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MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.

Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.

Reg protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.

Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

PMF1-BGLAP is a locus which represents naturally occurring read-through transcription between the neighboring polyamine-modulated factor 1 (PMF1) and bone gamma-carboxyglutamate Gla protein (BGLAP) genes on chromosome 1. There are multiple transcript variants encoding isoforms as a results of alternative splicing which share sequence identity with the upstream gene product, but they have a different C-termini because of frameshifts as opposed to the downstream gene coding sequence.

NME2 takes an important part in the synthesis of nucleoside triphosphates other than ATP. NME2 negatively controls Rho activity by interacting with AKAP13/LBC. NME2 acts as a transcriptional activator of the MYC gene. NME2 binds DNA non-specifically. NME2 is a heterodimeric enzyme functioning as a nucleoside diphosphate kinase. NME1 and NME2 contain 152 amino acids, A and B polypeptide chains of the NM23 enzyme, respectively. NME2 is identical to the beta subunit of human erythrocyte NDP kinase. NDP kinases participate in the synthesis of nucleoside triphosphates, and NM23 is involved in the regulation of signal transduction by complexing with G proteins, causing activation/inactivation of developmental pathways.

Immunoglobulin G (IgG) are antibody molecules. Each IgG is composed of four peptide chains - 2 heavy chains g and 2 light chains. Also, each IgG has 2 antigen binding sites. IgG antibodies are involved in primarily the secondary immune response. The presence of specific IgG, generally, relates to maturation of the antibody response. IgG also has an imperative role in Antibody-dependent cell-mediated cytotoxicity (ADCC) and Intracellular antibody-mediated proteolysis, in which it binds to TRIM21 (the receptor with greatest affinity to IgG in humans) in order to direct marked virions to the proteasome in the cytosol.

Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.

MECP2 is the key modificator of eukaryotic genomes and has a crucial part in mammalian development.
Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 form a family of nuclear proteins linked by the existence in each of a methyl-CpG binding domain (MBD). Each one of these proteins, with the exception of MBD3, can bind specifically to methylated DNA. In addition, MECP2, MBD1 and MBD2 can inhibit transcription from methylated gene promoters. Unlike other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is expendable in stem cells, but is vital for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common reasons of mental retardation in females.

Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.

Parainfluenza virus, PIV, contains a group of four distinct serotypes of single-stranded RNA viruses belonging to the paramyxovirus family and two subtypes (4a and 4b). Parainfluenza viruse is a negative-sense, single-stranded RNA viruse that possess fusion and hemagglutinin-neuraminidase glycoprotein "spikes" on their surface. The virion varies in size (average diameter between 150 and 300 nm) and shape.

The mammaglobin gene was first identified using a differential screening approach directed at the isolation of novel, human breast cancer-associated genes. Mammaglobin encodes a 10 kDa glycoprotein and is distantly relaetd to a family of epithelial secretory proteins that includes rat estramustine-binding protein/prostatein and human Clara cell 10 kDa protein (CC10)/uteroglobin. Mammaglobin, a mammary-specific member of the uterglobin family, is known to be overexpressed in human breast cancer. Studies suggest that mammaglobin is one of the first relatively mammary-specific and mammary-sensitive markers (85%). Mammaglobin may be valuable used in a panel with BRST-2 (GCDFP-15) and ER in evaluating tumors of unknown primary sites.
SCGB2A2 (the mammaglobin gene) is located on chromosome 11, at locus 11q13. SCGB2A2 is member of the secretoglobin superfamily of which is a group of small dimeric secreted and sometimes glycosylated proteins. Expressed mainly in mucosa, secretoglobins appear to be involved in cell signalling, immune response, chemotaxis, and might also serve as transporters for steroid hormones in humans.

RTN4IP1 is a unique mitochondrial protein that interacts with reticulon 4, which is an effective inhibitor of regeneration ensuing spinal cord injury. The reticulon 4 interaction with mitochondrial proteins may offer insight into the mechanisms for reticulon-induced inhibition of neurite growth.

PABPN1 is an highly expressed nuclear protein which has high affinity to nascent poly(A) tails. PABPN1 is essential for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and regulates the length of the poly(A) tail to about 250 nt. In its steady-state, PABPN1 is restricted to the nucleus however there are different poly(A) binding proteins which can be found in the cytoplasm. PABPN1 has a GCG trinucleotide repeat at the 5' end of the coding region. Expansion of this repeat from the normal 6 copies to 8-13 copies results in autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Associated pseudogenes were located on chromosomes 19 and X. Additionally, there is a read-through transcription between PABPN1 gene and the adjacent upstream BCL2L2 (BCL2-like 2) gene.

PCNA is located in the nucleus and is a cofactor of DNA polymerase delta. PCNA acts as a homotrimer and helps elevate the processivity of leading strand synthesis during DNA replication. In reaction to DNA damage, PCNA is ubiquitinated and takes part in the RAD6-dependent DNA repair pathway. 2 transcript variants encoding the same protein have been found for PCNA gene. Pseudogenes of this PCNA gene have been described on chromosome 4 and on the X chromosome. PCNA is expressed during late G1- phase, S-phase of mitosis and persists until the end of the M-phase because of its long biological half-life. PCNA is induced by UV irradiation.

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.

GAGE2A is a member of a multigene family expressed in a large variety of tumors while in normal tissues; expression is limited to germ cells. These genes organized in clustered repeats, have a high degree of predicted sequence identity, however differ by scattered single nucleotide change. Their sequences have either the antigenic peptide YRPRPRRY or YYWPRPRRY which is recognized by cytotoxic T-cells.

PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

Protein Phosphatase 4 Catalytic subunit (PPP4C), is a part of the Serine/threonine-protein phosphatase catalytic subunits which tskes part in dephosphorylation and regulation of HDAC3. The protein phosphatase (PP) holoenzyme is a trimeric complex compound of a regulatory subunit, a variable subunit and a catalytic subunit. 4 major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C.

Oligodendrocyte-myelin glycoprotein (OMG) is a cell membrane protein which contains 8 leucine-rich repeats. The OMG protein is expressed on the surface of oligodendrocytes and on large projection neurons, including Purkinje cells of the cerebellum, pyramidal cells of the hippocampus, motoneurons of the brainstem and anterior horn cells of the spinal cord. The neurite outgrowth inhibitory activities of all three myelin-derived proteins are mediated by binding to a joint receptor complex consisting of the Nogo receptor and the p75 neurotrophin receptor.