L1294
Lactoferrin human
recombinant, expressed in rice, Iron saturated, ≥90% (SDS-PAGE)
Synonyme(s) :
Holo Transferrin
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About This Item
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in rice
Type
for cell culture
Pureté
≥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)
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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)
Certificats d'analyse (COA)
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Les clients ont également consulté
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
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
Xinyuan Lai et al.
iScience, 25(4), 104136-104136 (2022-03-29)
The global pandemic of COVID-19 caused by the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection confers great threat to public health. Human breast milk is a complex nutritional composition to nourish infants and protect them from different kinds of infectious
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
Uxía Regueiro et al.
International journal of molecular sciences, 23(20) (2022-10-28)
Keratoconus (KC) is a corneal disorder whose etiology shares a close relationship with Lactoferrin (LTF) dysregulation and Toll-like Receptors 2 (TLR2) overexpression. This study shows how these two important biomarkers are clinically and molecularly interrelated, increasing knowledge about KC pathophysiology
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