Biosimilar Antibodies
Alpha-Dystroglycan, Bovine, mAb 2238, Hycult Biotech, HM5010
Monoclonal antibody 2238 recognizes a glycoepitope unique to brain alpha-dystroglycan. Alpha-dystroglycan (alpha-DG), also known as dystrophin-associated glycoprotein, is a laminin-binding protein of ~156 kDa (including glyco-groups). Alpha-DG is a component of the dystroglycan complex, which is involved in early development, morphogenesis and in the pathogenesis of muscular dystrophies. Alpha- and beta-DG are encoded by a single gene and are derived from a precursor polypeptide by posttranslational cleavage. Beta-DG is an integral membrane protein, whereas alpha-DG is membrane-associated through its noncovalent interaction with the extracellular domain of beta-DG. The alpha- and beta-DGs provide important physical linkages between components of basement membranes and cytoplasmic proteins that bind to the actin cytoskeleton. Alpha-DG is a heavily glycosylated, mucin-like protein anchored on the extracellular surface of the myotube, where it may provide linkage between the sarcolemma and extracellular matrix (ECM). Alpha-DG is expressed in a variety of fetal and adult tissues. Tissue-specific glycosylation modifies the laminin specificity of alpha-DG. The muscle and nonmuscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Alpha-DG has been shown to colocalize with laminin in skeletal and cardiac muscle and a number of other cells including peripheral nerve, astrocytes, Purkinje neurons and kidney epithelium. Laminin-10/11 was shown to bind preferentially to brain alpha-DG. In Duchenne muscular dystrophy, the expression of alpha-DG is dramatically reduced leading to a loss of linkage between the sarcolemma and extracellular matrix, rendering muscle fibers more susceptible to necrosis. In the central nervous system, dystroglycan functions as a dual receptor for agrin and laminin-2 for instance in the Schwann cell membrane. Furthermore, defects in dystroglycan are central to the pathogenesis of structural and functional brain abnormalities seen in congenital muscular dystrophies (CMD). The monoclonal antibody 2238 is specific for a glycoepitope on brain bovine alpha-dystroglycan, which is absent on alpha-dystroglycan expressed in all other tissues.
Host
Bovine
Reactivity
Applications
Conjugation
Alpha-V/Beta-3 Integrin, Human, mAb BV3, Hycult Biotech, HM2034
The monoclonal antibody BV3 recognizes human alpha-V/beta-3 integrin present on human cells. Integrins are a superfamily of αβ heterodimeric cell-surface adhesion receptors found in many species. They are expressed on a variety of cells and mediate numerous physiological processes, including inflammation, migration, adhesion and proliferation. The β3 family consist of 2 members: αIIbβ3 and αvβ3, which mediate cell-cell and cell-ECM interactions and are important for cellularc migration, regulation of gene expression, cell survival, adhesion and differentiation. All processes which are involved in tissue development, angiogenesis and thrombosis. Each subunit consist of an extracellular domain, a single transmembrane segment and a cytoplasmic tail. They connect to the actin cytoskeleton via adaptor proteins that bind theircytoplasmic tails. Cell matrix adhesions also act as signaling units by their capacity to organize the actin cytoskeleton and to accumulate various signaling intermediates. Integrin αvβ3 was originally identified as the vitronectin receptor. Nevertheless, other ligands include fibrinogen, fibronectin, laminin, thrombospondin, Von Willebrand factor, tenascin, osteopontin and several forms of collagen. The interactions of integrin αvβ3 to those ligands is mediated by the RGD (Arg-Gly-Asp) sequence motif present in these proteins. Deregulation of β3 integrins is involved in e.g. autoimmune diseases, cardiovascular disorders, transplant rejection and tumorigenesis. In contribution to the latter, integrin αvβ3 contribute by supporting growth of small (tumor) blood vessels thereby potentiating the metastatic potential. Overexpression of integrin αvβ3 has been demonstrated in various tumors and activated endothelium.
Host
Human
Reactivity
Applications
Conjugation
Alternative Complement Pathway, Human, Assay, Hycult Biotech, HK3012
Features activity assay: Quantitative measurement of complement activation Working at low serum dilutions resulting in less false negative results High throughput and offers higher reproducibility in comparison to hemolytic assays Assay time less than 2 hours The complement system plays essential roles in both innate and adaptive immune responses, providing inflammatory and protective reactions against pathogens. Comprising a complex family of proteins and receptors found in circulation, tissues, and body fluids, it operates through three activation pathways: the classical pathway (CP), initiated by immune complexes; the lectin pathway (LP), activated by surface-bound lectins; and the alternative complement pathway (AP), triggered on surfaces lacking specific protection. The AP activation involves spontaneous C3 hydrolysis, binding to fB, forming C3(H2O)Bb convertase, which can be stabilized by properdin. Regulation comes from proteins like fH and fI. All pathways produce a C3 convertase, cleaving C3 into the major fragment C3b. These pathways converge with C3b initiating the second convertase, the C5 convertase, cleaving C5 into C5a and C5b, amplifying complement activity and forming the cytolytic MAC. Complement protein assessment, or complement activity, helps identify system abnormalities in vivo and screen for complement inhibitor function. Traditionally, haemolysis assays were used, but they’re challenging to standardize due to complications like opsonization and erythrocyte stability. ELISA-based assays, while more versatile, face challenges from serum dilutions. The HK3012 AP complement activity assay addresses these issues, offering a standardized approach. With the high costs of complement inhibitors and the need for more potent options, accurate measurement of complement activity is crucial. The HK3012 Alternative complement pathway activity assay evaluates complement function in vitro using LPS-coated wells to detect the in vitro-formed MAC complex with a C9 neo-epitope antibody. It begins with a serum dilution of 7.5x and uses a specific buffer to prevent pathway interference. Employing a 1.5-fold dilution combined with regression analysis, it accurately measures complement activity and inhibitory capacity. Go to our FAQ for more detailed information
Host
Human
Reactivity
Applications
Conjugation
Amyloid-beta (N-term), Human, mAb VU17, Hycult Biotech, HM2325
Antibody clone VU17, formerly known as αVU Aß 17, recognizes the N-terminus of human amyloid beta (i.e. in: Aβ1-38; Aβ1-39; Aβ1-40; Aβ1-42). Alzheimer disease (AD) is the most common form of dementia, and is characterized by the intra neuronal accumulation of the microtubule-associated protein tau (MAPT), and by extracellular deposits of amyloid beta (Aß) in the brain parenchyma. Aß deposits have different appearances, ranging from loosely organized to dense-cored, deposits, also called plaques, as well as deposits in the walls of small blood vessels. The Aβ peptides are a proteolytic cleavage product of the membrane bound amyloid precursor protein (APP), upon cleavage by APP-cleaving enzyme 1 (BACE1) and the γ-secretase complex. There are multiple cleavage sites in Aβ domain leading to various fragments of 36-43 amino acids in length. Aβ is produced by various cell types and is secreted into the interstitial fluid. Aß peptides are readily detectable in cerebrospinal fuid (CSF). Aβ terminating at residue 40 (Aβ40) being approximately 10 times more abundant than Aβ42. Whereas Aβ40 levels are unchanged in AD compared to control cases, Aβ42 levels in CSF are reduced. Therefore, Aβ42 levels and the Aβ42: Aβ40 ratio in CSF are of diagnostic importance. Assessment of Aβ levels and co-localization of Aβ with other factors and specific cell types in brain tissue is essential for investigating the molecular mechanisms underlying AD. Antibody VU17 detects all forms of Aβ deposits without the need for formic acid pre-treatment on paraffin sections and can be applied in a double staining strategy, making it suitable for investigating co-localization. Antibody VU17 is raised against synthetic Aβ1-17, and detects a region within the first six amino acids of the N-terminus of Aβ.
Host
Human
Reactivity
Applications
Conjugation
Arginase 1, Human, mAb 6G3, Hycult Biotech, HM2162
Monoclonal antibody 6G3 reacts specifically with Arginase I, the final enzyme in the urea cycle, which is responsible for the hydrolysis of arginine to urea and ornithine. The highest concentration of the enzyme is present in the liver in which the bulk of ureagenesis occurs. Two types of arginases are known: Arginase I and II. The cytosolic enzyme found primarily in liver is Arginase I, a 35 kD protein that circulates as trimer. Arginase II is exclusively located in the mitochondrion. Arginase I is next to the liver in man also expressed by mature fetal and adult red blood cells and activated monocytic cells. During inflammation induction of Arginase I by inflammatory cytokines in monocytic cells is considered to lead to a local depletion of arginine resulting in a microenvironment that prevents nitric oxide production and arginine dependent T cell function. Arginase II is expressed by kidney, nucleated red blood cells, brain, spinal cord, gastro-intestinal tract, mammary gland and prostate. Enhanced circulating Arginase I levels have been reported after surgery, following haemorrhage and in asthmatic patients. Measurement of circulating Arginase I has been used experimentally as rapid marker for liver injury.
Host
Human
Reactivity
Applications
Conjugation
Arginase 1, Human, mAb 9C5, Hycult Biotech, HM2163
Monoclonal antibody 9C5 reacts specifically with Arginase I, the final enzyme in the urea cycle, which is responsible for the hydrolysis of arginine to urea and ornithine. The highest concentration of the enzyme is present in the liver in which the bulk of ureagenesis occurs. Two types of arginases are known: Arginase I and II. The cytosolic enzyme found primarily in liver is Arginase I, a 35 kD protein that circulates as trimer. Arginase II is exclusively located in the mitochondrion. Arginase I is next to the liver in man also expressed by mature fetal and adult red blood cells and activated monocytic cells. During inflammation induction of Arginase I by inflammatory cytokines in monocytic cells is considered to lead to a local depletion of arginine resulting in a microenvironment that prevents nitric oxide production and arginine dependent T cell function. Arginase II is expressed by kidney, nucleated red blood cells, brain, spinal cord, gastro-intestinal tract, mammary gland and prostate. Enhanced circulating Arginase I levels have been reported after surgery, following haemorrhage and in asthmatic patients. Measurement of circulating Arginase I has been used experimentally as rapid marker for liver injury.
Host
Human
Reactivity
Applications
Conjugation
Arginase I, Human, mAb D1.2, Hycult Biotech, HM2324
Monoclonal antibody D1.2 reacts specifically with Arginase I, the final enzyme in the urea cycle, which is responsible for the hydrolysis of arginine to urea and ornithine. The highest concentration of the enzyme is present in the liver in which the bulk of ureagenesis occurs. Two types of arginases are known: Arginase I and II. The cytosolic enzyme found primarily in liver is Arginase I, a 35 kD protein that circulates as trimer. Arginase II is exclusively located in the mitochondrion. Arginase I is next to the liver in man also expressed by mature fetal and adult red blood cells and activated monocytic cells. During inflammation induction of Arginase I by inflammatory cytokines in monocytic cells is considered to lead to a local depletion of arginine resulting in a microenvironment that prevents nitric oxide production and arginine dependent T cell function. Arginase II is expressed by kidney, nucleated red blood cells, brain, spinal cord, gastro-intestinal tract, mammary gland and prostate. Enhanced circulating Arginase I levels have been reported after surgery, following haemorrhage and in asthmatic patients. Measurement of circulating Arginase I has been used experimentally as rapid marker for liver injury.
Host
Human
Reactivity
Applications
Conjugation
ASGPR, Rat, mAb 8D7, FITC, Hycult Biotech, HM3020F
The asialoglycoprotein (ASGP) receptor is a transmembrane hepatocellular surface carbohydrate binding glycoproteins lacking terminal sialic acid residues (asialoglycoproteins). Characterization of the ASGP receptor- revealed its functional role in the binding, internalization and transport of a wide range of glycoproteins, which have exposed galactose or N-acetylgalactosamine residues, via the process of receptor-mediated endocytosis (RME). The ASGP receptor can bind a variety of important plasma proteins including transport proteins (i.e. transferrin), enzymes such as alkaline phosphatase, immunoglobulins including IgA, apoptotic hepatocytes, fibronectin and platelets. Additionally, the expression of the ASGP receptor has been clinically correlated to the level of hepatic function that is lost during liver diseases related to cancer, viral hepatitis, and cirrhosis. The ASGP receptor consists of major and minor subunits, which in the rat were identified as rat hepatic lectin (RHL) 1 and RHL 2/3, with molecular weights of respectively 42, 49 and 54 kDa. The selective binding (calcium and pH depended) and uptake of terminal galactosyl bearing proteins requires the formation of hetero-oligomers between these major and minor forms. The total ASGP receptor population consisted of two functionally distinct receptor populations, designated State 1 and State 2, which were involved in the endocytosis and intracellular processing of ligands by different pathways. The monoclonal antibody 8D7 recognizes a subunit-specific epitope on RHL-1 of rat ASGPR. The monoclonal antibody 8D7 is cross reactive with human ASGPR.
Host
Rat
Reactivity
Applications
Conjugation
ASGPR, Rat, mAb 8D7, Hycult Biotech, HM3020
The asialoglycoprotein (ASGP) receptor is a transmembrane hepatocellular surface carbohydrate binding glycoproteins lacking terminal sialic acid residues (asialoglycoproteins). Characterization of the ASGP receptor- revealed its functional role in the binding, internalization and transport of a wide range of glycoproteins, which have exposed galactose or N-acetylgalactosamine residues, via the process of receptor-mediated endocytosis (RME). The ASGP receptor can bind a variety of important plasma proteins including transport proteins (i.e. transferrin), enzymes such as alkaline phosphatase, immunoglobulins including IgA, apoptotic hepatocytes, fibronectin and platelets. Additionally, the expression of the ASGP receptor has been clinically correlated to the level of hepatic function that is lost during liver diseases related to cancer, viral hepatitis, and cirrhosis. The ASGP receptor consists of major and minor subunits, which in the rat were identified as rat hepatic lectin (RHL) 1 and RHL 2/3, with molecular weights of respectively 42, 49 and 54 kDa. The selective binding (calcium and pH depended) and uptake of terminal galactosyl bearing proteins requires the formation of hetero-oligomers between these major and minor forms. The total ASGP receptor population consisted of two functionally distinct receptor populations, designated State 1 and State 2, which were involved in the endocytosis and intracellular processing of ligands by different pathways. The monoclonal antibody 8D7 recognizes a subunit-specific epitope on RHL-1 of rat ASGPR. The monoclonal antibody 8D7 is cross reactive with human ASGPR.
Host
Rat
Reactivity
Applications
Conjugation
ATP7A, Mouse and Rat, pAb, Hycult Biotech, HP8040
Rabbit polyclonal antibody CT77 reacts with mouse and rat ATP7A. Copper is essential for human health and copper imbalance is a key factor in the aetiology and pathology of several neurodegenerative diseases. Copper uptake into cells is thought to be mediated by the plasma membrane protein CTR1. Metallochaperones also bind copper and target it to specific destinations within the cell. ATOX1 (HAH1) transfers copper to the copper-ATPases. Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B are evolutionarily conserved polytopic membrane proteins with essential roles in human physiology. The Cu-ATPases are expressed in most tissues, and their transport activity is crucial for central nervous system development, liver function, connective tissue formation, and many other physiological processes. These proteins have a dual role in cells, namely to provide sufficient amounts of essential intracellular copper and to mediate the excretion of excess of intracellular copper. ATP7A and ATP7B are members of a large family of P-type ATPases that are energy-utilizing membrane proteins functioning as cation pumps. They are called ‘P-type’ ATPases, as they form a phosphorylated intermediate during the transport of cations across a membrane. The domains involved in the catalytic cycle of the protein are the nucleotide-binding domain (N-domain), phosphorylation domain (P-domain), and activation domain (A-domain). ATP7A is anchored to a membrane through eight hydrophobic transmembrane domains, which form a channel for copper translocation through the membrane. At the N-terminus ATP7A has six metal-binding domains (MBD1–6) each with a consensus MTXCXXC motif. Copper binds to these domains in the reduced form, Cu(I). It is assumed that the two MBDs (MBD5 and MBD6) closest to the transmembrane domains are important for the functional activity of the protein, and at least one of these two sites is necessary for normal function of the protein. The first four metal-binding domains (MBD1–4) are thought to have a regulatory function. Interaction between ATP7A and the copper chaperone ATOX1 occurs through these domains. ATP7A is expressed in almost every organ except the liver where ATP7B is predominantly expressed. In concordance with this, copper is incorporated in ceruloplasmin by ATP7B in hepatocytes, while ATP7A is in charge in most other cell types in transporting copper to tissue-specific enzymes. The malfunctioning of copper homeostasis is demonstrated in Menkes disease in which the ATP7A gene is defective. Menkes disease results in copper accumulation in intestinal cells, placenta, mammary tissue and the kidneys and deficiency in the brain, liver and serum. This leads to disrupted neurological and connective tissue development, causing mental retardation and neurodegeneration and usually results in early childhood death. Disturbances in copper homeostasis are also associated with neurodegenerative disorders such as Parkinson’s and Alzheimer’s disease, age-related macular degeneration and prion-related disease. Polyclonal antiserum CT77, raised against the C-terminal end of ATP7A, recognizes the full length protein.
Host
Mouse/Rat
Reactivity
Applications
Conjugation
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