L1294
Lactoferrin human
recombinant, expressed in rice, Iron saturated, ≥90% (SDS-PAGE)
Synonyme(s) :
Holo Transferrin
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in rice
Type
for cell culture
Essai
≥90% (SDS-PAGE)
≥90% (biuret)
Forme
powder
Technique(s)
microbiological culture: suitable
Impuretés
≤10 EU/mg endotoxin
Numéro d'accès UniProt
Température de stockage
2-8°C
Informations sur le gène
human ... LTF(4057)
Vous recherchez des produits similaires ? Visite Guide de comparaison des produits
Application
Lactoferrin was used to grow Streptococcus mutans in an iron-limiting medium. It was used to test if lactoferrin impedes epithelial cell adhesion in vitro.
Actions biochimiques/physiologiques
Lactoferrin is an iron binding protein. It is structurally similar to transferrin, the plasma iron transport protein; but lactoferrin has a much higher affinity for iron (250 fold). It is very abundant in colostrum and small amounts can also be found in tears, saliva, mucous secretions and in the secondary granules of neutrophils. It is made by mucosal epithelium and neutrophils and is released by these cells in response to inflammatory stimuli. Bacterial growth is inhibited by its ability to sequester iron and also permeabilize bacterial cell walls by binding to lipopolysaccharides through its N-terminus. Lactoferrin can inhibit viral infection by binding tightly to the viral envelope protein. This prevents cell-virus fusion by blocking the binding domain. Lactoferrin appears to activate host defense systems in part by stimulating the release of interleukin-8, a neutrophil activator. It may also be involved in antibody and interleukin synthesis, lymphocyte proliferation and complement activation.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Faites votre choix parmi les versions les plus récentes :
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Les clients ont également consulté
N Huang et al.
In vitro cellular & developmental biology. Animal, 44(10), 464-471 (2008-09-20)
Today there is a concern about the use of animal source proteins and peptides in cell culture applications due to potential contamination by adventitious infectious pathogens. Recombinant production of these proteins using a plant host provides a safe and cost
Erwann Rousseau et al.
Molecular pharmacology, 84(6), 888-898 (2013-10-01)
Previous studies on postmortem human brain tissue have shown that the iron-binding glycoprotein lactoferrin is upregulated in dopamine (DA) neurons resistant to degeneration in Parkinson disease (PD). To study how this could possibly relate to disease progression, we used midbrain
Ling Tang et al.
Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 18(1), 123-131 (2010-01-20)
Human lactoferrin (hLF), a glycoprotein of the transferrin family, has recently been shown to stimulate wound repair through its antimicrobial effect and inflammation modulation. A recent study with several non-skin cell lines indicated that hLF may also have a stimulatory
Qingsheng Kong et al.
Molecular and cellular biochemistry, 406(1-2), 293-299 (2015-05-20)
The metalloprotease lethal factor (LF) from Bacillus anthracis plays a vital role in anthrax toxin action, and thus becomes a target for anti-anthrax therapy. Following the guidelines based on existing metalloprotease inhibitors, we designed a 'first-generation' LF inhibitor R9LF-1. This
Esmat Aly et al.
Food research international (Ottawa, Ont.), 118, 101-107 (2019-03-23)
This study aimed to evaluate the potential anti-inflammatory role of the most produced form of lactoferrin expressed in various expression systems (Fe-saturated recombinant human Lf, rhLf) and its hydrolysate in concentrations resembles that found in mature human milk. Co-culture model
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique