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ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.

Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.

SKP is a 17kDa trimeric periplasmic chaperone that supports outer membrane proteins in their folding and insertion into membranes. SKP protein is necessary for the normal release of ompA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of ompA into the outer membrane.

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.

Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.

Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

EIF4EBP2 belongs to the eukaryotic translation initiation factor 4E binding protein family. Even though EIF4EBP2 protein binds eIF4E and inhibits translation initiation, growth factors can release this inhibition by a phosphorylation-dependent disruption. EIF4EBP2 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. Regulation of this protein is associated to cell proliferation, cell differentiation and viral infection.

EIF4EBP1 (eukaryotic translation initiation factor 4E-binding protein 1) belongs to a family of translation repressor proteins. EIF4EBP1 regulates eIF4E (eukaryotic translation initiation factor 4E) activity by preventing its assembly into the eIF4F complex and mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. EIF4EBP1 is phosphorylated in response to various signals including UV irradiation, resulting in its dissociation from eIF4E and activation of mRNA translation. EIF4EBP1 C-terminus has domains which control function and phosphorylation. EIF4EBP1 has a role in progression of breast neoplasms through cell signaling.

ERO1-like protein alpha (ERO1L) is an essential oxidoreductase, which oxidizes proteins and is necessary for the folding of immunoglobulins. ERO1L covalently binds with PDI (protein disulfide-isomerase) and jointly they generate disulfide bonds between proteins in the endoplasmic reticulum. ERO1L is stimulated by hypoxia, proposing that ERO1L is regulated through the HIF (hypoxia inducible transcrip-tion factor) pathway. At low levels ERO1L is ubiquitously expressed, however at high levels it is expressed in the upper digestive tract and esophagus. In addition, ERO1L is involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thus having a role in retrotranslocation of the toxin. Furthermore, ERO1L plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.

Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 (EIF4EBP3) belongs to the EIF4EBP family whose proteins bind to eukaryotic initiation factor 4E and regulate its assembly into EIF4F, the multi-subunit translation initiation factor that identifies the mRNA cap structure.

Eukaryotic Translation Elongation Factor 2 (EEF2) which is necessary factor for protein synthesis is a part of the GTP-binding translation elongation factor family. EEF2 catalyzes the GTP-dependent ribosomal translocation step during translation elongation. EEF2 is also catalyzes the coordinated movement of the mRNA as well as the 2 tRNA molecules and conformational changes in the ribosome. EF-2 kinase phosporylation inactivates the EEF2 protein.

EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.

GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.

EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

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).

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."

Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.

PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.