Search results

GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.

Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.

Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.

Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.

Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.

STIM1 is a type-1 transmembrane protein that is necessary for store-operated Ca(2+) entry, a process of extracellular Ca(2+) influx in response to the depletion of Ca(2+) stores in the endoplasmic reticulum (ER). STIM1 localizes predominantly to the ER; upon Ca(2+) release from the ER, STIM1 translocates to the ER-plasma membrane junctions and activates Ca(2+) channels. STIM1 is an adhesion molecule involved in early hematopoiesis by mediating attachment to stromal cells. STIM1 controls the survival and/or proliferation of b-cell precursors. STIM1 gene is one of several genes located in the imprinted gene domain of 11p15.5, a significant tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. STIM1 is involved in malignancies as well as early hematopoiesis, by mediating attachment to stromal cells. STIM1 is oriented in a head-to-tail configuration with the ribonucleotide reductase 1 gene (RRM1), with the 3' end of this gene situated 1.6 kb from the 5' end of the RRM1 gene.

Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. SERPING1 is also activating C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.

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.

Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.

FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.

ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.

SLAMF7 belongs to the CS2 family of cell surface receptors. SLAMF7 is a single-pass type 1 membrane protein, SLAMF7 Isoform 1 mediates NK cell activation via aSH2D1A-independent extracellular signal-regulated ERK-mediated pathway. SLAMF7 functions in lymphocyteadhesion. Furthermore, SLAMF7 can exert activating of inhibitory influences on cells of the immune system depending on cellular context as well as the availability of effector proteins.

SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

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, ?, ?, ?, ?, ?, ? and ? that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

Myxovirus Resistance 1, also known as MX1 is a guanosine triphosphate (GTP)-metabolizing protein which takes part in the cellular antiviral response. MX1 is induced by type I and type II IFN, and also antagonizes the replication process of some different RNA & DNA viruses. In addition, there is a related gene located adjacent to MX1 on chromosome 21, and there are multiple pseudogenes positioned in a cluster on chromosome 4.

Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

Vacuolar protein sorting-associated protein 26A (VPS26A) is a vital element of the retromer complex, which is required to recover lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Furthermore, VPS26A is essential in the regulation of transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Expression analysis in yeast and mammalian cells reveal that VPS26A interacts directly with VPS35 that functions as the core of the retromer complex.

Flagellin FliA (H), also known as RNA polymerase sigma factor for flagellar operon, Sigma F and Sigma-28, is a part of the FliA subfamily or sigma-70 factor family. This sigma factor controls the expression of flagella-related genes. Flagellin FliA (H) regulates the expression of genes involved in virulence. Flagellin FliA (H) is an initiation factors which endorses the attachment of RNA polymerase to specific initiation sites and are then released.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.