Thrombin Porcine

Porcine Thrombin
Cat. No.
BT30195
Source
Porcine Blood.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Product Specs

Introduction
Thrombin enzyme (Activated Factor IIa) is a crucial clotting promoter responsible for converting soluble fibrinogen into insoluble, active fibrin strands. As a coagulation protein and serine protease (EC 3.4.21.5), thrombin catalyzes numerous coagulation-related reactions, including the activation of factors XI, V, XIII, and VIII. It also promotes platelet activation by engaging protease-activated receptors on platelets. Due to its high proteolytic specificity, thrombin is a significant biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely employed in linker regions within recombinant fusion protein constructs. Following fusion protein purification, thrombin cleaves between the Arginine and Glycine residues of this site, effectively and specifically removing the purification tag from the target protein.
Physical Appearance
Sterile filtered white lyophilized powder.
Formulation
Lyophilized Powder from glycine, calcium chloride pH 7.0 containing 0.9% NaCl.
Solubility
Reconstitute the lyophilized porcine Thrombin in sterile 0.9% NaCl.
Stability
Lyophilized Porcine Thrombin remains stable at room temperature for 3 weeks but should be stored desiccated below -18°C. After reconstitution, store IPF1 at 4°C for 2-7 days. For future use, store below -18°C. For long-term storage, add a carrier protein (0.1% HSA or BSA). Avoid freeze-thaw cycles.
Source
Porcine Blood.

Product Science Overview

Discovery and Historical Context

Thrombin was first discovered in the late 19th century by a physiologist in Scotland. The enzyme was purified and sequenced in 1951, which significantly advanced the understanding of its structure and function . Since then, thrombin has been widely studied and applied in clinical settings due to its prominent hemostatic properties.

Extraction and Purification

Porcine thrombin is typically extracted from fresh porcine blood using methods such as isoelectric precipitation and ammonium sulfate fractionation. The crude thrombin solution is then activated with a calcium solution and purified through chromatographic techniques, such as using a cellulose DEAE-52 column . The purified thrombin is often freeze-dried to obtain a white, pure form of the enzyme with high specific activity.

Applications

Porcine thrombin is widely used in medical and clinical settings as a hemostatic agent. It is particularly effective in controlling local bleeding from capillaries and small blood vessels, making it valuable in trauma care, surgery, and various medical procedures involving the oral cavity, ear-nose-throat, urinary, and alimentary canals . Thrombin can be applied directly to wounds in powder or solution form to control bleeding and promote clot formation. It is also used in combination with other drugs to create new dosage forms and as a raw material for various topical hemostatic agents.

Advantages and Safety

One of the significant advantages of using porcine thrombin is its safety and convenience. It has no obvious adverse effects even when used in high doses or over extended periods. Unlike some other hemostatic agents, porcine thrombin does not induce antigenicity or allergic reactions when applied topically or orally . This makes it a preferred choice for many medical applications.

Market Value and Environmental Impact

China is one of the leading producers of porcine blood, generating approximately 1 billion kilograms annually . However, much of this blood is often discarded as waste, leading to environmental pollution. By extracting thrombin from porcine blood, valuable biological resources can be utilized more efficiently, creating significant market value and reducing environmental impact .

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