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O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.

Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.

Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

Macrophage Scavenger Receptor 1, also known as MSR1 is a member of the class A macrophage scavenger receptors, which comprises three different types 1, 2 and 3 generated by alternative splicing. Furthermore, these receptors or isoforms are macrophage-specific trimeric integral membrane glycoproteins and have been implicated in many macrophage-associated physiological as well as pathological processes which include atherosclerosis, Alzheimer's disease, and host defense.

Metallothionein 3 (MT3) contains 3 zinc and 3 copper atoms per polypeptide chain and a minor amount of cadmium. MT3 inhibits survival and neurite formation of cortical neurons in vitro. MT3 also binds heavy metals.

RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.

CD33 is putative adhesion molecule of myelomonocytic-derived cells which mediates sialic-acid dependent binding to cells. CD33 prefers to bind to alpha-2,6-linked sialic acid. The sialic acid recognition site is masked by cis interactions with sialic acids on the same cell surface. In the immune response, CD33 perform as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatases through their SH2 domains which block signal transduction through dephosphorylation of signaling molecules. In addition, CD33 induces apoptosis in acute myeloid leukemia.

Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

SIL1 is localized to endoplasmic reticulum (ER). SIL1 is an N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. SIL1 acts as a nucleotide exchange factor for another unfolded protein response protein. Mutations in SIL1 are linked to Marinesco-Sjogren syndrome.

Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

Sialic acid-binding Ig-like lectin 6 isoform 1 (SIGLEC6) is a member of immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC6 mediates sialic-acid dependent binding to cells and binds to alpha-2, 6-linked sialic acid. The SIGLEC6 protein localizes in numerous compartments such as membrane fraction, extracellular region and so on. The SIGLEC6 receptor binds sialyl-TN glycans and leptin. Placental expression SIGLEC6 is upregulated in preeclampsia.

CD5 antigen-like (CD5L) participates in the regulation of the immune system. CD5L functions as an inhibitor of apoptosis. CD5L is expressed in the spleen, lymph node, thymus and bone marrow.

Ureaplasma urealyticum parvum is a pathogenic mycoplasma localized in genito-urinary tracts, Ureaplasma urealyticum parvum is one of the smallest free living organisms and the only organism expressing human immuno-globulin A1 protease to decompose human protective antibody. Ureaplasma parvum is realted with various diseases, causing male urethritis, pyelonephritis, chorioamnionitis, pelvic inflammation, infertility via placental inflammation and abnormal outcomes during the early infection of pregnancy via amniotic sac, other diseases include supperative arthritis, surgical infections, neonatal meningitis and neonatal disease. Lower respiratory infection is also very common for preterm infants and low birth weight baby. Which usually lead to bronco pulmonary dysplasia and congenital pneumonia, meningitis, and even death. MB antigen is considered as a major antigen of Ureaplasma parvum, it is preent in different clinical isolates.

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.

PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.

CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.

IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.