LACTOFERRICIN B

ArtNr	20-321-175257
Hersteller	GENWAY
Menge	1ml
Kategorie	Oncology Antibodies Primary Antibodies By Organ Lung Cancer
Typ	Antibody
Clon	5F12. 1. 2
Specific against	other
ECLASS 10.1	32160702
ECLASS 11.0	32160702
UNSPSC	12352203
Alias	GWB-C768F7
Similar products	20-321-175257
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Genway ID:	GWB-C768F7
Clone:	5F12. 1. 2
Applications:	The monoclonal antibody 5F12. 1. 2 can be used for Western blotting and as detection in immuno assay. Monoclonal antibody clone 5F12. 1. 2. anti bovine Lactoferricin B is highly specific for bovine Lactoferricin B. This peptide is derived by enzymatic cleavage of lactoferrin which is a member of the transferrin family of metal-binding proteins found in milk and other secretory fluids and also in blood. Cleavage by pepsin of bovine lactoferrin leads to the release of Lactoferricin B (aminoacid 17-41). This peptide is highly basic. possessing five Arg (R) and three Lys (K) residues. In addition. a number of Trp (W) and Phe (F) aromatic residues are present. The two Cys (C) residues from lactoferricin B form a disulfide bond. generating an almost completely cyclical peptide. Nevertheless. the disulfide bond is not required for the antimicrobial potency. Several studies have shown that Lactoferricin B has a broad-spectrum activity against various Gram-positive and Gram-negative bacteria. In addition the peptide has been shown to have antifungal. antiviral and antitumour activity and to bind lipopolysaccharides (LPS. endotoxin). Moreover. it is known to stimulate the adaptive immune response and has anti-inflammatory properties. Lactoferricin B belongs to a large group of cationic antimicrobial peptides. The monoclonal antibody 5F12. 1. 2 is specific for bovine Lactoferricin B and detects the QWR antigenic determinant specific for bovine Lactoferricin B. it lacks reactivity with bovine lactoferrin C-lobe. human lactoferrin or lactoferricin H. The QWR sequence recognized by the antibody 5F12. 1. 2 is not present in lactoferrin in human. pig. mouse. goat. rabbit. horse. rat. cockroach and African clawed frog.
Function:	Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion usually bicarbonate.
Function:	Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E. coli and P. aeruginosa.
Function:	Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.
Function:	The lactotransferrin peptidase S60 domain 1 functions as a serine protease that cuts arginine rich regions. This function contributes to the antimicrobial activity.
Catalytic Activity:	Preferential at -Arg-Ser-Arg-Arg-\|- and -Arg-Arg-Ser-Arg-\|- and of Z-Phe-Arg-\|-aminomethylcoumarin.
Enzyme Regulation:	Inhibited by PMSF and Pefabloc. Biophysicochemical Properties:
Subunit:	Monomer.
Subcellular Location:	Secreted.
Miscellaneous:	The second peptidase S60 domain does not have protease function as the catalytic residues are missing.
Similarity:	Belongs to the transferrin family.
Similarity:	Contains 2 peptidase S60 domains [view classification]. [1] Pierce A. Colavizza D. Benaissa M. Maes P. Tartar A. Montreuil J. and Spik G. Molecular cloning and sequence analysis of bovine lactotransferrin[2] Goodman R. E. and Schanbacher F. L. et al. Bovine lactoferrin mRNA: sequence analysis and expression in the mammary gland[3] Tsang T. C. Burns D. K. Wang F. Pan Y. C. E. Schmidt A. M. and Stern D. Cloning of a 80-kD advanced glycosylation end product (AGE) binding protein from bovine lung[4] Seyfert H. M. Tuckoricz A. Interthal H. Koczan D. and Hobom G. et al. Structure of the bovine lactoferrin-encoding gene and its promoter[5] Nakamura I. Shimazaki K. Yagi Y. and Watanabe A. et al. Direct Submission[6] Pierce A. Colavizza D. Benaissa M. Maes P. Tartar A. Montreuil J. Spik G. Molecular cloning and sequence analysis of bovine lactotransferrin. [7] Goodman R. E. Schanbacher F. L. Bovine lactoferrin mRNA: sequence analysis and expression in the mammary gland. [8] Tsang T. C. Burns D. K. Wang F. Pan Y. C. E. Schmidt A. M. Stern D. Cloning of a 80-kD advanced glycosylation end product (AGE) binding protein from bovine lung. [9] Seyfert H. -M. Tuckoricz A. Interthal H. Koczan D. Hobom G. Structure of the bovine lactoferrin-encoding gene and its promoter. [10] Nakamura I. Shimazaki K. Yagi Y. Watanabe A. Bovine lactoferrin.

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