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Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

Mannose-6-Phosphate Receptor (M6PR) belongs to the P-type lectin family. P-type lectins play a vital role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The M6PR protein functions as a homodimer and needs divalent cations for ligand binding. Lysosomal enzymes carrying phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the ensuing receptor-ligand complex is transferred to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.

General Transcription Factor IIA, 1 (GTF2A1) in a complex along with TBP mediates transcriptional activity. GTF2A1 is a part of the transcription machinery of RNA polymerase II and is also participates in transcriptional activation.

COMMD1 is accountable for inhibition of TNF-induced NFκB p50 and n facilitats of biliary copper excretion within hepatocytes. High expression of COMMD1 is localized in liver tissue, with lower expressions in lung, heart, kidney and brain tissue. COMMD1 interacts directly with COMMD6 and ATP7B, and indirectly with IκB-β and COMMD7.

Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).

TNFSF12 is a cytokine that is part of the TNF ligand family. TNFSF12 is a ligand for the FN14/TWEAKR receptor. TNFSF12 has overlapping signaling functions with TNF, but displays a much wider tissue distribution. TNFSF12 induces apoptosis through multiple pathways of cell death in a cell type-specific manner. TNFSF12 promotes proliferation and migration of endothelial cells, and therefore acts as a regulator of angiogenesis. TNFSF12 is expressed in adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK h induces NFkB and chemokine secretion. TNFSF12 exerts an apoptotic activity in HT-29 human adenocarcinoma cells whilst cultured in the presence of IFN-?. TNFSF12 promotes proliferation and migration of endothelial cells.

This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Migration And Invasion Enhancer 1 (MIEN1) is a member of the SelWTH family. MIEN1 enhances cell migration by stimulating filopodia formation at the leading edge of migrating cells and takes parts in regulation of apoptosis, probably via control of CASP3. MIEN1 participates in a redox-related process as well.

S100 calcium binding protein A5 (S100A5) belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A5 has a Ca2+ affinity 20-100 fold higher than the other S100 proteins investigated under identical conditions. Furthermore, S100A5 protein binds Zn2+ and Cu2+, and Cu2+ strongly which harms the binding of Ca2+. S100A5 is expressed in very limited regions of the adult brain.

CTBP1 participates in controlling the equilibrium between tubular and stacked structures in the Golgi complex. CTBP1 functions in brown adipose tissue differentiation. CTBP1 has dehydrogenase activity. CTBP1 binds to the C-terminus of adenovirus E1A proteins. CTBP1 phosphoprotein is a transcriptional repressor and that takes part during cellular proliferation. CTBP1 & CTBP2 can dimerize and interact with a polycomb group protein complex which is involved in regulation of gene expression during development.

SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.

Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

CXADR is a component of the epithelial apical junction complex which operates as an homophilic cell adhesion molecule and is crucial for tight junction integrity. CXADR also takes part in transepithelial relocation of leukocytes through adhesive interactions with AMICA1/JAML a transmembrane protein of the plasma membrane of leukocytes. A number of transcript variants encoding different isoforms were identified for this gene. Pseudogenes of this gene were located on chromosomes 15, 18, and 21.

SDCBP is a multifunctional intracellular adapter protein. SDCBP protein has tandemly repeated PDZ domains which react with the FYA (phe-tyr-ala) carboxyterminal amino acid sequence of the syndecans. SDCBP is has a role in organization of protein complexes in the plasma membranes, regulation of B-cell development, activation of transcription factors, intracellular trafficking and cell-surface targeting, synaptic transmission, and axonal outgrowth.

ANGPT1 is an angiogenic factor which intervenes in blood vessel maturation and takes part in endothelial development. ANGPT1 is a secreted ligand for Tie-2, a cell surface receptor tyrosine kinase expressed in endothelial and hemopoietic cells. The glycosylated ANGPT1 protein has a coiled-coil region in the amino terminus and a fibrinogen-like domain at the carboxy terminus.

Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.

Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1) is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate. SERPIND1 gene is a member of the serpin gene superfamily. SERPIND1 protein contains 5 exons and 4 introns. SERPIND1 shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. SERPIND1 gene mutations are linked with cofactor II deficiency. SERPIND1 protein is activated by dermatan sulfate, and glycosaminoglycans. Allelic variations in the SERPIND1 gene are linked with cofactor II deficiency.

AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.

HRSP12 (UK114) is an endoribonuclease found mainly in the human adult kidney and liver, and which is responsible for inhibiting translation by cleaving mRNA. HRSP12 cleaves phosphodiester bonds only in single-stranded RNA. HRSP12 may be an important biomarker for heptatic carcinoma.

Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.

HtrA2 also called Omi is a mammalian serine protease at high temperatures and has a chaperone activity at low temperature. The full-length HtrA2 is synthesized as a precursor protein and then targeted to the mitochondria where it is matured by the removal of N-terminal 133 residues. Mature HtrA2 consists of a putative transmembrane domain; an inhibitor of apoptosis protein (IAP)-binding motif; a single C-terminal PDZ domain that mediates protein-protein interactions. Recently, HtrA2 has known to contribute both to caspase-dependent and caspase-independent cell death.

ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.