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UGDH is part of the UDP-glucose/GDP-mannose dehydrogenase family and is a widely expressed enzyme localized in the liver. UGDH transfers UDP-glucose to UDP-glucuronate and thus takes part in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated products are ordinary molecules of the extracellular matrix and participate in signal transduction, cell migration, and cancer growth and metastasis.

Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.

Human immunodeficiency virus type-1 (HIV-1) regulatory Tat protein plays an essential role in viral replication and infectivity. The HIV-1 TAT is a molecule of 86 aminoacids encoded by two exons. The product of the first exon is sufficient for the transactivation of the HIV-1 promoter. Biotin molecules can be coupled easily to either antigens (such as avidin, streptavidin, Fc binding proteins like Protein A or G) or antibodies and they can be used in a variety of detection systems.
Biotin can be conjugated to many proteins without significantly changing their biological activity. Biotin binds with high affinity to avidin, streptavidin and NeutrAvidin protein.
Every single protein can react with several molecules of biotin, each of which, in turn, can bind a molecule of avidin. This greatly increases the sensitivity of many assay procedures. The avidin-biotin interaction is the strongest known noncovalent biological interaction (Ka = 1015 M-1) between protein and ligand. The bound formation between biotin and avidin is very rapid and, once formed, withstands extremes of pH, organic solvents and other denaturing agents. The avidinbiotin complex can withstand up to 3 M guanidine•HCl. Biotin can be released by 8 M guanidine•HCl at pH 1.5, or by autoclaving.

Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.

HIV-1 Nef is anessential factor for efficient viral replication and pathogenesis and therefore is produced shortly after virus infection. HIV-1 Nef is also facilitates virus replication and enhances virions infectivity. Nef exerts pleiotropic effects: decreases cell surface CD4 antigen by interacting with the Src family kinase LCK, down-modulates surface MHC-I molecules and protects the infected cell from apoptosis in order to keep it alive until the next virus generation is mature. Nef protein bypasses host T-cell signaling byinducing a trascriptional program almost identical to that of anti-CD3 cell activation.

MSH6 deficiency result in hereditary non-polyposis colorectal cancer (Lynch syndrome). HNPCC is an autosomal, dominantly inherited disease linked with rise in cancer susceptibility. MSH6 is is known by its familial predisposition to premature onset colorectal carcinoma (crc).
MSH6 is involved in repairing DNA. MSH6 protein repairs mistakes that occure during DNA replication in preparation for cell division. The MSH6 protein bonds with MSH2 protein and form an active protein complex which recognizes specific parts on the DNA where mistakes have been made during DNA replication. MLH1-PMS2 protein complex, afterwards takes over with the repair. MSH6 gene is part of the set of the mismatch repair (MMR) genes.

A fusion tag called FLAG consists of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site. FLAG is specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody denoted as M1 binds the peptide in the presence of bivalent metal cations preferably Ca(+). Elution is effected by chelating agents. Another strategy is competitive elution with excess of free Flag Peptide. The FLAG peptide purifies and detects recombinant fusion proteins. FLAG peptide is useful in Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure, and protein localization. Flag peptide is a hydrophilic tag which significantly improves the detection and purification of recombinant fusion proteins.

RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

APIP catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). APIP has an anti-apoptotic function and inhibits muscle ischemic impairment. APIP inhibits the cytochrome c-dependent and APAF1-mediated cell death.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.

Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

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.

Metadherin (MTDH) downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. MTDH activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Furthermore, MTDH promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a central component in tumor cell expansion. In addition, MTDH promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Metadherin also induces chemoresistance.

Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.

SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

DnaJ (Hsp40) Homolog, Subfamily C, Member 27 (DNAJC27) which contains one J domain is a part of the small GTPase superfamily. DNAJC27 is a GTPase which activates the MEK/ERK pathway and induces cell transformation when overexpressed.