Transferrin Human

Transferrin Human Recombinant
Cat. No.
BT30413
Source
Oryza sativa (rice).
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Purity

Purity as determined by SDS-PAGE is 97%.

Usage
Prospec'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

Recombinant Human Transferrin produced in Plant is a non-glycosylated, polypeptide chain containing 679 amino acids and having a molecular mass of 76 kDa.
The Recombinant Human Transferrin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Transferrin, the iron-transport protein found in vertebrate serum, delivers iron to cells by interacting with a specific membrane receptor known as CD71. This protein appears to be crucial for the growth of most cells in tissue culture. Often referred to as a growth factor, transferrin exhibits similarities to other growth factor-receptor interactions. Proliferating cells display a high number of transferrin receptors, and the binding of transferrin to these receptors is essential for cells to initiate and sustain DNA synthesis. Beyond its role in iron transport, transferrin also functions as a cytokine, exhibiting activities that may not directly relate to its iron-carrying capacity.
Description
Recombinant Human Transferrin, produced in a plant-based expression system, is a non-glycosylated polypeptide chain consisting of 679 amino acids. It has a molecular mass of 76 kDa. The purification of Recombinant Human Transferrin is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Formulation
The protein was lyophilized without any additives to a concentration of 1mg/ml.
Solubility
To prepare stock solutions, gently dissolve the lyophilized powder in PBS. Allow for several minutes of gentle mixing. Recommended stock concentrations range from 5mg/ml to 20 mg/ml in PBS, although other concentrations may be suitable. Avoid introducing bubbles while dissolving the protein. Sterilize the solution by filtering it through a 0.2µm filter.
Stability
Lyophilized Transferrin remains stable at room temperature for up to 3 weeks. However, it is recommended to store it desiccated below -18°C. After reconstitution, Recombinant Human Transferrin should be stored at 4°C for 2-7 days. For long-term storage, it is advisable to store it below -18°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity

The purity, as determined by SDS-PAGE analysis, is 97%.

Iron Content

The average Ferric Iron content in our Transferrin product is 0.4-0.5µg per mg of protein. The protein concentration is measured by absorbance at 280 nm.

Biological Activity

One mg of Recombinant Human Transferrin has the capacity to bind to approximately 2 micrograms of iron (Fe).

Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Source
Oryza sativa (rice).

Product Science Overview

Structure and Function

Human transferrin is a bilobal glycoprotein with a molecular weight of approximately 76.5 kDa . It consists of two homologous domains, each capable of binding one ferric ion (Fe3+). This ability to reversibly bind iron with high affinity makes transferrin a key player in iron homeostasis. The protein is produced in the liver and circulates in the blood plasma at a concentration of about 2.5 mg/mL .

Mechanism of Iron Transport

Transferrin binds iron in the bloodstream and delivers it to cells via the transferrin receptor (TFR) on the cell surface. At physiological pH (7.4), transferrin with bound iron (holo-transferrin) has the highest affinity for TFR . The transferrin-receptor complex is internalized through clathrin-mediated endocytosis, and the acidic environment of the endosome triggers the release of iron from transferrin. The iron-free transferrin (apo-transferrin) is then recycled back to the cell surface to bind more iron .

Recombinant Production

The production of recombinant human transferrin involves the use of advanced genetic engineering techniques. Initially, prokaryotic and simple eukaryotic expression systems were used, but these approaches faced challenges such as low expression levels and nonfunctional protein production . More complex eukaryotic systems, such as Baby Hamster Kidney (BHK) cells, have been employed to overcome these issues and produce functional recombinant transferrin .

Recombinant human transferrin is typically produced in HEK293 cells, which are human embryonic kidney cells. The recombinant protein is purified to ensure high purity and functionality. It is often used in cell culture media to support cell growth and proliferation, especially in serum-free conditions .

Applications

Recombinant human transferrin has several important applications:

  1. Cell Culture: It is a critical component of serum-free cell culture media, providing essential iron for cell growth and proliferation .
  2. Research: It is used in various biochemical and biophysical studies to understand iron metabolism and related disorders.
  3. Therapeutics: Recombinant transferrin is being explored for therapeutic applications, including the treatment of iron deficiency and anemia.

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