in patients with bleeding disorders or thrombotic conditions .

Therapeutic Strategies: Thrombin inhibitors, such as dabigatran, are used as anticoagulant therapies to prevent and treat thromboembolic disorders .

Role in the Life Cycle

Role Throughout the Life Cycle: Thrombin plays a vital role in hemostasis from birth to aging . Newborns have lower levels of thrombin activity, which gradually increase to adult levels . Thrombin is also involved in wound healing, tissue repair, and the progression of cardiovascular diseases .

© Copyright 2024 Thebiotek. All Rights Reserved.