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Lactotransferrin (Lactoferrin) (EC 3.4.21.-) [Cleaved into: Lactoferricin-B (Lfcin-B)]

 TRFL_BOVIN              Reviewed;         708 AA.
P24627; Q1JQC9; Q29629; Q6LEC7; Q9MZY3;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
25-OCT-2017, entry version 177.
RecName: Full=Lactotransferrin;
Short=Lactoferrin;
EC=3.4.21.-;
Contains:
RecName: Full=Lactoferricin-B;
Short=Lfcin-B;
Flags: Precursor;
Name=LTF;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Submandibular gland;
PubMed=2001696; DOI=10.1111/j.1432-1033.1991.tb15801.x;
Pierce A., Colavizza D., Benaissa M., Maes P., Tartar A.,
Montreuil J., Spik G.;
"Molecular cloning and sequence analysis of bovine lactotransferrin.";
Eur. J. Biochem. 196:177-184(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1718281; DOI=10.1016/S0006-291X(05)81257-4;
Goodman R.E., Schanbacher F.L.;
"Bovine lactoferrin mRNA: sequence, analysis, and expression in the
mammary gland.";
Biochem. Biophys. Res. Commun. 180:75-84(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
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.";
FASEB J. 6:233-233(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Blood, and Mammary gland;
PubMed=8206385; DOI=10.1016/0378-1119(94)90108-2;
Seyfert H.-M., Tuckoricz A., Interthal H., Koczan D., Hobom G.;
"Structure of the bovine lactoferrin-encoding gene and its promoter.";
Gene 143:265-269(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Nakamura I., Shimazaki K., Yagi Y., Watanabe A.;
"Bovine lactoferrin.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 20-59.
PubMed=2805645;
Rejman J.J., Hegarty H.M., Hurley W.L.;
"Purification and characterization of bovine lactoferrin from
secretions of the involuting mammary gland: identification of multiple
molecular weight forms.";
Comp. Biochem. Physiol. 93B:929-934(1989).
[8]
PROTEIN SEQUENCE OF 36-60, IDENTIFICATION OF LACTOFERRICIN PEPTIDE,
FUNCTION, AND SYNTHESIS OF 36-60.
TISSUE=Milk;
PubMed=1599934; DOI=10.1016/0167-4838(92)90346-F;
Bellamy W., Takase M., Yamauchi K., Wakabayashi H., Kawase K.,
Tomita M.;
"Identification of the bactericidal domain of lactoferrin.";
Biochim. Biophys. Acta 1121:130-136(1992).
[9]
FUNCTION OF LACTOFERRICIN.
PubMed=8980754;
Hoek K.S., Milne J.M., Grieve P.A., Dionysius D.A., Smith R.;
"Antibacterial activity in bovine lactoferrin-derived peptides.";
Antimicrob. Agents Chemother. 41:54-59(1997).
[10]
ANTIMICROBIAL ACTIVITY.
PubMed=14650542; DOI=10.1186/1751-0147-44-35;
Kutila T., Pyorala S., Saloniemi H., Kaartinen L.;
"Antibacterial effect of bovine lactoferrin against udder pathogens.";
Acta Vet. Scand. 44:35-42(2003).
[11]
PROTEASE FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15222473; DOI=10.1023/B:BIOM.0000027700.90780.45;
Massucci M.T., Giansanti F., Di Nino G., Turacchio M., Giardi M.F.,
Botti D., Ippoliti R., De Giulio B., Siciliano R.A., Donnarumma G.,
Valenti P., Bocedi A., Polticelli F., Ascenzi P., Antonini G.;
"Proteolytic activity of bovine lactoferrin.";
BioMetals 17:249-255(2004).
[12]
FUNCTION.
PubMed=15166119; DOI=10.1210/en.2003-1307;
Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U.,
Watson M., Lin J.M., Tong P.C., Chen Q., Chan V.A., Reid H.E.,
Fazzalari N., Baker H.M., Baker E.N., Haggarty N.W., Grey A.B.,
Reid I.R.;
"Lactoferrin is a potent regulator of bone cell activity and increases
bone formation in vivo.";
Endocrinology 145:4366-4374(2004).
[13]
FUNCTION.
PubMed=20345905; DOI=10.1111/j.1742-4658.2010.07620.x;
Ando K., Hasegawa K., Shindo K., Furusawa T., Fujino T., Kikugawa K.,
Nakano H., Takeuchi O., Akira S., Akiyama T., Gohda J., Inoue J.,
Hayakawa M.;
"Human lactoferrin activates NF-kappaB through the Toll-like receptor
4 pathway while it interferes with the lipopolysaccharide-stimulated
TLR4 signaling.";
FEBS J. 277:2051-2066(2010).
[14]
ERRATUM.
Massucci M.T., Giansanti F., Di Nino G., Turacchio M., Giardi M.F.,
Botti D., Ippoliti R., De Giulio B., Siciliano R.A., Donnarumma G.,
Valenti P., Bocedi A., Polticelli F., Ascenzi P., Antonini G.;
BioMetals 17:745-745(2004).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=9398529; DOI=10.1006/jmbi.1997.1386;
Moore S.A., Anderson B.F., Groom C.R., Haridas M., Baker E.N.;
"Three-dimensional structure of diferric bovine lactoferrin at 2.8-A
resolution.";
J. Mol. Biol. 274:222-236(1997).
[16]
STRUCTURE BY NMR OF 36-60.
PubMed=9521752; DOI=10.1021/bi972323m;
Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J.;
"Three-dimensional solution structure of lactoferricin B, an
antimicrobial peptide derived from bovine lactoferrin.";
Biochemistry 37:4288-4298(1998).
-!- 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 is a major iron-binding and
multifunctional protein found in exocrine fluids such as breast
milk and mucosal secretions. Has antimicrobial activity.
Antimicrobial properties may include bacteriostasis, which is
related to its ability to sequester free iron and thus inhibit
microbial growth, as well as direct bactericidal properties
leading to the release of lipopolysaccharides from the bacterial
outer membrane. The most effective inhibitory activity is seen
against E.coli and P.aeruginosa. Has anabolic, differentiating and
anti-apoptotic effects on osteoblasts and can also inhibit
osteoclastogenesis, possibly playing a role in the regulation of
bone growth. Interferes with the lipopolysaccharide (LPS)-
stimulated TLR4 signaling, but cannot directly stimulate the TLR4
signaling pathway and subsequent NF-kappa-B activation.
-!- FUNCTION: Lactoferricin B is an antimicrobial peptide. Inhibits
the growth of Gram-negative and Gram-positive bacteria.
-!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions
as a serine protease of the peptidase S60 family that cuts
arginine rich regions. This function contributes to the
antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-
Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-
aminomethylcoumarin sites.
-!- ENZYME REGULATION: Inhibited by PMSF and Pefabloc.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for Z-Phe-Arg-|-aminomethylcoumarin
{ECO:0000269|PubMed:15222473};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:15222473};
Temperature dependence:
Optimum temperature is 25 degrees Celsius.
{ECO:0000269|PubMed:15222473};
-!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and
SEMG1 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-8076910, EBI-6904269;
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
Note=Secreted into most exocrine fluids by various endothelial
cells. Stored in the secondary granules of neutrophils (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
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EMBL; X57084; CAA40366.1; -; mRNA.
EMBL; M63502; AAA30617.1; -; mRNA.
EMBL; L08604; AAA30609.1; -; mRNA.
EMBL; L19993; AAA21722.1; -; Genomic_DNA.
EMBL; L19982; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19983; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19984; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19985; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19986; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19988; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19989; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19990; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19991; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19992; AAA21722.1; JOINED; Genomic_DNA.
EMBL; L19981; AAA30610.1; -; mRNA.
EMBL; AB046664; BAB03470.1; -; mRNA.
EMBL; BC116051; AAI16052.1; -; mRNA.
PIR; I45919; TFBOL.
RefSeq; NP_851341.1; NM_180998.2.
RefSeq; XP_015315141.1; XM_015459655.1.
UniGene; Bt.44264; -.
PDB; 1BLF; X-ray; 2.80 A; A=20-708.
PDB; 1LFC; NMR; -; A=36-60.
PDB; 1NKX; X-ray; 1.90 A; A=361-708.
PDB; 1SDX; X-ray; 2.06 A; A=361-695, E=700-704.
PDB; 1Y58; NMR; -; A=38-49.
PDB; 2ALU; X-ray; 2.09 A; A=361-708.
PDB; 2AYS; X-ray; 1.86 A; A=361-708.
PDB; 2B65; X-ray; 1.50 A; A=361-705.
PDB; 2DOJ; X-ray; 2.40 A; A=361-705.
PDB; 2DP8; X-ray; 2.50 A; A=361-705.
PDB; 2DQV; X-ray; 2.70 A; A=361-705.
PDB; 2DS9; X-ray; 2.80 A; A=361-705.
PDB; 2DSF; X-ray; 2.80 A; A=361-705.
PDB; 2DVC; X-ray; 3.00 A; A=361-705.
PDB; 2DWA; X-ray; 2.07 A; A=361-705.
PDB; 2DWH; X-ray; 2.80 A; A=361-705.
PDB; 2DWI; X-ray; 2.20 A; A=361-705.
PDB; 2DWJ; X-ray; 2.30 A; A=361-705.
PDB; 2DXR; X-ray; 2.85 A; A=361-705.
PDB; 2DXY; X-ray; 2.03 A; A=361-705.
PDB; 2DYX; X-ray; 2.00 A; A=361-705.
PDB; 2E0S; X-ray; 2.15 A; A=361-705.
PDB; 2E1S; X-ray; 2.70 A; A=361-705.
PDB; 2FA7; X-ray; 2.38 A; A=361-705.
PDB; 2G93; X-ray; 1.90 A; A=361-705.
PDB; 2H4I; X-ray; 2.55 A; A=361-705.
PDB; 2HCA; X-ray; 2.80 A; A=361-705.
PDB; 2MD1; NMR; -; A=287-303.
PDB; 2MD2; NMR; -; A=287-296.
PDB; 2MD3; NMR; -; A=296-303.
PDB; 2MD4; NMR; -; A=287-298.
PDB; 2NUV; X-ray; 2.25 A; A=361-705.
PDB; 2NWJ; X-ray; 2.25 A; A=361-705.
PDB; 2O1L; X-ray; 1.97 A; A=361-705.
PDB; 2O51; X-ray; 3.00 A; A=361-705.
PDB; 2OCU; X-ray; 2.38 A; A=361-705.
PDB; 2P1S; X-ray; 1.93 A; A=361-704.
PDB; 2PX1; X-ray; 2.50 A; A=361-705.
PDB; 2Q8J; X-ray; 2.71 A; A=361-708.
PDB; 2QJE; X-ray; 2.30 A; A=361-708.
PDB; 2R71; X-ray; 2.07 A; A=361-705.
PDB; 2R9J; X-ray; 2.55 A; A=361-705.
PDB; 2ZMB; X-ray; 2.90 A; A=361-705.
PDB; 3CFL; X-ray; 2.25 A; A=361-705.
PDB; 3CI8; X-ray; 2.40 A; A=361-705.
PDB; 3CRB; X-ray; 2.60 A; A=361-705.
PDB; 3E9X; X-ray; 2.70 A; A=361-705.
PDB; 3IAZ; X-ray; 2.00 A; A=361-705.
PDB; 3IB0; X-ray; 1.40 A; A=361-705.
PDB; 3IB1; X-ray; 2.20 A; A=361-705.
PDB; 3IB2; X-ray; 2.29 A; A=361-705.
PDB; 3K0V; X-ray; 1.91 A; A=361-705.
PDB; 3KJ7; X-ray; 1.91 A; A=361-705.
PDB; 3MJN; X-ray; 2.38 A; A=361-705.
PDB; 3O97; X-ray; 2.68 A; A=361-705.
PDB; 3RGY; X-ray; 2.00 A; A=361-705.
PDB; 3SDF; X-ray; 2.10 A; A=361-705.
PDB; 3TAJ; X-ray; 1.70 A; A=361-705.
PDB; 3TOD; X-ray; 1.38 A; A=361-695, B=700-705.
PDB; 3TTR; X-ray; 2.27 A; A=361-705.
PDB; 3TUS; X-ray; 2.50 A; A=361-705.
PDB; 3U72; X-ray; 2.20 A; A=361-695, B=700-705.
PDB; 3U8Q; X-ray; 1.97 A; A=361-695, B=700-705.
PDB; 3UGW; X-ray; 1.87 A; A=361-695, B=700-705.
PDB; 3UK4; X-ray; 1.98 A; A=361-695, B=700-705.
PDB; 3USD; X-ray; 2.40 A; A=361-695, B=700-705.
PDB; 3V5A; X-ray; 1.44 A; A=361-695, B=700-705.
PDB; 3VDF; X-ray; 1.46 A; A=361-695, B=700-705.
PDB; 4DIG; X-ray; 1.80 A; A=361-695, B=700-705.
PDB; 4DXU; X-ray; 1.46 A; A=361-695, B=700-705.
PDB; 4FIM; X-ray; 1.80 A; A=361-695, B=700-705.
PDB; 4FJP; X-ray; 1.68 A; A=361-695, B=700-705.
PDB; 4FOR; X-ray; 1.58 A; A=361-695, B=700-705.
PDB; 4G2Z; X-ray; 1.90 A; A=361-695, B=700-705.
PDB; 4G77; X-ray; 1.98 A; A=361-705.
PDB; 4G8H; X-ray; 1.88 A; A=361-705.
PDB; 4GRK; X-ray; 1.68 A; A=361-695, B=700-705.
PDB; 4N6P; X-ray; 1.40 A; A=361-695, B=700-705.
PDB; 4NED; X-ray; 2.10 A; A=361-705.
PDB; 4OQO; X-ray; 2.42 A; A/B=361-708.
PDB; 5CRY; X-ray; 2.79 A; A/B=361-708.
PDB; 5HBC; X-ray; 2.79 A; A/B=361-708.
PDBsum; 1BLF; -.
PDBsum; 1LFC; -.
PDBsum; 1NKX; -.
PDBsum; 1SDX; -.
PDBsum; 1Y58; -.
PDBsum; 2ALU; -.
PDBsum; 2AYS; -.
PDBsum; 2B65; -.
PDBsum; 2DOJ; -.
PDBsum; 2DP8; -.
PDBsum; 2DQV; -.
PDBsum; 2DS9; -.
PDBsum; 2DSF; -.
PDBsum; 2DVC; -.
PDBsum; 2DWA; -.
PDBsum; 2DWH; -.
PDBsum; 2DWI; -.
PDBsum; 2DWJ; -.
PDBsum; 2DXR; -.
PDBsum; 2DXY; -.
PDBsum; 2DYX; -.
PDBsum; 2E0S; -.
PDBsum; 2E1S; -.
PDBsum; 2FA7; -.
PDBsum; 2G93; -.
PDBsum; 2H4I; -.
PDBsum; 2HCA; -.
PDBsum; 2MD1; -.
PDBsum; 2MD2; -.
PDBsum; 2MD3; -.
PDBsum; 2MD4; -.
PDBsum; 2NUV; -.
PDBsum; 2NWJ; -.
PDBsum; 2O1L; -.
PDBsum; 2O51; -.
PDBsum; 2OCU; -.
PDBsum; 2P1S; -.
PDBsum; 2PX1; -.
PDBsum; 2Q8J; -.
PDBsum; 2QJE; -.
PDBsum; 2R71; -.
PDBsum; 2R9J; -.
PDBsum; 2ZMB; -.
PDBsum; 3CFL; -.
PDBsum; 3CI8; -.
PDBsum; 3CRB; -.
PDBsum; 3E9X; -.
PDBsum; 3IAZ; -.
PDBsum; 3IB0; -.
PDBsum; 3IB1; -.
PDBsum; 3IB2; -.
PDBsum; 3K0V; -.
PDBsum; 3KJ7; -.
PDBsum; 3MJN; -.
PDBsum; 3O97; -.
PDBsum; 3RGY; -.
PDBsum; 3SDF; -.
PDBsum; 3TAJ; -.
PDBsum; 3TOD; -.
PDBsum; 3TTR; -.
PDBsum; 3TUS; -.
PDBsum; 3U72; -.
PDBsum; 3U8Q; -.
PDBsum; 3UGW; -.
PDBsum; 3UK4; -.
PDBsum; 3USD; -.
PDBsum; 3V5A; -.
PDBsum; 3VDF; -.
PDBsum; 4DIG; -.
PDBsum; 4DXU; -.
PDBsum; 4FIM; -.
PDBsum; 4FJP; -.
PDBsum; 4FOR; -.
PDBsum; 4G2Z; -.
PDBsum; 4G77; -.
PDBsum; 4G8H; -.
PDBsum; 4GRK; -.
PDBsum; 4N6P; -.
PDBsum; 4NED; -.
PDBsum; 4OQO; -.
PDBsum; 5CRY; -.
PDBsum; 5HBC; -.
ProteinModelPortal; P24627; -.
SMR; P24627; -.
BioGrid; 158240; 1.
IntAct; P24627; 4.
STRING; 9913.ENSBTAP00000001704; -.
ChEMBL; CHEMBL2796; -.
Allergome; 1065; Bos d LF.
MEROPS; S60.001; -.
UniCarbKB; P24627; -.
PaxDb; P24627; -.
PeptideAtlas; P24627; -.
PRIDE; P24627; -.
Ensembl; ENSBTAT00000001704; ENSBTAP00000001704; ENSBTAG00000001292.
GeneID; 280846; -.
KEGG; bta:280846; -.
CTD; 4057; -.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
GeneTree; ENSGT00390000001619; -.
HOGENOM; HOG000043759; -.
HOVERGEN; HBG000055; -.
InParanoid; P24627; -.
KO; K17283; -.
OMA; LRPFLNW; -.
OrthoDB; EOG091G0242; -.
TreeFam; TF324013; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-6799990; Metal sequestration by antimicrobial proteins.
Reactome; R-BTA-6803157; Antimicrobial peptides.
SABIO-RK; P24627; -.
EvolutionaryTrace; P24627; -.
PMAP-CutDB; P24627; -.
Proteomes; UP000009136; Chromosome 22.
Bgee; ENSBTAG00000001292; -.
ExpressionAtlas; P24627; baseline and differential.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0044218; C:other organism cell membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0042581; C:specific granule; ISS:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CAFA.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IMP:AgBase.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IEA:Ensembl.
GO; GO:0051673; P:membrane disruption in other organism; IEA:Ensembl.
GO; GO:0044793; P:negative regulation by host of viral process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0032780; P:negative regulation of ATPase activity; IEA:Ensembl.
GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB.
GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IDA:UniProtKB.
GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
InterPro; IPR030684; Lactotransferrin.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
PANTHER; PTHR11485:SF33; PTHR11485:SF33; 1.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500683; Lactotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Immunity; Ion transport; Iron; Iron transport; Metal-binding;
Osteogenesis; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:2805645}.
CHAIN 20 708 Lactotransferrin.
/FTId=PRO_0000035726.
PEPTIDE 36 60 Lactoferricin-B.
/FTId=PRO_0000035727.
DOMAIN 25 352 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 364 693 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
ACT_SITE 92 92 {ECO:0000255|PROSITE-ProRule:PRU00741}.
ACT_SITE 278 278 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 79 79 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 111 111 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 211 211 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 272 272 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 414 414 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 452 452 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 545 545 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
METAL 614 614 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
BINDING 136 136 Carbonate 1.
BINDING 140 140 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
BINDING 142 142 Carbonate 1; via amide nitrogen.
BINDING 143 143 Carbonate 1; via amide nitrogen.
BINDING 478 478 Carbonate 2.
BINDING 482 482 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:9398529}.
BINDING 484 484 Carbonate 2; via amide nitrogen.
BINDING 485 485 Carbonate 2; via amide nitrogen.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000186.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000197.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000198.
DISULFID 28 64 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 38 55
DISULFID 134 217 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 176 192 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 189 200 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 250 264 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 367 399 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 377 390 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 424 703 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 444 666 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 476 551 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 500 694 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 510 524 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 521 534 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 592 606 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 644 649 {ECO:0000255|PROSITE-ProRule:PRU00741}.
CONFLICT 63 63 E -> A (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 66 67 RA -> PG (in Ref. 2; AAA30617).
{ECO:0000305}.
CONFLICT 145 145 I -> V (in Ref. 1; CAA40366 and 4;
AAA21722/AAA30610). {ECO:0000305}.
CONFLICT 164 165 LQ -> PP (in Ref. 1; CAA40366).
{ECO:0000305}.
CONFLICT 264 264 C -> Y (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 273 273 A -> P (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 281 281 G -> A (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 291 291 S -> R (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 297 297 F -> S (in Ref. 2; AAA30617).
{ECO:0000305}.
CONFLICT 340 340 G -> A (in Ref. 1; CAA40366).
{ECO:0000305}.
CONFLICT 418 418 I -> V (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 436 436 S -> T (in Ref. 4; AAA30610).
{ECO:0000305}.
CONFLICT 439 439 H -> Y (in Ref. 1; CAA40366 and 4;
AAA30610). {ECO:0000305}.
CONFLICT 459 459 K -> R (in Ref. 4; AAA21722).
{ECO:0000305}.
CONFLICT 514 514 A -> R (in Ref. 1; CAA40366 and 4;
AAA30610). {ECO:0000305}.
CONFLICT 632 632 H -> R (in Ref. 5; BAB03470).
{ECO:0000305}.
STRAND 25 31 {ECO:0000244|PDB:1BLF}.
HELIX 32 45 {ECO:0000244|PDB:1BLF}.
HELIX 46 48 {ECO:0000244|PDB:1BLF}.
STRAND 53 57 {ECO:0000244|PDB:1BLF}.
HELIX 61 69 {ECO:0000244|PDB:1BLF}.
STRAND 75 78 {ECO:0000244|PDB:1BLF}.
HELIX 80 87 {ECO:0000244|PDB:1BLF}.
TURN 89 91 {ECO:0000244|PDB:1BLF}.
STRAND 93 102 {ECO:0000244|PDB:1BLF}.
STRAND 104 120 {ECO:0000244|PDB:1BLF}.
STRAND 133 136 {ECO:0000244|PDB:1BLF}.
TURN 141 144 {ECO:0000244|PDB:1BLF}.
HELIX 145 155 {ECO:0000244|PDB:1BLF}.
TURN 159 161 {ECO:0000244|PDB:1BLF}.
HELIX 164 169 {ECO:0000244|PDB:1BLF}.
STRAND 172 176 {ECO:0000244|PDB:1BLF}.
TURN 182 184 {ECO:0000244|PDB:1BLF}.
HELIX 186 188 {ECO:0000244|PDB:1BLF}.
HELIX 210 219 {ECO:0000244|PDB:1BLF}.
STRAND 224 229 {ECO:0000244|PDB:1BLF}.
HELIX 232 236 {ECO:0000244|PDB:1BLF}.
HELIX 240 243 {ECO:0000244|PDB:1BLF}.
STRAND 246 248 {ECO:0000244|PDB:1BLF}.
TURN 261 263 {ECO:0000244|PDB:1BLF}.
STRAND 266 270 {ECO:0000244|PDB:1BLF}.
STRAND 273 280 {ECO:0000244|PDB:1BLF}.
HELIX 283 296 {ECO:0000244|PDB:1BLF}.
TURN 298 300 {ECO:0000244|PDB:2MD1}.
STRAND 325 328 {ECO:0000244|PDB:1BLF}.
HELIX 335 351 {ECO:0000244|PDB:1BLF}.
HELIX 354 362 {ECO:0000244|PDB:1BLF}.
STRAND 364 369 {ECO:0000244|PDB:3TOD}.
HELIX 370 383 {ECO:0000244|PDB:3TOD}.
TURN 384 386 {ECO:0000244|PDB:3TOD}.
STRAND 387 395 {ECO:0000244|PDB:3TOD}.
HELIX 396 404 {ECO:0000244|PDB:3TOD}.
STRAND 410 413 {ECO:0000244|PDB:3TOD}.
HELIX 415 423 {ECO:0000244|PDB:3TOD}.
STRAND 427 434 {ECO:0000244|PDB:3TOD}.
STRAND 437 439 {ECO:0000244|PDB:2B65}.
STRAND 440 442 {ECO:0000244|PDB:1BLF}.
HELIX 444 446 {ECO:0000244|PDB:3TOD}.
STRAND 452 459 {ECO:0000244|PDB:3TOD}.
HELIX 467 469 {ECO:0000244|PDB:3TOD}.
STRAND 474 478 {ECO:0000244|PDB:3TOD}.
TURN 483 486 {ECO:0000244|PDB:3TOD}.
HELIX 487 497 {ECO:0000244|PDB:3TOD}.
HELIX 502 504 {ECO:0000244|PDB:3TOD}.
STRAND 505 510 {ECO:0000244|PDB:3TOD}.
HELIX 519 521 {ECO:0000244|PDB:3TOD}.
STRAND 527 530 {ECO:0000244|PDB:2DQV}.
TURN 531 534 {ECO:0000244|PDB:3TOD}.
HELIX 544 553 {ECO:0000244|PDB:3TOD}.
STRAND 558 563 {ECO:0000244|PDB:3TOD}.
HELIX 564 569 {ECO:0000244|PDB:3TOD}.
STRAND 571 575 {ECO:0000244|PDB:2ZMB}.
TURN 578 582 {ECO:0000244|PDB:3TOD}.
HELIX 585 587 {ECO:0000244|PDB:3TOD}.
STRAND 588 591 {ECO:0000244|PDB:3TOD}.
STRAND 597 599 {ECO:0000244|PDB:3TOD}.
HELIX 600 605 {ECO:0000244|PDB:3TOD}.
STRAND 608 611 {ECO:0000244|PDB:3TOD}.
STRAND 615 618 {ECO:0000244|PDB:3TOD}.
HELIX 620 637 {ECO:0000244|PDB:3TOD}.
STRAND 638 640 {ECO:0000244|PDB:1SDX}.
TURN 642 647 {ECO:0000244|PDB:3TOD}.
STRAND 653 656 {ECO:0000244|PDB:3IB0}.
STRAND 658 660 {ECO:0000244|PDB:4OQO}.
STRAND 664 668 {ECO:0000244|PDB:3TOD}.
STRAND 671 673 {ECO:0000244|PDB:2O1L}.
HELIX 676 680 {ECO:0000244|PDB:3TOD}.
HELIX 682 692 {ECO:0000244|PDB:3TOD}.
HELIX 698 703 {ECO:0000244|PDB:4OQO}.
HELIX 704 707 {ECO:0000244|PDB:5CRY}.
SEQUENCE 708 AA; 78056 MW; C6FD7FC15D68E93F CRC64;
MKLFVPALLS LGALGLCLAA PRKNVRWCTI SQPEWFKCRR WQWRMKKLGA PSITCVRRAF
ALECIRAIAE KKADAVTLDG GMVFEAGRDP YKLRPVAAEI YGTKESPQTH YYAVAVVKKG
SNFQLDQLQG RKSCHTGLGR SAGWIIPMGI LRPYLSWTES LEPLQGAVAK FFSASCVPCI
DRQAYPNLCQ LCKGEGENQC ACSSREPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK
ADRDQYELLC LNNSRAPVDA FKECHLAQVP SHAVVARSVD GKEDLIWKLL SKAQEKFGKN
KSRSFQLFGS PPGQRDLLFK DSALGFLRIP SKVDSALYLG SRYLTTLKNL RETAEEVKAR
YTRVVWCAVG PEEQKKCQQW SQQSGQNVTC ATASTTDDCI VLVLKGEADA LNLDGGYIYT
AGKCGLVPVL AENRKSSKHS SLDCVLRPTE GYLAVAVVKK ANEGLTWNSL KDKKSCHTAV
DRTAGWNIPM GLIVNQTGSC AFDEFFSQSC APGADPKSRL CALCAGDDQG LDKCVPNSKE
KYYGYTGAFR CLAEDVGDVA FVKNDTVWEN TNGESTADWA KNLNREDFRL LCLDGTRKPV
TEAQSCHLAV APNHAVVSRS DRAAHVKQVL LHQQALFGKN GKNCPDKFCL FKSETKNLLF
NDNTECLAKL GGRPTYEEYL GTEYVTAIAN LKKCSTSPLL EACAFLTR


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