Search results

Type IV collagen is a major structural component of basement membranes. It is a multimeric protein composed of 3 alpha subunits, which are encoded by 6 different genes, alpha 1 through alpha 6. Each of these alpha subunits can form a triple helix structure with 2 other subunits to form type IV collagen. The Goodpasture syndrome is a condition in which autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are restricted basically to the non-collagenous C-terminal domain of the protein. There are numerous alternative transcripts that appear to be unique to the human COL4A3 and alternative splicing is limited to the six exons that encode this C-terminal domain. COL4A3 is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to the Alport syndrome are also situated within the exons that encode this C-terminal region. COL4A3 is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Several exons of COL4A3 are interspersed with exons of an uncharacterized gene which is on the opposite strand.

GAP43 is a phosphoprotein of the presynaptic membrane that takes part in synaptic reorganization and neural development. GAP43 is found in large quantities in neuronal growth cones all through the development and axonal regeneration. Additionally, GAP43 is involved in specific regions of the normal adult nervous system and has a vital part in the conservation mechanism of long-term potentiation (LTP).

EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

CXADR Like Membrane Protein or CLMP, part of the CTX family within the immunoglobulin superfamily, is a type 1 transmembrane peptide. CLMP is expressed in the placenta and small intensine, skeletal muscle, colon, lungs and heart. CLMP is located in junction complexes across endothelial and epithelial cells and can take part in cell adhesion. The protein has influence on development of obesity via adipocyte differentiation.

Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.

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.

Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which functions as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. GM2A participates in lipid metabolism. GM2A protein is localized in lysosomes. The GM2A protein forms a large binding pocket for a number of single chain phospholipids and fatty acids. GM2A demonstrates calcium-independent phospholipase activity. GM2A stimulates ganglioside GM2 degradation by presenting GM2 to beta-hexosaminidase A. The Beta-hexosaminidase A, along with GM2A, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A gene mutations result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease.

Proteasome subunit alpha type-2 (PSMA2) 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. PSMA2 is a 20S core alpha subunit of proteasome belonging to the peptidase T1A family. PSMA2 functions as a docking domain for the regulatory particles and exterior gates blocking unregulated access to the inner cavity.

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%.

lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).

MAP1LC3A takes part in formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver and skeletal muscle, but are absent in thymus and peripheral blood leukocytes.

LASP1 has a vital part in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation can additionally assist in regulation of actin-associated ion transport activities in the parietal cell and in several other F-actin-rich secretory epithelial cell types.

Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

Cysteine protease ATG4B (ATG4B) belongs to the autophagin protein family. Autophagy is the manner by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is vital for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. ATG4B is a cysteine protease necessary for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is then transformed to a smaller form (form II). Form II, with an exposed C-terminal glycine, is deemed to be the phosphatidylethanolamine (PE)-conjugated form, and is capable of binding to autophagosomes. Reduced levels of autophagy are seen in some malignant tumors; therefore autophagy may have a role in controlling the unregulated cell growth linked to cancer.

The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.

SARS Membrane protein is a membranal protein which plays a crucial role in the virus’ life cycle. This protein has 3 outer cell structural antigens, the envelope (E), membrane (M)and spike (S) antigens. SARS Membrane protein is essential to the process of assembly, budding, creation of the envelope and pathogenesis.

Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.

MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

Norrie Disease (NDP) is a secreted regulatory protein which activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. NDP takes part in retinal vascularization by acting as a ligand for FZD4 which signals through stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. NDP is involved in a pathway that regulates neural cell differentiation and proliferation and also in neuroectodermal cell-cell interaction.

A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.