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KRAS is part of the small GTPase superfamily. A single amino acid substitution is accountable for an activating mutation. KRAS participates in various malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma.

Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.

NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Protein Tyrosine Phosphatase 1B is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of INS signaling by dephosphorylating the phosphotryosine residues of INS receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to IFN stimulation.

Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It h

XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid

Synovial Sarcoma, X Breakpoint 1 (SSX1) is a member of a family of highly homologous synovial sarcoma X (SSX) breakpoint proteins. SSX proteins are localized to the nucleus and expressed in testis and some types of cancers and, hence, they are classified as C/T (cancer/testis) antigens. These proteins may serve as transcriptional repressors. SSX1 genes are involved in the t (X;18) translocation typically found in all synovial sarcomas. This translocation leads to the fusion of the synovial sarcoma translocation gene on chromosome 18 to one of the SSX genes on chromosome X. These hybrid proteins are most likely responsible for transforming activity.

Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.