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Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.

Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.

Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.

Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.

Charged multivesicular body protein 3 (VPS24/CHMP3) is a member of the vacuolar sorting protein family and function as chromatin modifying proteins. VPS24 links directly with CHMP2 and CHMP4 for the disassembly of ESCRT-III complex in an ATP-dependent manner. During HIV-1 infection, the virus uses the ESCRT-III complex to mediate budding and exocytosis of viral proteins. VPS24 overexpression strongly hinders HIV-1 release.

VPS28 is a subunit of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. VPS28 is involved in endosomal sorting of cell surface receptors using a multivesicular body/late endosome pathway. VSP28 binding with the TSG101 may have significant roles in budding of Retroviruses, such as HIV-1 and Ebola virus.
VSP28 interacts with TSG101, VPS37B, VPS37C, FAM125A and FAM125B, and also with VPS36, this interaction mediates the association with the ESCRT-II complex. Furthermore it interacts with SNF8 and VPS25 and CEP55.

Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.

Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

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.

HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.

STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.

Borrelia is a part of the 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. Variable major protein like sequence E1 protein (VlsE1) is a borrelial surface protein which is the most sensitive protein for IgG antibody detection in all stages of Lyme disease.

CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

VAMP4 belongs to the synaptobrevin family who are involved in docking and/or fusion of vesicles with cell membrane. VAMP4 is enriched in the trans-Golgi network and may be a factor in the trans-Golgi network-to-endosome transport. VAMP4 is involved in the pathway which functions to eliminate an inhibitor (most likely synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. Synaptobrevins, syntaxins, and SNAP25 are the chief components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane.

Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted.

CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.