目录号 | 产品详情 | 靶点 | |
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TP1583 | |||
Affibody (affibody) ligands that are specific for the extracellular domain of human epidermal growth factor receptor 2 (HER2/neu) have been selected by phage display technology from a combinatorial protein library based on the 58 amino acid residue staphy | |||
T76570 | |||
PSM-β, 一种从表皮葡萄球菌中分离的活性肽,属于葡萄球菌毒素类似物,并且是酚溶性调节蛋白。该化合物展现出抑菌作用和低溶血性。 | |||
T63370 | |||
FtsZ-IN-2 是细菌细胞分裂蛋白 FtsZ 抑制剂,对 GTPase 的活性具有抑制作用。FtsZ-IN-2 表现出抗葡萄球菌作用,对 MSSA 和 MRSA 的MIC 值均为 2 μg/ml。 | |||
T79409 | |||
Antibacterialagent 154(compound 7)作为Fluoroquinolones类衍生物,适用于口服的抗菌治疗。它针对革兰氏阳性菌与阴性菌具有抑制作用,并在小鼠葡萄球菌败血症模型中显示出了体内效力。 | |||
T77111 | |||
Omodenbamab 是一种抗 SpA(葡萄球菌蛋白 A) 人源化单克隆抗体,KD 值为 0.0467 nM。Omodenbamab 通过靶向细胞壁部分蛋白 A (SpA) 来规避关键的 S. aureus 逃避机制。Omodenbamab 可用于 S. aureus 血流感染的研究。 | |||
T74803 | |||
Levonadifloxacin ((S)-(-)-Nadifloxacin; WCK 771),作为一种宽谱抗葡萄球菌药物,对甲氧西林敏感金黄色葡萄球菌(MSSA)及对甲氧西林耐药金黄色葡萄球菌(MRSA)显示出显著的抗菌活性,并能有效减少THP-1单核细胞对MRSA和MSSA菌株的吞噬。 | |||
T73824 | |||
Thymidine 3',5'-diphosphate (Deoxythymidine 3′,5′-diphosphate) tetrasodium,为一种选择性抑制剂,主要针对葡萄球菌核酸酶及含1的都铎结构域(SND1,MicroRNA调控复合体RISC亚基)和[3,5-2H2]酪氨酸核酸酶([3,5-2H2] tyrosyl nuclease)。此化合物还展示了抗肿瘤活性,并可在生化反应中作为催化剂使用。 | |||
T38178 | |||
Ristocetin A, a glycopeptide related to vancomycin, is an antibiotic produced by the microorganism Nocardia lurida[1]. Ristocetin A is currently in clinical use to treat bacterial infections [1]. Ristocetin A is an antibiotic which can be used to treat staphylococcal infections. The side effects of ristocetin A include thrombocytopenia and platelet agglutination. Ristocetin A has been used in two assays: the ristocetin cofactor assay and the ristocetin-induced platelet aggregation assay. These two assays could be used to diagnosis the von Willebrand disease and other bleeding disorders [2, 3]. The structural features of Ristocetin A are similar to vancomycin. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00820 | IgG1 Fc Protein, Human, Recombinant (C103S) | Human | HEK293 | ||
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (5 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-01191 | CD3 epsilon/CD3e Protein, Human, Recombinant (HEK293,His) | Human | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00125 | Recombinant Protein A | E. coli | |||
Staphylococcal Protein A, or SPA, is a type I membrane protein covalently linked to the cell wall of most strains of the Gram-positive bacterium Staphylococcus aureus. It has high affinity to IgG from various species, for instance human, rabbit and guinea pig but only weak interaction with bovine and mouse. Protein A interacts with antibodies through two distinct binding events: the “classical” binding site on the Fc portion of human IgG1, IgG2, and IgG4, and the “alternate” binding site found on the Fab portion of human IgG, IgM, IgA, and IgE that contain heavy chains of the VH3 subfamily. The most reported molecular weight of protein A from Staphylococcus aureus is about 42,000. The recombinant Streptococci protein A consists of 299 amino acids and has a predicted molecular mass of 33.8 kDa as estimated by SDS-PAGE.
Protein A consists of three regions: S, being the signal sequence that is processed during secretion; five homologous IgG binding domains E, D, A, B and C and a cell-wall anchoring regionXM. The truncated protein lacking region X has a molecular weight of about 31kD. The domains are independently capable to bind to the Fc-part of IgG1, IgG2 and IgG4, but shows only weak interaction with IgG3. In addition, all native protein A domains show comparable Fab binding. The binding site for the Fc part of the IgG molecule has been determined in a study of the B domain.
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TMPY-00616 | CD3 epsilon/CD3e Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02701 | CD3 epsilon/CD3e Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00105 | Recombinant Protein G | E. coli | |||
Protein G is a bacterial cell wall protein expressed at the cell surface of certain group C and group G Streptococcal strains.
It has affinity for both Fab- and Fc-fragments of human IgG by independent and separate binding sites. Binding to the Fc region of immunoglobulins from several species by a non-immune mechanism exhibits great affinity for almost all mammalian immunoglobulin G (IgG) classes, including all human IgG subclasses (IgG1, IgG2, IgG3 and IgG4) and also rabbit, mouse, and goat IgG. Protein G bound all tested monoclonal IgG from mouse IgG1, IgG2a, and IgG3, and rat IgG2a, IgG2b, and IgG2c. In addition, polyclonal IgG from man, cow, rabbit, goat, rat, and mouse bound to protein G, whereas chicken IgG did not. Protein G has also been shown to bind human serum albumin but at a site that is structurally separated from the IgG-binding region. Protein G shows a broader range of binding to IgG subclasses than staphylococcal protein A. This applies to polyclonal IgG from cow, rat, goat, human and rabbit sources as well as several of rat and mouse monoclonal antibodies. In contrast, protein A shows stronger interaction with polyclonal IgG from human, guinea-pig, pig, dog and mouse. Both proteins interacted with same relative strength to polyclonal rabbit IgG.
Protein G consists of nearly 600 amino acid residues. The carboxy-terminal half contains three immunoglobulin G (IgG)-binding domains which are referred to as domains I, II, and III or units C1, C2 and C3, each containing 55 amino acid residues with two 'spacers', of 16 amino acids, Dl and D2. Following the IgG-binding regions there is a region W, which most likely is involved in cell wall interactions. Domains in the NH2-terminal half of the protein have been found to bind human serum albumin (HSA).
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TMPH-03548 | Enterotoxin type G Protein, S. aureus (strain N315), Recombinant (His) | Staphylococcus aureus | Yeast | ||
Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
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TMPH-03545 | Enterotoxin type E Protein, S. aureus, Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03547 | Enterotoxin type G Protein, S. aureus (strain Mu50/ATCC 700699), Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
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TMPH-03546 | Enterotoxin type G Protein, S. aureus (strain N315), Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
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TMPH-03549 | Enterotoxin type H Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | Yeast | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
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TMPH-03541 | Enterotoxin type C-2 Protein, S. aureus, Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03551 | Exfoliative toxin A Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | E. coli | ||
Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS).
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TMPH-03539 | Enterotoxin type B Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | Yeast | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03542 | Enterotoxin type C-2 Protein, S. aureus, Recombinant | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03543 | Enterotoxin type C-3 Protein, S. aureus, Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03540 | Enterotoxin type B Protein, S. aureus, Recombinant (GST) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03544 | Enterotoxin type D Protein, S. aureus, Recombinant (His & SUMO) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of proinflammatory cytokines. In addition, induces B-cell proliferation and differentiation in the presence of T-cells. Causes also the intoxication staphylococcal food poisoning syndrome.
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TMPH-03538 | Enterotoxin type A Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | Baculovirus | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, waves of cellular activation, cytokine production, and migration into the lung tissue and airways occur via alphabeta T-cells. Causes also the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death (Probable).
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TMPH-03537 | Enterotoxin type A Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | E. coli | ||
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, waves of cellular activation, cytokine production, and migration into the lung tissue and airways occur via alphabeta T-cells. Causes also the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death (Probable).
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TMPH-03552 | Exfoliative toxin B Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | E. coli | ||
Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS).
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TMPY-05138 | IgG1 Fc Protein, Human, Recombinant (C103S), Biotinylated | Human | HEK293 | ||
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (5 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-06893 | IgG1 Fc Protein, Human, Recombinant (C103S, Avi), Biotinylated | Human | HEK293 | ||
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (5 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-05557 | Recombinant Protein A, Biotinylated | E. coli | |||
Staphylococcal Protein A, or SPA, is a type I membrane protein covalently linked to the cell wall of most strains of the Gram-positive bacterium Staphylococcus aureus. It has high affinity to IgG from various species, for instance human, rabbit and guinea pig but only weak interaction with bovine and mouse. Protein A interacts with antibodies through two distinct binding events: the “classical” binding site on the Fc portion of human IgG1, IgG2, and IgG4, and the “alternate” binding site found on the Fab portion of human IgG, IgM, IgA, and IgE that contain heavy chains of the VH3 subfamily. The most reported molecular weight of protein A from Staphylococcus aureus is about 42,000. The recombinant Streptococci protein A consists of 299 amino acids and has a predicted molecular mass of 33.8 kDa as estimated by SDS-PAGE.
Protein A consists of three regions: S, being the signal sequence that is processed during secretion; five homologous IgG binding domains E, D, A, B and C and a cell-wall anchoring regionXM. The truncated protein lacking region X has a molecular weight of about 31kD. The domains are independently capable to bind to the Fc-part of IgG1, IgG2 and IgG4, but shows only weak interaction with IgG3. In addition, all native protein A domains show comparable Fab binding. The binding site for the Fc part of the IgG molecule has been determined in a study of the B domain.
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TMPJ-00751 | IgG4 hFc Protein, Human, Recombinant (aa 99-326) | Human | Human Cells | ||
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as the antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (50 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-06605 | IgG1 Fc Protein, Mouse, Recombinant (C102S) | Mouse | HEK293 | ||
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (5 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-05124 | CD3 epsilon/CD3e Protein, Human, Recombinant (His), Biotinylated | Human | CHO | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00628 | CD3 epsilon/CD3e Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02690 | CD3 epsilon/CD3e Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05478 | CD3 epsilon/CD3e Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-06641 | CD3 epsilon/CD3e Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04867 | CD3 epsilon/CD3e Protein, Human, Recombinant (His) | Human | CHO | ||
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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