Biosimilar Antibodies
Beta2-adrenoceptor, Human, mAb 6H8, Hycult Biotech, HM2238
The monoclonal antibody 6H8 recognizes human beta2-adrenoceptor. The b -adrenoceptors can be divided into b1, b2, b3 and b4-adrenoceptors defined in terms of agonist potencies, b2-adrenoceptors displayed a higher selectivity for nor-adrenaline than for adrenaline. B2-receptors are mainly postsynaptic and are located on a number of tissues including blood vessels, bronchi, GIT, skeletal muscle, liver and mast cell. Activation results in vasodilatation, bronchodilation, relaxation of the GIT, glycogenolysis in the liver, tremor in skeletal muscle and inhibition of histamine release from mast cells.- Transduction is via G-proteins coupled to the intracellular second messenger adenylate cyclase. B-receptors are positively coupled to adenylate cyclase via activation of Gs G-protein, however activation of the b2-adrenoceptors results in stimulation and inhibition of adenylate cyclase. The b2-receptor selective agonists are widely used in the treatment of asthma and other related bronchospastic conditions. They are commonly used in the treatment of angina pectoris, cardiac arrhythmia and for the long-term treatment of patients who survive myocardial infarction. B-receptor antagonists have also been used as anti-hypertensive for a number of years. Beta -blockers have also proven useful in the treatment of conditions such as migraine, anxiety disorders, hyperthyroidism, alcohol withdrawal and when applied topically are useful in the treatment of glaucoma and ocular hypertension.
Host
Human
Reactivity
Applications
Conjugation
BPI, Human, ELISA kit, Hycult Biotech, HK314
The antimicrobial protein BPI (Bactericidal Permeability Increasing protein) is a 55 kDa protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airway disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21 kDa bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage against invasive pneumococcal disease by binding to the gram-positive bacterial pathogen, pneumolysin. In plasma of healthy individuals BPI is present at levels of <0.5 ng/ml, which increases approximately 10-fold during acute phase responses.
Host
Human
Reactivity
Applications
Conjugation
BPI, Human, mAb 3F9, Hycult Biotech, HM2041
The monoclonal antibody 3F9 reacts specifically with full length human natural and recombinant Bactericidal Permeability Increasing protein (BPI). The antimicrobial protein BPI is a 55 kDa protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airways disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21 kDa bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage against invasive pneumococcal disease by binding to the gram-positive bacterial pathogen, pneumolysin. The monoclonal antibody 3F9 recognizes only free BPI and does not interact with BPI that has formed a complex with LPS.
Host
Human
Reactivity
Applications
Conjugation
BPI, Human, mAb 4H5, Hycult Biotech, HM2042
The monoclonal antibody 4H5 reacts specifically with full length human natural and recombinant Bactericidal Permeability Increasing protein (BPI). The antimicrobial protein BPI is a 55 kDa protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airways disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21 kDa bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage against invasive pneumococcal disease by binding to the gram-positive bacterial pathogen, pneumolysin. The monoclonal antibody 4H5 recognizes only free BPI and does not interact with BPI that has formed a complex with LPS.
Host
Human
Reactivity
Applications
Conjugation
BPI, Human, pAb, Hycult Biotech, HP9022
The polyclonal antibody reacts specifically with full length human natural and recombinant Bactericidal Permeability Increasing protein (BPI). The antimicrobial protein BPI is a 55 kDa protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airways disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21 kDa bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage against invasive pneumococcal disease by binding to the gram-positive bacterial pathogen, pneumolysin. The polyclonal antibody recognizes only free BPI and does not interact with BPI that has formed a complex with LPS.
Host
Human
Reactivity
Applications
Conjugation
C1-INH, Human, clone 15/12, Hycult Biotech, HM2411
Mouse monoclonal antibody HM2411 recognizes human C1-inhibitor. The complement system plays important roles in both innate and adaptive immune response and can produce an inflammatory and protective reaction to challenges from pathogens before an adaptive response can occur. There are three pathways of complement activation. The classical pathway (CP) is initiated by Immune complexes; the lectin pathway (LP) by surface bound mannan binding lectin; and the alternative (AP) by all the surfaces that are not specifically protected against it. Each generates a C3 convertase, a serine protease that cleaves the central complement protein C3, and generates the major cleavage fragment C3b. The C3 and C5 convertases are enzymatic complexes that initiate and amplify the activity of the complement pathways and ultimately generate the cytolytic MAC (C5b-9). C1 inhibitor (C1-INH) is a heavily glycosylated single chain molecule of 500 AA. It inhibits multiple enzymes, including C1s&r of the CP and MASP-1&2 of the LP, plasmin in the fibrinolytic system and Factor XIIa&XIa of the contact and coagulation system. C1-INH is also called C1 esterase inhibitor, due C1s is often cleaved by synthetic esters in spectrophotometry. C1-INH plays an important role in suppression of inflammation and vascular permeability. C1-INH binding of C1 to the catalytic site of both C1r and C1s releases the latter two from the complex. As a result the activation of the complement system is blocked. Binding to MASP blocks function and thereby consumption of C2,3&4. C1-INH spares the AP, leaving part of the innate antibacterial defense intact. Besides, C1-INH can directly bind and neutralize LPS, inhibiting sepsis and endotoxin shock. C1-INH administration is the common treatment for hereditary angioedema (HAE). A disease commonly caused by heterozygous deficiency of C1-INH and leading to low levels of functional C1-INH and recurrent episodes of dermal and submucosal swelling. This is mediated by its ability to control activation of the contact system in inhibiting bradykinin generation and thereby control of vascular permeability.
Host
Human
Reactivity
Applications
Conjugation
C1-INH, Human, ELISA, Hycult Biotech, HK396
C1 Inhibitor (C1-INH) stands as a sentinel in immune regulation, orchestrating the delicate balance of our body’s defense mechanisms. As a master suppressor, C1-INH targets key enzymes across various immune pathways, safeguarding against unwarranted inflammation and preserving vascular stability. Its distinctive function in conserving the Alternative Pathway, while meticulously regulating the Classical and Lectin pathways, marks it as an integral component in immune homeostasis. In the clinical realm, C1-INH is pivotal in managing hereditary angioedema (HAE)—a condition marked by sudden, intense swelling. As a diagnostic marker, C1-INH is gaining recognition for its potential to detect early signs of MIS-C, SLE, and MS, heralding a new era in the proactive management of these complex conditions.
Host
Human
Reactivity
Applications
Conjugation
C1q, Human, ELISA kit, Hycult Biotech, HK356
C1q, a key player in the classical complement pathway, seamlessly bridges innate and adaptive immunity. As part of the C1 complex, along with C1r and C1s, it activates upon binding to antibody-antigen complexes. This vital function positions C1q as an essential mediator in immune response management. Beyond activation, C1q recognizes IgG or IgM antibodies, initiating classical pathway activation through critical conformational changes. Its ability to bind apoptotic cells enhances immune clearance, preventing overstimulation. Predominantly produced by macrophages and dendritic cells, C1q is pivotal in maintaining host defense and preventing autoimmune diseases like systemic lupus erythematosus (SLE). C1q deficiencies, whether genetic or from anti-C1q antibodies, impair apoptotic cell clearance, heightening SLE risk. This correlation is evident in conditions like proliferative glomerulonephritis and SLE flares, where C1q levels are notably low. The C1QA gene polymorphism, associated with reduced C1q levels, highlights its integral role in immune regulation. C1q’s significance extends to its diagnostic potential in understanding complex immune diseases, making it a vital biomarker in immunological research. .
Host
Human
Reactivity
Applications
Conjugation
C1q, Mouse, ELISA kit, Hycult Biotech, HK211
C1q forms together with C1r and C1s the C1 macromolecule, the first component of the classical complement pathway. The formation of an antibodyantigen complex (immune complex) is the principal way of activating the classical pathway of the complement system. C1q triggers the activation process when it docks onto antibodies within these immune complexes. In this way, C1q acts to bridge the innate and adaptive immune systems. Interaction of immune complexes with C1q induces a conformational change within the C1 complex, which results in activation of the classical pathway. C1q functions as recognition unit by binding to the heavy chain of IgG or IgM (Fc gamma and Fc micro) provided that the immunoglobulins are bound to their antigen. Furthermore, C1q can bind to apoptotic blebs, where it activates the classical complement pathway and mediates phagocytosis. As such, C1q promotes the clearance of apoptotic cells and subsequent exposure of auto-antigens, thereby preventing stimulation of the immune system. C1q is predominantly produced by macrophages but also by follicular dendritic cells, interdigitating cells and cells of the monocyte-macrophage lineage. C1q deficiency has a profound effect on host defense and clearance of immune complexes. Inherited C1q deficiency is also associated with the development of systemic lupus erythematosus (SLE). In the case of C1q deficiency, SLE is found in- 90% of reported cases. C1q plays a role in the prevention of- autoimmunity by facilitating the physiological clearance and processing of apoptotic debris. Absence of C1q may cause autoimmunity by impairment of the clearance of apoptotic cells.Anti-C1q autoantibodies deposit in glomeruli together with C1q but induce overt renal disease only in the context of glomerular immune complex disease. This provides an explanation why anti-C1q antibodies are especially pathogenic in patients with SLE. Low C1q levels are associated with proliferative glomerulonephritis (WHO class III and IV). Furthermore, C1q concentrations decrease prior to clinical manifestations of flares of the disease. Low C1q levels have also been shown to predict the histopathological outcome of lupus nephritis. A single nucleotide polymorphism in the C1QA gene results in decreased C1q serum levels and has been linked to photosensitive Lupus-specific skin disease, subacute cutaneous lupus erythematosus (SCLE).
Host
Mouse
Reactivity
Applications
Conjugation
C1q, Mouse, mAb 7H8, Hycult Biotech, HM1044
The monoclonal antibody 7H8 recognizes mouse CIq. Clq, a member of the ‘defense collagen’ family, is the first subcomponent of the Cl complex of the classical pathway of complement activation. Several functions have been assigned to the pattern recognition molecule Clq, which include antibody-dependent and independent immune functions like triggering of rapid enhanced phagocytosis resulting in efficient containment of pathogens or clearance of cellular debris, apoptotic cells and immune complexes , and is considered to be mediated by Clq receptors present on the effector cell surface. There remains some uncertainty about the identities of the receptors that mediate Clq functions. Some of the previously described Clq receptor molecules, such as gClqR and cClqR, now appear to have less of a role in Clq functions than in functions unrelated to Clq. Experiments with gene targeted homozygous Clq-deficient mice have suggested a role for Clq in modulation of the humoral immune response, and also in protection against development of autoimmunity. The first component of complement Cl is a complex of three glycoproteins – Clq, Clr, and Cls. Cls and Clr interact to form a Cazf-dependent tetrameric proenzyme complex, C lr,-C 1 s2, which makes contacts with the Clq collagen domain. Binding of Clq to immune complexes (IgG or IgM) via the gClq domain, is considered to induce a conformational change in the collagen region of Clq, which leads to the autoactivation of Clr which, in turn, activates Cls. The activated Cl complex then cleaves components C4 and C2 in the classical complement cascade.
Host
Mouse
Reactivity
Applications
Conjugation
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