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TFPI is a protease inhibitor which controls the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process starts with the creation of a factor VIIa-TF complex, that proteolytically triggers additional proteases (factors IX and X) and eventually results in a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly located in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. A number of alternatively spliced transcript variants of this gene have are known, however the full-length nature of several of these variants were not yet established.

Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.

Pollen allergen Phl p 1 (PhI p 1) causes an allergic reaction in humans.

NF-kappa-B inhibitor-interacting Ras-like protein 1 (NKIRAS1) is a member of the small GTPase superfamily. NKIRAS1 is an unusual Ras-like protein which acts as a potent regulator of NF-kappa-B activity by thwarting the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, describing why NFKBIB is more resistant to degradation. NKIRAS1 functions by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.

The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.

The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

SRP54 is a 54-kDa subunit of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex which leads the translocation of newly synthesized secretory proteins from the polysome to the endoplasmic reticulum. SRP is composed of six polypeptides and a tRNA-like molecule known as 7SL RNA. SRP54 is a GTP-binding protein that directly binds the signal sequences of nascent secretory and membrane proteins. Anti-SRP autoantibodies take place in patients with an autoimmune chronic muscle inflammation called polymyositis. These auto-antibodies predominantly recognize the SRP54 subunit and in addition are able to immunoprecipitate several of the SRP subunits and the RNA component. Nearly 5% of myositis patients are positive for anti-SRP autoantibodies, increasing to 18% in the subgroup of Jo-1 autoantibody-negative patients. The classic 'anti-SRP syndrome' is a severe form of polymyositis in which the myositic inflammation is acute and aggressive onset, with common myalgias and cardiac involvement. Normally there is a poor reaction to therapy with a 5-year survival rate of about 25%.

Lipopolysaccharides (LPS) are a type of glycolipids on the outer cell wall of Gram-negative bacteria. Lipopolysaccharide binding protein (aka LBP) is a plasma protein which facilitates the diffusion of bacterial LPS (endotoxin). LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. LBP belongs to a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). The LBP gene is found on chromosome 20, directly downstream of the BPI gene. LBP catalyzes the transfer of LPS monomers from LPS aggregates to HDL particles, to phospholipid bilayers, and to a binding site on soluble CD14 (sCD14). sCD14 is capable of speeding up the transfer by receiving an LPS monomer from an LPS aggregate, and then yielding it to an HDL particle, therefore acting as a soluble "shuttle" for an insoluble lipid.

Fibronectin Leucine Rich Transmembrane Protein 2 or FLRT2 is a glycoprotein, part of the 3 FLRT glycoproteins (fibronectin, leucine rich repeat, transmembrane). This protein can be found in apparent areas of the brain and additional tissues. The genes of FLRT1 & FLRT3 extracellular domain has about 47% similarity to FLRT2. A domain of fibronectin in FLRT1, FLRT3 & FLRT2 can be bound to epidermal growth factor receptors.

Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.

Anterior gradient protein 3 homolog precursor (AGR3) is a secreted cytoplasmic protein that is involved in metastasis induction and p53 tumor suppressor inhibition. AGR3 may function as molecular marker and potential therapeutic target for hormone-responsive breast tumors.

Ribosomal Protein L35, also known as RPL35 is a ribosomal protein which is a component of the 60S subunit. Ribosomes are the organelles which catalyze protein synthesis, they consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and about 80 structurally different proteins. RPL35 is a member of the L29P family of ribosomal proteins. RPL35 is located in the cytoplasm. As typicaly for genes encoding ribosomal proteins, there are multiple processed pseudogenes of RPL35 dispersed through the genome.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.

THAP Domain Containing, Apoptosis Associated Protein 7 (THAP7) holds one THAP-type zinc finger. THAP7 is a chromatin-associated, histone tail-binding protein which represses transcription by recruiting HDAC3 and nuclear hormone receptor corepressors.

Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.

The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

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.

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.

Nedd4 Family Interacting Protein 1 (NDFIP1) is a part of a small group of evolutionarily conserved proteins having 3 ransmembrane domains. NDFIP1 is a possible target for ubiquitination by the Nedd4 family of proteins. NDFIP, which is a member of a family of integral Golgi membrane proteins, also modulates EGFR signaling through multiple pathways.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.