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SLAMF1 is a member of the immunoglobulin gene superfamily and is involved in T-cell stimulation. The SLAMF1 protein is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes, and a fraction of B cells, and is swiftly induced on naive T cells after activation. There are probably 2 modes of SLAM signaling: one in which the inhibitor SH2D1A serves as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction functions.

There are several proteolytic fragments or specific domains of proteins that act as inhibitors of angiogenesis. These include fragments of plasminogen such as Angiostatin protein kringles 1-4 and kringles 1-5, Endostatin, Restin, PEX, the N-terminal fragment of prolactin, and the Nterminally truncated platelet factor. Angiostatin is a proteolytic protein fragment of plasminogen that is comprised of the first 4 kringle regions. Angiostatin k1-4 prevents the growth of endothelial cells, and its systemic administration inhibits the growth of primary carcinomas in mice. Angiostatin Kringles 1-3 segment has a larger inhibitory activity than the Angiostatin kringles 1-4 fragment. The protease-activated angiostatin kringles 1-5 is the most potent plasminogen fragment with over 50 times larger endothelial cell specific inhibitory activity. Angiostatin kringles 1-5 systemic administration inhibits growth of fibrosarcoma and significantly reduces neovascularization.
Angiostatin is an angiogenesis inhibitor in mouse serum and urine. Angiostatin is a 38 kDa protein fragment of the plasminogen composed of the 1st 4 kringle domains of plasminogen. Angiostatin K1-4 is also named plasminogen kringles 1-4 and PK1-4.
Angiostatin protein is manufactured by the protelytic cleavage of plasminogen by a serine protease from several prostate carcinoma cell lines. The manufacturing of angiostatin by pancreatic cancer cells can be inhibited by TGF-beta 1 along with plasminogen activator inhibitor type-1 (PAI1).

Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.

V-Ets Avian Erythroblastosis Virus E26 Oncogene 2 (ETS2) is a transcription factor that regulates genes involved in development and apoptosis. ETS2 is also a protooncogene which takes part in regulation of telomerase. ETS2 protein’s pseudogene is located on the X chromosome.

Calcipressin-3 (RCAN3) takes part in central nervous system development. RCAN3 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Overexpression of calcipressin-3 results in inhibition of calcineurin activity towards the nuclear factor of activated T-cells (NFAT) transcription factors and also downregulates NFAT-dependent cytokine gene expression in activated Jurkat T-cells. Highest expression takes place s in heart, skeletal muscle kidney, liver and peripheral blood leukocytes.

Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.

Mediator Complex Subunit 27 (MED27) is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, together with TFIID, is necessary for efficient activation by SP1. MED27 is a component of the Mediator complex, a coactivator involved in the regulated transcription of virtually all RNA polymerase II-dependent genes. MED27 protein is also a component of other multisubunit complexes such as the thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. The activation of MED27 gene transcription is a multistep process, which is triggered by factors that identify transcriptional enhancer sites in DNA.

Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.

PSMD9 is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. PSMD9 acts as a chaperone through the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex compilation, PSMD9 is part of an intermediate PSMD9:PSMC6:PSMC3 module, also called modulator trimer complex. PSMD9 is released during the further base assembly process.

Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

PSMB1 is part of the proteasome B-type family, also identified as the T1B family, that is a 20S core beta subunit. PSMB1 is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species.The main function of PSMB1 is its degradation activity of unnecessary or damaged proteins by proteolysis. PSMB1 is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with arg, phe, tyr, leu, and glu adjacent to the leaving group at neutral or slightly basic ph. the proteasome has an atp-dependent proteolytic activity.

Rab3A is a member of the small GTPase superfamily, Rab family. Rab3A is a small, Ras-like GTPase expressed in neuroendocrine cells, in which Rab3A is linked with secretory vesicle membranes and regulates exocytosis. Rab3A protein may have a role in neurotransmitter release by regulating membrane flow in the nerve terminal.

Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.

TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

Osteoclasts are multinucleated cells that resorb bone and are essential for bone homeostasis. OSCAR plays crucial roles in the regulation of the innate and adaptive immune responses.Unlike the other LRC members, OSCAR expression is found specifically in preosteoclasts or mature osteoclasts. OSCAR is an important bone-specific regulator of osteoclast differentiation. Multiple alternative splicing transcript variants encodes different isoforms have been found for this gene.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DL1 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, p58.1, cl-42, NKAT1, or KIR-K6), which recognizes class I MHC molecules (HLA-Cw2, -Cw4, -Cw5, and Cw6). The extracellular domain of KIR2DL1 was over expressed as insoluble protein aggregates (inclusion bodies).

Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

AKR7A2 participates in the detoxification of aldehydes and ketones. AKR7A2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. AKR7A2 is involved in producing the neuromodulator gamma-hydroxybutyrate (GHB). AKR7A2 has extensive substrate specificity. AKR7A2 shows NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2 reduces 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). AKR7A2 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A2 takes part in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.