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Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.

PPP1CA is one of the 3 catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase which is involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity is detected in the end stage of heart failure. Studies in both human and mice suggest that PP1 is a significant regulator of cardiac function. Mouse studies also propose that PP1 functions as a suppressor of learning and memory.

Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

FSCN1 is an actin-bundling protein that is responsible for rigidity to filopodial bundles to efficiently push the membrane forward during cytoskeleton remodeling and cell migration. FSCN1 takes part in the gathering of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. FSCN1 is absent from most normal epithelia though is upregulated in multiple forms of human carcinoma, where its expression associates clinically with a poor prognosis. FSCN1 expression is abundantly found in neurons, glial cells, and endothelial cells.

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.

Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture.

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

EPH Receptor A4 (Epha4), is a single-pass type 1 membrane protein which is a part of the protein kinase superfamily and ephrin receptor subfamily. Epha4 is a receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells mainly in the nervous system and in erythropoiesis.

FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

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.

Full-length recombinant human neutrophil MMP-8, latent form.
Matrix metalloproteinase 8 (MMP-8), degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.

Membrane Metalloendopeptidase, also known as MME is a zinc metallopeptidase which is expressed at the cell surface of various cells. MME degrades the amyloid beta peptide whose abnormal misfolding as well as aggregation in neural tissue has been implicated as the cause for Alzheimer's disease. MME is expressed in an extended range of tissues and is especially plentiful in the kidney. MME is also a common acute lymphocytic leukemia antigen which is a significant cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). MME is used in hematological diagnosis because it is expressed by early B, pro-B and pre-B lymphocytes, and also by lymph node germinal centers.

EPHB4 or Ephrin type-B receptor 4 is encoded by the EPHB4 gene in humans. The receptor and its ligands (the ephrins) take part in different developmental stages, mainly in the nervous system. EPHB4 and other Ephrin receptors are the biggest subgroup of the RTK receptors. EPHB4 binds to ephrin B2 and has a crucial part in the development of the vascular system.

Alpha-parvin (PARVA) belongs to the parvin family of actin-binding proteins. PARVA has a role in the regulation of cell adhesion, cytoskeleton organization, motility and survival as well as in ciliogenesis. Parvins are related with focal contacts and contain calponin homology domains which connect to actin filaments. PARVA is extensively expressed, with the highest levels in heart, skeletal muscle, kidney and liver.

Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

PEBP1 (Phosphatidylethanolamine binding protein 1) belongs to the phosphatidylethanolamine-binding protein family and a serine protease inhibitor that inhibits thrombin, neuropsin. PEBP1 plays a key modulatory part in several protein kinase signaling cascades. PKC phosphorylates PEBP1, resulting in the release of Raf-1 and activation of MEK and ERK. PEBP1 is expressed in many tissues and implicated in the regulation of such physiological processes as membrane biosynthesis, spermatogenesis, neural development, and metastasis suppression.
PEBP1 binds ATP, opioids and phosphatidylethanolamine, however it has lower affinity for phosphatidylinositol and phosphatidylcholine. PEBP1 may also be involved in the function of the presynaptic cholinergic neurons of the CNS. PEBP1 increases the production of choline acetyltransferase although not acetylcholinesterase. Furtheremore, PEBP1 functions in potentially sequestering toxic compounds, including locostatin which may have harmful effects on cells.
Loss of PEBP1 expression may have a significant role as prognostic marker in Gastrointestinal stromal tumors. In addition, PEBP1 is found differentially expressed in the Wernicke's Area from schizophrenia patients. PEBP1 is also, an invasion suppressor protein in nasopharyngeal carcinoma.

PEBP1 (Phosphatidylethanolamine binding protein 1) belongs to the phosphatidylethanolamine-binding protein family and a serine protease inhibitor that inhibits thrombin, neuropsin. PEBP1 plays a key modulatory part in several protein kinase signaling cascades. PKC phosphorylates PEBP1, resulting in the release of Raf-1 and activation of MEK and ERK. PEBP1 is expressed in many tissues and implicated in the regulation of such physiological processes as membrane biosynthesis, spermatogenesis, neural development, and metastasis suppression.
PEBP1 binds ATP, opioids and phosphatidylethanolamine, however it has lower affinity for phosphatidylinositol and phosphatidylcholine. PEBP1 may also be involved in the function of the presynaptic cholinergic neurons of the CNS. PEBP1 increases the production of choline acetyltransferase although not acetylcholinesterase. Furtheremore, PEBP1 functions in potentially sequestering toxic compounds, including locostatin which may have harmful effects on cells.
Loss of PEBP1 expression may have a significant role as prognostic marker in Gastrointestinal stromal tumors. In addition, PEBP1 is found differentially expressed in the Wernicke's Area from schizophrenia patients. PEBP1 is also, an invasion suppressor protein in nasopharyngeal carcinoma.

EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

EPHA2 is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors are implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. The EPHA2 gene encodes a protein that binds ephrin-A ligands. Mutations in the EPHA2 gene are the origin of certain genetically-related cataract disorders.

Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.