LTF Holo Human
Greater than 95% as determined by SDS-PAGE.
Description
Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.
The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.
Product Specs
Recombinant Human Holo Lactoferrin, produced in plants, is a glycosylated polypeptide with a molecular weight of approximately 80 kDa. Purification is achieved through proprietary chromatographic techniques.
The lyophilization process of Human Holo Lactoferrin is carried out without any additional additives.
While Recombinant Holo Lactoferrin remains stable at room temperature for up to 5 days, it is recommended to store it in a desiccated state below -18°C. Frequent freeze-thaw cycles should be avoided.
For reconstitution, dissolve the lyophilized LTF Holo Human in sterile water at a concentration of 10mg/ml. This solution can be further diluted with other aqueous solutions as needed.
SDS-PAGE analysis confirms a purity exceeding 95%.
Product Science Overview
Lactoferrin is a multifunctional glycoprotein that plays a crucial role in the immune system. It is predominantly found in mammalian milk, but also in other bodily fluids such as saliva, tears, and mucous secretions. Lactoferrin has a high affinity for iron, which allows it to sequester iron from pathogens, thereby inhibiting their growth. The recombinant form of lactoferrin, particularly the holo form (iron-saturated), has garnered significant interest due to its potential applications in biotechnology and medicine.
Lactoferrin consists of a single polypeptide chain folded into two lobes, each capable of binding one ferric iron ion. This iron-binding capability is central to its antimicrobial properties, as it deprives bacteria of the iron necessary for their growth. Additionally, lactoferrin can permeabilize bacterial cell walls and inhibit viral infections by binding to viral envelope proteins .
Recombinant human lactoferrin (rhLF) is produced using various expression systems, including yeast, rice, and other plant-based systems. These systems offer a safe and cost-effective alternative to animal-derived lactoferrin, reducing the risk of contamination by pathogens . The production process involves the expression of the lactoferrin gene in the host organism, followed by purification and iron saturation to produce holo-lactoferrin.
To prepare holo-rhLF, partially iron-saturated lactoferrin (pis-rhLF) is mixed with a ferric nitrate solution at a specific molar ratio. The mixture is then concentrated and desalted to remove any excess unbound iron . Another method involves dialyzing apo-lactoferrin (iron-free) against a buffer containing ferric ammonium citrate and bicarbonate, followed by further dialysis to remove excess iron .
Recombinant holo-lactoferrin has shown promise in various applications:
- Cell Culture Media: It enhances cell growth and protects cells from apoptosis, making it a valuable supplement for cell culture media .
- Antimicrobial Agent: Its ability to sequester iron and disrupt bacterial cell walls makes it an effective antimicrobial agent .
- Immunomodulation: Lactoferrin can stimulate the release of interleukin-8 and other cytokines, enhancing the immune response .
- Therapeutic Potential: Recombinant lactoferrin has been investigated for its potential in treating infections, inflammation, and even cancer .
