Thrombin Human, HEK

Thrombin Human Recombinant, HEK
Cat. No.
BT30133
Source
HEK
Synonyms
Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.
Appearance
Sterile Filtered colorless solution.
Purity
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
Quick Inquiry

Description

Recombinant Human Thrombin produced in HEK cells, having a total molecular weight of 36kDa.
The Thrombin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Thrombin, also known as activated Factor IIa, is a crucial enzyme in the coagulation cascade. It acts as a serine protease (EC 3.4.21.5) that converts soluble fibrinogen into insoluble fibrin strands, which are essential for blood clot formation. Thrombin's role in coagulation involves the activation of various clotting factors, including Factor XI, Factor V, Factor VIII, and Factor XIII. Moreover, thrombin plays a role in platelet activation by interacting with protease-activated receptors on the platelet surface. Thrombin's high specificity for its cleavage site (Leu-Val-Pro-Arg-Gly-Ser) has made it a valuable tool in biotechnology. This specific sequence is commonly engineered into linker regions of recombinant fusion proteins. After protein purification, thrombin is used to cleave the linker at the arginine-glycine bond, separating the target protein from the purification tag with high precision.
Description
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.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The Thrombin is supplied in a solution containing 20mM MES buffer at pH 6.0 and 500mM Choline Chloride.
Stability
For long-term storage, it is recommended to keep the Thrombin frozen at temperatures between -20°C and -80°C. Repeated freezing and thawing should be avoided to maintain protein integrity.
Assay Conditions
The activity of Thrombin was assessed at a concentration of 1nM. The assay was performed at 25°C using SPECTROZYME TH (20 µM) as the substrate in a buffer composed of 5mM Tris-HCl (pH 8.0), 0.1% PEG, and 200mM NaCl.
Biological Activity
The biological activity of this Thrombin is 5396 NIH Units per mg. This activity was determined by comparison to a standard human plasma thrombin from Sigma. The protein concentration was measured using an extinction coefficient (E0.1%) of 1.83 at 280 nm.
Synonyms
Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.
Source
HEK

Product Science Overview

Introduction

Thrombin is a serine protease enzyme that plays a crucial role in the blood coagulation process. It is derived from prothrombin, a glycoprotein produced in the liver. Thrombin’s primary function is to convert fibrinogen into fibrin, leading to blood clot formation. The recombinant form of thrombin, expressed in Human Embryonic Kidney (HEK) 293 cells, is widely used in research and therapeutic applications due to its high purity and activity.

Production in HEK 293 Cells

HEK 293 cells are immortalized human embryonic kidney cells that are commonly used for protein production. These cells are robust, fast-growing, and easy to maintain, making them ideal for producing recombinant proteins. The recombinant human thrombin produced in HEK 293 cells is a glycoprotein heterodimer, consisting of a heavy chain (31 kDa) and a light chain (6 kDa) joined by a disulfide bond .

Structure and Function

Thrombin is composed of two chains: the A chain (light chain) and the B chain (heavy chain). The enzyme selectively cleaves the Arg-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B . The predominant form of thrombin in vivo is the zymogen prothrombin (factor II), which is activated by factor Xa in the presence of factor Va, calcium ions, and phospholipids .

Applications

Recombinant thrombin is used in various applications, including:

  • Hemostasis: Thrombin is used to promote blood clotting in surgical procedures and to control bleeding in patients with coagulation disorders.
  • Protein Cleavage: Thrombin is employed for site-specific cleavage of recombinant fusion proteins containing a thrombin recognition site, facilitating the removal of affinity tags .
  • Research: Thrombin is used in studies to assess hemostatic properties and to investigate the mechanisms of blood coagulation .
Advantages of Recombinant Thrombin

The use of recombinant thrombin expressed in HEK 293 cells offers several advantages:

  • High Purity: The recombinant form is highly purified, reducing the risk of contamination with other proteins or pathogens.
  • Consistency: Recombinant production ensures batch-to-batch consistency in terms of activity and quality.
  • Ethical Considerations: Using recombinant thrombin eliminates the need for animal-derived products, aligning with ethical standards in research and therapeutic applications.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

Related Products

Thrombin
Human Thrombin
Cat. No.
BT29957
Source
Human Plasma.
Thrombin Bovine
Bovine Thrombin
Cat. No.
BT30005
Source
Bovine Blood.
Thrombin Human
Thrombin Human Recombinant
Cat. No.
BT30088
Source
Escherichia Coli.
Thrombin Porcine
Porcine Thrombin
Cat. No.
BT30195
Source
Porcine Blood.
THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.