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PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.

CD160 antigen (CD160) is a human natural killer (NK)-cell-activating receptor which is also expressed on T-cell subsets. CD160 is a tumor-specific antigen known to mediate cellular activation signals in CLL, and is a novel target for therapeutic manipulation and monitoring of minimal residual disease. CD160 was identified as a T cell coinhibitory molecule which interacts with the herpesvirus entry mediator (HVEM) on antigen-presenting cells to deliver a potent inhibitory signal to CD4(+) T cells. CD160 expression is strongly associated with peripheral blood NK cells and CD8 T lymphocytes with cytolytic effector activity. CD160 is expressed on all intestinal intraepithelial lymphocytes. CD160 has a broad specificity for binding to both classical and nonclassical MHC class I molecules.

Trypanosoma cruzi, better known as T. cruzi, is a deadly parasite that causes Chagas’ disease. This disease is a chronic infection, which primarily affects the heart and nervous system, causing severe neurological disorders, as well as swelling or denervation of nervous tissue in the heart, colon and esophagus. Chagas’ disease often goes undiagnosed due to close association of symptoms to heart disease and a variety of other disorders. The organism can circulate in the blood of infected patients for many years after infection, and can lead to transfusion-acquired infections in blood recipients from these infected donors. Contaminated blood transfusions are suspected to be the primary way in which the parasite has been transmitted to industrialized countries.

Integrase is an enzyme produced by the HIV which enables its genetic material to be integrated into the DNA of the infected cell and is a key component in the pre-integration complex. HIV integrase contains 3 domains, an N-terminal HH-CC zinc fingerdomainwhich is partially responsible for multimerization, a central catalytic domain and a C-terminal domain. Both Central catalytic domain and C-terminal domains have been shown to bind both viral and cellular DNA. No crystal structure data exists with Integrase bound to its DNA substrates. HIV-1 integrase functions as a dimeror a tetramer. Additionally, several host cellular proteins interact with integrase and may facilitate the integration process.

Aldolase A (ALDOA) is a glycolytic enzyme, which catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ALDOA is found in the developing embryo and is produced in even greater amounts in adult muscle. ALDOA expression is repressed in the adult liver, kidney and intestine and similar to ALDOC levels in the brain and other nervous tissue. ALDOA deficiency has been linked with myopathy and hemolytic anemia.

Lymphotoxin-alpha (LT-alpha or LTA) belongs to the TNF ligand superfamily, which bind the same TNF receptor and mediate similar pleiotropic effect. LTA is a proinflammatory cytokine with important biological activity and immunomodulatory function and is known to influence a variety of cellular response. Furthermore, LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses, is involved in the formation of secondary lymphoid organs during development and has a role in apoptosis. LTA is highly inducible, secreted, and forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA, which is located within the MHC III region of chromosome 6, shows close relation to the HLA class I (HLA-B) and class II (HLA-DR) genes. Polymorphism in the LTA gene appears to contribute to infectious disease susceptibility and infection. Genetic variations in the LTA gene are linked to susceptibility to leprosy type 4 and psoriatic arthritis.

VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).

The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

HIV-2 protease is very significant in the life cycle of the HIV virus. It is expressed in the infected cells as a part of Gag-Pol polyprotein from which it is auto-catalytycaly released after formation of an immature viral particle. The enzyme subsequently cleaves the other parts of viral polyproteins resulting in the maturation of the virus. In HIV-infected patients the enzyme is subjected to intensive mutagenesis and mutants resistant to applied medicines are produced as a result of the selection pressure.

L1 Cell Adhesion Molecule (L1CAM) which is a cell adhesion receptor of the immunoglobulin superfamily takes part in nerve cell function. L1CAM is a neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. L1CAM takes part in cell migration, neurite outgrowth and myelination. Furthermore, L1CAM plays an important role in the dynamics of neuronal structure and function in the mature brain.

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.

DYNLL1 is a protein that cooperates with NOS1 causing NOS1 inhibition. Binding of DYNLL1 weakens NOS1 (Neuronal nitric oxide synthase) dimer, a conformation needed for activity, and it regulates several biologic processes through its effects on nitric oxide synthase activity. DYNLL1 is a ubiquitously expressed protein that demonstrates high expression in testis and moderate expression in brain.

PPA1 is a member of the PPase family. PPA1 catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Many biochemical pathways use the hydrolysis of PPi to two phosphate ions to make the reactions permanently irreversible. A prominent illustration of this phenomenon is the inorganic pyrophosphatase catalyzation in the hydrolysis reaction at the beginning of lipid degradation. Inorganic pyrophosphatase provides the motivation for the activation of fatty acids destined for oxidation by stimulating the rapid hydrolysis of pyrophosphate.

C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.

Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

MARCKS-related protein (MARCKSL1) which is a part of MARCKS family of PKC substrate is broadly used in the signal transduction studies as an indicator of PKC activation. MARCKSL1 plays a part in the coordination of membrane-cytoskeletal signaling events, including secretion, migration, phagocytosis and cell adhesion and is expressed in a variety of tissues with highest levels found in testis and uterus. Furthermore, MARCKSL1 serves as a regulator of Integrin activation and is thought to regulate Integrin-dependent signal transduction pathways, particularly those involved in macrophage spreading.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.

TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.

TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.