Other Monoclonal Antibodies

Vitamin D3, also known as cholecalciferol, is a fat-soluble vitamin which takes a great part in maintaining bone health, immune function, and muscle strength. It is often called the sun vitamin as our body produces it naturally when our skin is exposed to UVB rays from sunlight.

HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

DNA repair protein complementing XP-A cells, (XPA), is a member of the XPA family. XPA protein takes a part in DNA excision repair. It Inductees repair by binding to damaged sites with different affinities depending on the photoproduct and the transcriptional state of the region. Defects in XPA is the reason of xeroderma pigmentosum complementation group A (XP-A), which is infrequent human autosomal recessive disease which characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight, also may cause to neurological abnormalities.

RASSF1A is a protein similar to the RAS effector proteins. Loss or altered expression of the RASSF1A gene has been linked to the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of the RASSF1A gene. The inactivation of the RASSF1A gene was found to be interconnected with the hypermethylation of its CpG-island promoter region. The RASSF1A protein was found to interact with DNA repair protein XPA. RASSF1A was also shown to inhibit the accumulation of cyclin D1, and thus induce cell cycle arrest.

CRADD is a 22kDa, widely-expressed cytosolic adaptor/signaling protein that induces cell apoptosis/cell death in numerous tissues. CRADD is a death domain (CARD) that recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes TNFR1A, RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.

CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation. CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus. CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation.

CRABP1 is a member of special carrier proteins for members of the vitamin A family. It is believed that CRABP1 has an essential role in retinoic acid-mediated differentiation and proliferation processes. Though, CRABP1 is structurally similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. CRABP1 is constitutively expressed and is thought to have different functions in the cell than the related CRABP2. CRABP1 forms a beta-barrel structure which accommodates hydrophobic ligands in its interior. Loss of CRABP1 function as a result of hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma. Furthermore, frequent methylation-associated silencing of CRABP1 is linked to esophageal squamous-cell carcinoma.

The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins are implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. WNT3A is a member of the WNT gene family. WNT3A is a protein which shows 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. The WNT3A gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region.

Cytochrome C Oxidase Subunit Va (COX5A) is a member of the cytochrome c oxidase subunit 5A family. COX (Cytochrome C Oxidase), which is the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced Cytochrome C to oxygen. The COX component is a heteromeric complex comprised of three catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits serve in electron transfer, and the nuclear-encoded subunits act in the regulation and assembly of the complex. COX5A is the heme A-containing chain of Cytochrome C Oxidase,which is the terminal oxidase in mitochondrial electron transport.

RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.

HAX1 associates with hematopoietic cell-specific Lyn substrate 1, which is a substrate of Src family tyrosine kinases. HAX1 also interacts with the product of the polycystic kidney disease 2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with the F-actin-binding protein, cortactin. It was earlier thought HAX1 is mainly localized to the mitochondria, however, recent studies indicate it to be localized in the cell body. Mutations in the HAX1 gene result in autosomal recessive severe congenital neutropenia, aka Kostmann disease.

Vps20-associated 1 homolog (VTA1) is a member of the VTA1 family. The VTA1 protein is involved in the endosomal multivesicular bodies (MVB) pathway. Furthermore, VTA1 is interacts with CHMP1B, CHMP2A, CHMP5, VPS4B, KIAA0174 (IST1) and possibly CHMP3. VTA1 is believed to be a cofactor of VPS4A/B, which catalyzes membrane-associated ESCRT-III assemblies. In addition, VTA1 is involved in the sorting and down-regulation of EGFR and also in HIV-1 budding.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.

MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.

RAC2 is a small signaling G protein/GTPase which is part of the RAS superfamily of small GTP-binding proteins which regulate cell growth, actin cytoskeletal organization, cell proliferation, survival, cell cycle progression, gene transcription rgulation and the activation of protein kinases. RAC2 cycles between an active gtp-bound and inactive gdp-bound state. In active state, RAC2 binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. RAC2 is involved in the regulation of the nadph oxidase.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Eschericia coli bacteria, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes.
Maltose binding protein MalE,MBP, is part of the maltodextrin transport system in E. coli. The maltodextrins diffuse through the LamB pore located in the outer membrane into the periplasm. The sugar is bound to MalE which prevents it to diffuse back outside. MalE passes the sugar to a complex of MalF and MalG in the cytoplasmic membrane where active tranport is mediated by the ATPase MalK. MBP molecular weight is 40,622 dalton. There are two domains in the protein with similar secondary structure (central pleated sheets are surrounded by helices) . The domains are connected by three bridges, between the domains is a deep groove in which the sugar is bound. All hydroxyl groups of the sugar are fixed by sidechains of the protein by hydrogen bonds. Some water molecules are part of the hydrogen bridge network.

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.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.

Coactosin-like protein (COTL1) is one of the numerous actin-binding proteins which regulate the actin cytoskeleton. COTL1 binds F-actin, it also interacts with 5-lipoxygenase, which is the first committed enzyme in leukotriene biosynthesis. COTL1 binds to F-actin in a calcium-independent way and has no direct effect on actin depolymerization.

Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).

RAB7A belongs to the Ras superfamily of small Rab GTPases. RAB7A connects with the RIPL effector protein to regulator membrane trafficking from early to late endosome and to lysosomes. RAB7A can also regulate growth receptor endocytic trafficking, degradation, maturation of phagosome and autophagic vacuoles.

Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in  sheet (-domain) and a smaller -helical domain (-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).

RAB5A is a member of RAS oncogene family. The small GTPase, RAB5A is a crucial regulatory component of the endocytic pathway. Activation of RAB5A is mediated by GDP-GTP exchange factors (GEFs) that generate the Rab5-GTP complex). RAB5A is required for the fusion of plasma membranes and early endosomes.

MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

Glycophorins A & B (GYPA &GYPB) are the main sialoglycoproteins of the human erythrocyte membrane which carry the antigenic determinants for the MN and Ss blood groups. Along with the M or N and S or s antigens which normally occur in all populations, approximately 40 related variant phenotypes were identified. These variants comprise all the variants of the Miltenberger complex and some isoforms of Sta, as well as Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. GYPA is significant for the function of SLC4A1 and is necessary for high activity of SLC4A1. GYPA is involved in translocation of SLC4A1 to the plasma membrane. GYPA is also a receptor for: the influenza virus, Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans and is also a receptor for Hepatitis A virus (HAV).

Cellular nucleic acid-binding protein (CNBP) is a nucleic-acid binding protein with seven zinc-finger domains, which has a preference for binding single stranded DNA and RNA. CNBP serves in cap-independent translation of ornithine decarboxylase mRNA, and also in sterol-mediated transcriptional regulation. The expansion of A CCTG in CNBP protein’s first intron results in myotonic dystrophy type 2.

c-Myc is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of c-Myc have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.

c-Myc is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of c-Myc have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.

VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

MAFK is a member of the bZIP family and Maf subfamily. Members from Maf family of basic region/leucine zipper (bZIP) transcription factors influence transcription in a positive or negative way, depending on their protein associate and the context of the target promoter. Small Mafs act as transcriptional repressors when they dimerize among themselves. Yet, they seem to function as transcriptional activators by dimerizing with other basic-zipper proteins and employing them to specific DNA-binding sites.

CLEC4E (MINCLE or CLECSF9), belongs to a diverse family of proteins which were originally defined by their ability to recognize a wide range of ligands of carbohydrate structure. MINCLE is expressed in macrophages subjected to several types of stress. CLEC4E has an important role in response to trehalose-6,6''-dimycolate (TDM) and activated by a synthetic analogue, trehalose dibehenate (TDB). It was reported recently that MINCLE is connected with an immunoreceptor tyrosine-based activation motif–containing Fc receptor γ chain (FcRγ) and functions as an activating receptor for damaged self- and non–self-pathogenic fungi.

Myeloid differentiation antigen Gr1 (Ly6G) is a GPI-anchored protein, which is briefly expressed on monocytes in the bone marrow. The level of the Ly6G expression in the bone marrow completely correlates with granulocyte differentiation and maturation. Ly6G ligation on murine neutrophils inhibits neutrophil recruitment, thus providing the first evidence of a function for the Ly6G molecule. Ly6G is seen primarily on neutrophils, also in a subgroup of eosinophils, differentiating pre-monocytes and plasmacytoid dendritic cells.

PSME1 is an interferon gamma (IFNG) inducible proteasome activator essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.

Myeloid differentiation antigen Gr1 (Ly6G) is a GPI-anchored protein, which is briefly expressed on monocytes in the bone marrow. The level of the Ly6G expression in the bone marrow completely correlates with granulocyte differentiation and maturation. Ly6G ligation on murine neutrophils inhibits neutrophil recruitment, thus providing the first evidence of a function for the Ly6G molecule. Ly6G is seen primarily on neutrophils, also in a subgroup of eosinophils, differentiating pre-monocytes and plasmacytoid dendritic cells.

CISD1 protein holds a CDGSH iron-sulfur domain and is known to bind a redox-active [2Fe-2S] cluster. CISD1 is restricted to the outer membrane of mitochondria and takes part in oxidation regulation.

LSM5 also known as LSM5 Homolog, U6 Small Nuclear RNA Associated belongs to the Sm protein family. This family is identified in a variety of organisms based on sequence homology. Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length which folds as a loop. In addition, the Sm-like proteins are thought to create a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. Among the diseases associated with LSM5 are spinal muscular atrophy, and muscular atrophy.

LSM2 is a member of the snRNP Sm proteins family. Sm-like proteins are branded in several organisms based on sequence homology with the Sm protein family. Sm-like proteins hold the Sm sequence motif that is made up of 2 regions separated by a linker of variable length which folds as a loop. The Sm-like proteins are believed to create a steady heteromer present in tri-snRNP particles, which are vital for pre-mRNA splicing. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA nad takes part in pre-mRNA splicing.