Transferrin

11 Results Found

Purified Rat Transferrin

Product is the lyophilized powder of rat transferrin and buffer salts

Purified Human Transferrin

Product is the lyophilized powder of human transferrin and buffer salts. ransferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains. The N-terminal and C-terminal domains of this protein are globular moieties of about 330 amino acids. Each of these domains is divided into two sub-domains, with the iron- and anion-binding sites found within the intersubdomain cleft. The binding cleft opens with iron release and closes with iron binding. Transferrin binds iron with an association constant of approximately 1022 M-1. Ferric iron couples to transferrin only in the presence of an anion (usually carbonate) that serves as a bridging ligand between metal and protein, excluding water from the two coordination sites. Without the anion cofactor, iron binding to transferrin is negligible. In the presence of anions, ferric transferrin is resistant to all but the most potent chelators. The remaining four coordination sites are provided by the transferrin protein - a histidine nitrogen, an aspartic acid carboxylate oxygen, and two tyrosine phenolate oxygens. Available evidence suggests that anion-binding takes place prior to iron-binding. Iron release from transferrin involves protonation of the carbonate anion, loosening the metal-protein bond.

Human Transferrin Iron Poor (APO)

Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains.

Human Transferrin Iron Saturated

Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains.

Lactoferrin

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.

Lactoferrin

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.

Lactoferrin

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.

Purified Human Lactoferrin

Product is the lyophilized powder of human lactoferrin and buffer salts. Human lactoferrin is purified from pooled human colostrum using multi-step procedures which may include salt fractionation, gel filtration, ion-exchange chromatography and immunoabsorption.

Purified Mouse Transferrin

Product is the lyophilized powder of mouse transferrin and buffer salts. Mouse transferrin is purified from pooled mouse serum using multi-step procedures which may include salt fractionation, gel filtration, ion-exchange chromatography and immunoabsorption.

BOVINE TRANSFERRIN (APO)

Bovine Transferrin is an iron-depleted product supplied as a heat-treated, lyophilised powder.

BOVINE TRANSFERRIN (HOLO)

Bovine Transferrin is chromatographically purified from New Zealand-sourced bovine plasma in an ISO quality system assuring complete traceability and consistent high quality. Transferrin (HOLO) is an iron-rich product supplied as a heat-treated, lyophilised powder.

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