Transferrin

Bovine Transferrin Iron Saturated (Holo) (Heat Treated)

Bovine Transferrin Iron Saturated (Holo) (Heat Treated)

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.

Bovine Transferrin Iron Poor (Apo) (Heat Treated)

Bovine Transferrin Iron Poor (Apo) (Heat Treated)

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

Purified rat transferrin, 5 mg

Purified rat transferrin, 5 mg

0855953

Product is the lyophilized powder of rat transferrin and buffer salts

Purified mouse transferrin, 10 mg

Purified mouse transferrin, 10 mg

0855943

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.

Purified human lactoferrin, 10 mg

Purified human lactoferrin, 10 mg

0855839

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.

Lactoferrin

Lactoferrin

0215233380

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

0215233350

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

0215233310

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.

Human transferrin, iron saturated, 1 g

Human transferrin, iron saturated, 1 g

08823431

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

Human transferrin, iron poor (apo), 1 g

Human transferrin, iron poor (apo), 1 g

08823411

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

Purified human transferrin, 10 mg

Purified human transferrin, 10 mg

0855915

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.

11 Items