LCN1 / VEGP / Lipocalin-1 Recombinant Protein | LCN1 recombinant protein

Recombinant Human LCN1 / VEGP / Lipocalin-1 Protein (His tag)

Cat. Num. AAA2545738

• Gene Names: LCN1; TP; TLC; PMFA; VEGP
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: LCN1 / VEGP / Lipocalin-1; Recombinant Human LCN1 / VEGP / Lipocalin-1 Protein (His tag); MGC71975; PMFA; TLC; TP; VEGP; LCN1 recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 176

• Application Notes: The secreted recombinant human LCN1 consists of 169 amino acids and has a predicted molecular mass of 19 kDa The apparent molecular mass of the protein is approximately 20 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: His 19
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for LCN1 recombinant protein

Background: Lipocalin-1, also known as Von Ebner gland protein, VEG protein, Tear prealbumin, VEGP, Tear lipocalin and LCN1, is a secreted protein which belongs to the calycin superfamily and Lipocalin family. Human Lipocalin-1 / VEGP was originally described as a major protein of human tear fluid, which was thought to be tear specific. Lipocalin-1 / VEGP is identical with lingual von Ebner's gland protein, and is also produced in prostate, nasal mucosa and tracheal mucosa. Homologous proteins have been found in rat, pig and probably dog and horse. Lipocalin-1 / VEGP is an unusual lipocalin member, because of its high promiscuity for relative insoluble lipids and binding characteristics that differ from other members. Lipocalin-1 / VEGP acts as the principal lipid binding protein in tear fluid, a more general physiological function has to be proposed due to its wide distribution and properties. Lipocalin-1 / VEGP would be ideally suited for scavenging of lipophilic, potentially harmful substances and thus might act as a general protection factor of epithelia. Lipocalin-1 / LCN1 could play a role in taste reception. It could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Lipocalin-1 / LCN1 can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. It exhibits an extremely wide ligand pocket.

Description: A DNA sequence encoding the human LCN1 (NP_002288.1) extracellular domain (Met 1-Asp176) was fused with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 4504963
• NCBI GeneID: 3933
• NCBI Accession #: NP_002288.1
• NCBI GenBank Nucleotide #: NM_002297.3
• UniProt Accession #: P31025; Q5T8A1
• Molecular Weight: 19,250 Da
• NCBI Official Full Name: lipocalin-1 isoform 1
• NCBI Official Synonym Full Names: lipocalin 1
• NCBI Official Symbol: LCN1
• NCBI Official Synonym Symbols: TP; TLC; PMFA; VEGP
• NCBI Protein Information: lipocalin-1
• UniProt Protein Name: Lipocalin-1
• Protein Family: Lipocalin
• UniProt Gene Name: LCN1
• UniProt Synonym Gene Names: VEGP; Tlc; TP; VEG protein

NCBI Description

This gene encodes a member of the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins that bind to a variety of hydrophobic ligands. The encoded protein is the primary lipid binding protein in tears and is overproduced in response to multiple stimuli including infection and stress. The encoded protein may be a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and two pseudogenes of this gene are also located on the long arm of chromosome 9. [provided by RefSeq, Nov 2011]

Uniprot Description

Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket.