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IgG1 Fcplays a role in antigen binding activity and immunoglobulin receptor binding activity. IgG1 Fc takes part in the activation of immune & defensive response. IgG1 Fc takes part in the upstream of immunoglobulin mediated immune response, positive regulation of hypersensitivity & regulation of phagocytosis.

BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.

Krueppel-like factor 12 (KLF12) belongs to the Kruppel-like zinc finger protein family and can repress expression of the AP-2 alpha gene by binding to a particular site in the AP-2 alpha gene promoter. AP-2 alpha (Activator protein-2 alpha) is a developmentally-regulated transcription factor and vital regulator of gene expression during vertebrate development and carcinogenesis. KLF12 gene repression entails binding with a corepressor, CtBP1.

GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.

GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.

The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.

Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.

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.

The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

26S proteasome complex subunit DSS1 (SHFM1) has been suggested as a candidate gene for the autosomal dominant form of the heterogeneous limb developmental disorder split hand/split foot malformation type 1. SHFM1 is a subunit of the 26S proteasome which plays a part in ubiquitin-dependent proteolysis. SHFM1 binds and stabilizes BRCA2 and is therefore involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. Furthermore, SHFM1 may have a role in the completion of the cell cycle. SHFM1 is a component of the TREX-2 complex (transcription and export complex 2), comprised of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3.

SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.

Fibroblast Growth Factors (FGFs) comprise a family of at least 18 structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). An IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

DDB1-and CUL4-associated factor (DCAF7) is involved in craniofacial development. The DCAF7 protein acts upstream of the EDN1 pathway and is essential for formation of the upper jaw equivalent, the palatoquadrate. The activity necessary for the EDN1 pathway function varies between the first and second arches. DCAF7 associates with DIAPH1 and controls GLI1 transcriptional activity. DCAF7 may be involved in normal and diseased skin development.

DiGeorge syndrome critical region gene 6 (DGCR6) shares homology with the Drosophila melanogaster gonadal protein, that participates in gonadal and germ cell development, and also with the gamma-1 subunit of human laminin. DGCR6 is involved in DiGeorge syndrome pathology and in schizophrenia.