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Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

MOG is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a primary target antigen involved in immune-mediated demyelination. MOG is involved in completion and maintenance of the myelin sheath and in cell-cell communication. Alternatively spliced transcript variants encoding different isoforms have been identified Minor component of the myelin sheath is involved in completion and/or maintenance of the myelin sheath and in cell- cell communication.

Nucleotide Binding Protein 2, also known as NUBP2 is an adenosine triphosphate (ATP) as well as metal-binding protein which is essential for the assembly of cyotosolic iron-sulfur proteins. NUBP2 performs in a heterotetramer with nucleotide-binding protein 1 (NUBP1). Moreover, alternative splicing results in multiple transcript variants have been found for NUBP2.

N-Acetylglucosamine Kinase (NAGK) is a part of the eukaryotic-type N-acetylglucosamine kinase family. NAGK transforms endogenous N-acetylglucosamine (GlcNAc), a main component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK is a significant salvage enzyme of amino sugar metabolism in mammals which has ManNAc kinase activity.

XG is the XG blood group antigen, and is at the pseudoautosomal boundary on the short (p) arm of chromosome X. The three 5' exons are located in the pseudoautosomal area and the remaining exons within the X-specific end. A shorted copy of XG is found on the Y chromosome at the pseudoautosomal boundary. XG is transcribed, although not expected to make a Y-chromosome specific gene product.

Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.

The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.

Neural Cell Adhesion Molecule 1 (NCAM1) is apart of the immunoglobulin superfamily. NCAM1 bindsspecifically to neurite fasciculation, neuronneuron adhesion, outgrowth of neurites, and more. The polysialyation of NCAM1 reduces its adhesive property and increases its neurite outgrowth promoting features.NCAM1is mainly expressed in NK cells and a subset of T lymphocytes that mediate MHC-unrestricted cellmediated cytotoxicity. High expression of NCAM-1 differentiates NK cells as having an activated phenotype. During hematopoiesis, NCAM1plays a role as the prototypic marker of NK cells and also present on subset of CD4+, CD8+ and T cells. In cell adhesion, NCAM1 contributes to cell-cell adhesion during embryonic development.

GNB3 belongs to the WD repeat G protein beta family. GNB3 is an important regulator of alpha subunit, as well as of certain signal transduction receptor and effector. A single-nucleotide polymorphism (C825T) in GNB3 is linked with essential hypertension and obesity. In addition, this polymorphism is also linked with the occurrence of the splice variant GNB3-s, which seems to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. Further splice variants may exist for GNB3, however they have not been fully described. Among the diseases associated with GNB3 are syncope, and aortic coarctation.

Fetuin is a liver-produced negative acute phase protein composed of two subunits, the A and B chains.
Fetuin homologs have been identified in several species including rat, sheep, pig, rabbit, guinea pig, cattle, mouse and human. Multiple physiological roles for these homologs have been suggested, including ability to bind to hydroxyapatite crystals and to specifically inhibit the tyrosine kinase (TK) activity of the insulin receptor (IR).
Fetuin-A (alpha2-Heremans-Schmid glycoprotein; AHSG) is an important circulating inhibitor of calcification in vivo, and is downregulated during the acute-phase response.
Sera from patients on long-term dialysis with low AHSG concentrations showed impaired ex-vivo capacity to inhibit CaxPO4 precipitation.
Fetuin may influence the resolution of inflammation by modulating the phagocytosis of apoptotic cells by macrophages.
ASHG blocks TGF-beta-dependent signaling in osteoblastic cells, and mice lacking ASHG display growth plate defects, increased bone formation with age, and enhanced cytokine-dependent osteogenesis.

NAGK is a member of the eukaryotic-type N-acetylglucosamine kinase family. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a key component of complex carbohydrates, from lysosomal degradation or alimentary sources into GlcNAc 6-phosphate. NAGK is a prominent salvage enzyme of amino sugar metabolism in mammals. NAGK cooperates with STK16 and LNX1 and has ManNAc kinase activity.

Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.

Myelin Oligodendrocyte Glycoprotein is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a prime target antigen that plays a role in immune-mediated demyelination. Myelin Oligodendrocyte Glycoprotein is involved in completion and maintenance of the myelin sheath and in cell-cell communication. MOG protein was found to differentially expressed in the dorsolateral prefrontal cortex and in the temporal lobe from patients with schizophrenia. MOG-specific antibody is crucial to the initiation of MOG-induced murine experimental autoimmune encephalomyelitis.

Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

MAK16 is a member of the MAK16 family.

Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.

Neuroblastoma suppressor of tumorigenicity 1 (NBL1) is a part of the evolutionarily conserved CAN (Cerberus and DAN) family of proteins, which contain a domain resembling the CTCK (C-terminal cystine knot-like) motif found in several signaling molecules. NBL1 is a is a tumor suppressor of neuroblastoma and takes part in preventing cells from entering the final stage (G1/S) of the transformation process. NBL1 is produced in small neurons of the dorsal root ganglion. The expression of NBL1 is triggered by MATH-1.

GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Eschericia coli bacteria, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes.
Maltose binding protein MalE,MBP, is part of the maltodextrin transport system in E. coli. The maltodextrins diffuse through the LamB pore located in the outer membrane into the periplasm. The sugar is bound to MalE which prevents it to diffuse back outside. MalE passes the sugar to a complex of MalF and MalG in the cytoplasmic membrane where active tranport is mediated by the ATPase MalK. MBP molecular weight is 40,622 dalton. There are two domains in the protein with similar secondary structure (central pleated sheets are surrounded by helices) . The domains are connected by three bridges, between the domains is a deep groove in which the sugar is bound. All hydroxyl groups of the sugar are fixed by sidechains of the protein by hydrogen bonds. Some water molecules are part of the hydrogen bridge network.