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AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.

BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.

SPRY domain-containing SOCS box protein 1 (SPSB1) belongs to the SOCS box protein subfamily. SPSB1 includes a central SPRY domain and a C-terminal SOCS box. Even though, some of the SOCS protein subfamilies function as adaptors for a large family of ubiquitin-protein isopeptide ligases to regulate certain signaling pathways, the function of the SSB subfamily remains to be determined. SPSB1 may have an imperative role in enhancing the HGF-induced Erk-Elk-1-SRE pathway. SPSB1 overexpression exhibited no effect on the basal level or epidermal growth factor-induced SRE-luciferase activity.

Ectonucleotide Pyrophosphatase (ENPP1) belongs to the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. ENPP1 is a type II transmembrane glycoprotein comprised of 2 identical disulfide-bonded subunits. The ENPP1 protein has broad specificity and cleaves various substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. The ENPP1 protein can hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and it may also hydrolyze diadenosine polyphosphates. ENPP1 gene mutations are linked with 'idiopathic' infantile arterial calcification and ossification of the posterior longitudinal ligament of the spine (OPLL).

TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.

Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.

LAMTOR2 is a member of the GAMAD family. LAMTOR2 is highly conserved with a mouse protein linked with the cytoplasmic face of late endosomes and lysosomes. The mouse protein interacts with MAPK scaffold protein 1, which is a component of the mitogen-activated protein kinase pathway. LAMTOR2 gene mutation has been associated with a primary immunodeficiency syndrome in humans, proposing a role for this protein in endosomal biogenesis.

Proteasome subunit beta type-2 (PSMB2) belongs to the proteasome T1B family, which is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. A crucial function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB2 is up-regulated in ovarian cancer cell lines.

Ribokinase (RBKS) is a member of the pfkB family of carbohydrate kinases. Ribokinase phosphorylates ribose to form ribose-5-phosphate in the presence of ATP and magnesium as a first step in ribose metabolism.

GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP5 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.

Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.

Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.

LY6D encloses 1 UPAR/Ly6 domain and is only expressed at the keratinocyte of stratified squamous epithelia and the outer cell surface of transitional epithelia. LY6D performs as a specification marker at earliest stage specification of lymphocytes between B- and T-cell developments.

ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.

HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.

SERPINB5 (Maspin) is a tumor suppressor protein of the serine proteinase inhibitor family. Maspin plays a vital role in embryonic development through critical functions in cell adhesion. In addition, Maspin is present in normal breast and prostatic epithelial cells although down regulated in the particular carcinomas. SERPINB5 impedes the growth, invasion, and metastatic properties of mammary tumors as well as the invasive ability of pancreatic ductal adenocarcinoma cells. SERPINB5 being a breast tumor suppressor gene is a significant marker of the disease progression in breast neoplasms. Furthermore, high expression of maspin is linked to squamous cell carcinoma in non-small-cell lung cancer. Moreover, maspin expression has been directly linked with the biological aggressiveness of ovarian carcinoma. Maspin exhibits no serine protease inhibitory activity since it does not undergo the stressed to relaxed conformational transition typical of active serpins.

HSPB11 is a component of IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20. HSPB11 is detected in the placenta.

SRP14 is a ribonucleoprotein complex which mediates the directing of proteins to the endoplasmic reticulum. The “Alu domain” of SRP is comprised of the heterodimer of the SRP9 and SRP14 proteins that are bound to the 5' and 3' terminal sequences of SRP RNA. SRP9/14 binding may be critical to the transcription, maturation, nucleolus localization and transport of SRP RNA.

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.

GLIPR2 is linked to plant pathogenesis-related (PR-1) proteins, which are upregulated in reaction to pathogen attack. GLIPR2 is localized within lipid-enriched microdomains on the cytosolic side of the endomembrane system. GLIPR2 is closely attached to membranes and lacks the cytosol, though it lacks a membrane-spanning domain.

Proline-Serine-Threonine Phosphatase Interacting Protein 1 (PSTPIP1) which is a scaffold protein and a regulator of the actin cytoskeleton binds ABL1, PTPN18, WAS, CD2AP, and PTPN12. PSTPIP1 also binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. Mutations in PSTPIP1 are a cause of PAPA syndrome.

Ras-related protein Rab-6B (RAB6B) is a member of the Rab6 family of the small GTPase superfamily. The Rab6 subfamily consists of 3 different isoforms: Rab6A, Rab6A' and Rab6B. Both Rab6A and Rab6A' are ubiquitously expressed while Rab6B is mainly expressed in brain. Rab6 is a main regulator in the retrograde transfer from endosomes via the Golgi to the ER and may act in retrograde tansport in neuronal cells.