Biosimilar Antibodies
C1s, Human, mAb M241, Hycult Biotech, HM2109
Monoclonal antibody M241 reacts with an epitope on human C protein activated C1s, a subcomponent of the first component of C (C1). Activated C1s is a glycosylated single-polypeptide zymogen of 85 kD. Activation of the proenzyme C1s occurs through cleavage by the active form of C1r. The activated protease, activated C1s, consists of a disulfide-linked H chain and a L chain. Activated C1s is a serine protease and its catalytic site is located in the L chain. Activation of the classical C pathway is triggered by activated C1s which cleaves C4 and C2 to form the C3 convertase, C4bC2a. The epitope recognised by the antibody M241 is domain IV and/or V of the gamma-domain of activated C1s. Monoclonal antibody M241 blocks C4 activation and C4 binding to activated C1s. The antibody binds specifically to the active centre of C1s.
Host
Human
Reactivity
Applications
Conjugation
Activated C3, Human, mAb bH6, Hycult Biotech, HM2168
Insights from the Monoclonal Antibody bH6 The complement system, a crucial component of innate immunity, relies significantly on the third complement component, C3. The activation of C3, central to the classical, alternative, and lectin pathways, plays a pivotal role in immune defense mechanisms. In this context, activated C3 becomes a focus of study, particularly its interaction with monoclonal antibodies like bH6. The Abundance and Regulation of C3 C3 stands out as the most abundant protein in the complement system, with serum protein levels around 1.3 mg/ml. Its synthesis is tissue-specific and responds to various stimulatory agents, underlining the regulated nature of activated C3 in immune responses. C3 Cleavage and the Specificity of bH6 The proteolysis of C3, resulting in its cleavage into components like C3a and C3b, is a critical step in its activation. Further cleavage of C3b into iC3b, C3c, C3dg, and C3f highlights the complex nature of this process. Notably, the monoclonal antibody bH6 is specific to the neo-epitope on C3b, iC3b, and C3c, but not on C3dg and C3f, offering a precise tool for studying activated C3. Conclusion Through its various forms and interactions, C3 remains a key area of research in understanding innate immunity. The use of monoclonal antibodies like bH6 to detect neo-epitopes on activated C3 fragments enhances our ability to quantify and understand the complement activation process, paving the way for better therapeutic strategies in immune-related disorders. Not sure which C3 to use? With numerous options available, it is essential to select the right antibody to ensure the success of your research. We designed a guide to assist you in making an informed decision: Go to our C3 researcher’s guide and choose the right antibody
Host
Human
Reactivity
Applications
Conjugation
Activated C3, Human, mAb I3/15, Hycult Biotech, HM2257
C3 itself is a pivotal 190 kD protein central to the complement system, integral to the classical, alternative, and lectin pathways of complement activation. Notably, its synthesis is tissue-specific and responds dynamically to various stimulatory agents. Being the most abundant complement system protein, with serum levels around 1.3 mg/ml, C3’s activation is a key event in immune response. Activation of C3, a critical step identified by the activated C3 antibody, involves its cleavage into C3a and C3b. C3a plays a vital role in mediating local inflammatory processes, with notable anaphylatoxic properties. It induces smooth muscle contraction, increases vascular permeability, and triggers histamine release from mast cells and basophils. Conversely, C3b attaches to immune complexes and undergoes further cleavage into iC3b, C3c, C3dg, and C3f. Collectively, these fragments are known as activated C3 (act. C3). The most significant function of these C3 fragments is their interaction with other immune cells. The neo-epitopes formed during activation, which the activated C3 antibody detects, are vital for understanding the complement cascade’s impact on the immune system. Monoclonal antibodies like I3/15, which target these neo-epitopes, have become essential tools for directly quantifying activation at different steps of the complement cascade. Studying the activated C3 antibody’s role in C3 activation is key for immune response insights and therapies. Not sure which C3 antibody to use? With numerous options available, it is essential to select the right C3 antibody to ensure the success of your research. We designed a guide to assist you in making an informed decision: Go to our C3 researcher’s guide and choose the right antibody
Host
Human
Reactivity
Applications
Conjugation
ADAMTS-13, Human, mAb 20A5, Hycult Biotech, HM2226
The monoclonal antibody 20A5 recognizes human ADAMTS-13, A Disintegrin And Metalloprotease with ThromboSpondin type 1 domain 13. ADAMTS-13 is produced by hepatic stellate cells and in smaller amounts by human endothelial cells, and is present in plasma at a concentration of approximately 1 ug/ml. ADAMTS-13 is a zinc-containing metalloprotease belonging to the ADAMTS family characterized by a protease domain, an adjacent disintegrin-like domain, one or more thrombospondin type 1 repeats, a cystein-rich domain and a typical spacer region. ADAMTS-13 is composed of a series of domains (amino to carboxy terminal): metalloprotease, disintegrin-like, central thrombospondin-1 (TSP-1), cysteine-rich, spacer, seven additional TSP-1 domains and two unique CUB domains. ADAMTS-13 has no hydrophobic transmembrane domain, and hence it is not anchored in the cell membrane. The apparent molecular weight is 170 or 190 kDa on non-reducing or reducing SDS-PAGE, respectively. ADAMTS-13 has an important function in haemostasis, where it catalyzes the cleavage of the peptide bond between tyrosine-1605 and methionine-1606 in the A2 domain of von Willebrand Factor (VWF), resulting in 2 electrophoretic reduced fragments of 176 and 140 kDa, respectively. This process renders large multimers less adhesive and hence less reactive in the setting of thrombus formation. ADAMTS-13 is therefore said to be a natural anti-thrombotic agent. Severe ADAMTS-13 deficiency is associated with systemic microvascular thrombosis in familial or acquired thrombotic thrombocytopenic purpura (TTP). The accumulation of non-cleaved large VWF multimers causes spontaneous systemic platelet aggregation blocking oxygen supply to vital organs. This life-threatening disorder can lead to ischemic disease with (multiple) organ failure. The monoclonal antibody 20A5 recognizes the central to C-terminal TSP-1 repeats 2 to 5 of ADAMTS-13 (amino acid 686-894).
Host
Human
Reactivity
Applications
Conjugation
Allergin-1, Mouse, clone TX83, Hycult Biotech, HM1143
Monoclonal antibody clone Tx83 recognizes mouse allergy inhibitory receptor-1 (Allergin-1; also known as mast cell antigen AG-32). It is an immune regulatory molecule predominantly expressed on mast cells, but also found on other myeloid cells like macrophages, dendritic cells and neutrophils. The receptor consist of an immunoreceptor tyrosine-based inhibitory motif (ITIM) like domain. It’s main function is to suppress IgE (FcεRI-) mediated degradation and TLR2- mediated signaling in mast cells. Thereby inhibiting production of cytokines and other inflammatory mediators. Allergin-1 is tyrosine phosphorylated and recruits SH2 phosphatases , such as SHP-1, SHP-2 or SHIP. Co-ligation with FcεRI decreases mast cell degranulation. Currently three isoforms of human allergin-1 are identified: allergin-1L, Allergin-1S1 & allergin-1S2. Mast cells play a pivotal role in allergic reactions in barrier tissues, like skin and intestinal mucosa. Allergin-1 is suggested to play a role in skin diseases like dermatitis, the autoimmune diseases such as SLE and airway hyperresponsiveness. In macrophages it is suggested to play a role by suppressing autoantibody production via the promotion of apoptotic cell clearance.
Host
Mouse
Reactivity
Applications
Conjugation
Alpha-1-antitrypsin, Human, ELISA kit, Hycult Biotech, HK387
The human alpha-1 antitripsin ELISA detects both the healthy monomeric form (M variant) and the disease associated polymeric forms (Z variants) of human alpha-1-antitrypsin with equal affinity. Alpha-1-antitrypsin is a member of the serine protease inhibitor (serpin) superfamily which are proteins known for their ability to inhibit proteases. It is the most abundant circulating protease inhibitor known. It mainly targets enzymes released by neutrophils, especially neutrophil elastase (NE) but also proteinase 3 (PR3) and Cathepsin G (CG). Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serpin superfamily. The best known is Alpha-1-antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). This severe autosomal dominant disorder causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. Due to this accumulation of polymers in hepatocytes, blood alpha-1 trypsin levels will decrease leading to chronic uninhibited tissue breakdown. This causes the degradation especially of lung tissue which will eventually lead to pulmonary emphysema. In addition, accumulation of polymers in hepatocytes causes liver diseases such as neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.
Host
Human
Reactivity
Applications
Conjugation
Alpha-1-antitrypsin, Human, mAb 2C1, Hycult Biotech, HM2289
The mouse monoclonal antibody clone 2C1 recognizes polymeric forms of human alpha-1-antitrypsin. Alpha-1-antitrypsin is the most abundant circulating protease inhibitor. Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serine protease inhibitor or serpin superfamily of proteins.1 The best known is a1-antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). The severe Z deficiency allele (Glu342Lys) causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. This causes neonatal hepatitis, cirrhosis, and hepatocellular carcinoma. Clone 2C1 recognizes polymers formed by Z α1-antitrypsin in vivo. It also recognizes polymers formed by the Siiyama (Ser53Phe) and Brescia (Gly225Arg) mutants, and the novel His334Asp shutter domain mutant of a1-antitrypsin that is associated with prolonged neonatal jaundice in a 6-week-old boy. These data show that Z and shutter domain mutants form polymers with a shared epitope.
Host
Human
Reactivity
Applications
Conjugation
Alpha-1-antitrypsin, Human, mAb 3C11, Hycult Biotech, HM2358
Antibody clone 3C11 recognizes both the healthy monomeric form (M variant) and the disease associated polymeric forms (Z variants) of human alpha-1-antitrypsin with equal affinity. Alpha-1-antitrypsin is a member of the serine protease inhibitor (serpin) superfamily which are proteins known for their ability to inhibit proteases. It is the most abundant circulating protease inhibitor known. It mainly targets enzymes released by neutrophils, especially neutrophil elastase (NE) but also proteinase 3 (PR3) and Cathepsin G (CG). Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serpin superfamily. The best known is alpha-1 antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). This severe autosomal dominant disorder causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. Due to this accumulation of polymers in hepatocytes, blood alpha-1 trypsin levels will decrease leading to chronic uninhibited tissue breakdown. This causes the degradation especially of lung tissue which will eventually lead to pulmonary emphysema. In addition, accumulation of polymers in hepatocytes causes liver diseases such as neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.
Host
Human
Reactivity
Applications
Conjugation
Alpha-1-antitrypsin, Human, pAb, Hycult Biotech, HP9063
The goat polyclonal antibody recognizes human alpha-1-antitrypsin. This protein is a member of the serine protease inhibitor (serpin) superfamily which are proteins known for their ability to inhibit proteases. It is the most abundant circulating protease inhibitor known. It mainly targets enzymes released by neutrophils, especially neutrophil elastase (NE) but also proteinase 3 (PR3) and Cathepsin G (CG). Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serpin superfamily. The best known is alpha-1 antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). This severe autosomal dominant disorder causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. Due to this accumulation of polymers in hepatocytes, blood alpha-1 trypsin levels will decrease leading to chronic uninhibited tissue breakdown. This causes the degradation especially of lung tissue which will eventually lead to pulmonary emphysema. In addition, accumulation of polymers in hepatocytes causes liver diseases such as neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.
Host
Human
Reactivity
Applications
Conjugation
Alpha-5 Integrin (Fibronectin-receptor), Human, mAb NKI-SAM1, Hycult Biotech, HM2126
Fibronectin receptor, also designated VLA-5, is a 130/150 kDa protein. The protein functions as a receptor for fibronectin and mediates binding of B and T lymphocytes to fibronectin. Fibronectin is an extracellular matrix glycoprotein that functions in cell adhesion and migration in wound healing, embryonic development and malignant transformation. The fibronectin receptor is expressed on monocytes and monocytoid cell lines, leukocytes, memory T cells, fibroblasts, platelets and muscle cells.
Host
Human
Reactivity
Applications
Conjugation
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