目录号 | 产品详情 | 靶点 | |
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T1312 | Antibacterial Antibiotic | ||
Nafcillin sodium monohydrate (CL 8491) 是一种抗生素,是可逆的β-lactamase 抑制剂。它用于治疗由耐青霉素的葡萄球菌菌株引起的感染。 | |||
T62665 | |||
Antistaphylococcal agent 2 是一种抗葡萄球菌的治疗剂。 | |||
T61855 | |||
Antistaphylococcal agent 1 是一种抗葡萄球菌的治疗剂。 | |||
T39886 | |||
Antistaphylococcal agent 3 is an antistaphylococcal therapeutic agent. | |||
TP1699L | Others | ||
SEB Domain 144-153 acetate(210229-94-0 free base) 是葡萄球菌肠毒素 B 结构域氨基酸残基 163-172。它已被证明可抑制多种葡萄球菌肠毒素、SEA、SEE 和 TSST-1 的转胞吞作用。 | |||
T1235 | ribosome Antibacterial Antibiotic | ||
Lincomycin hydrochloride monohydrate (Lincomycin hydrochloride hydrate) 是一种窄谱抗生素, 具有与红霉素相似的效力, 对革兰氏阳性球菌的作用效果很好, 主要抑制细菌细胞蛋白质的合成。 | |||
T22297 | Antibiotic | ||
Clindamycin hydrochloride monohydrate(Clindamycin alcoholate)是一种口服蛋白质合成抑制剂,具有在金黄色葡萄球菌中以亚抑制浓度(sub-MICs)抑制毒力因子表达的能力。其抗性来源于50S核糖体亚基(23S rRNA)的抗生素结合位点通过酶促甲基化。此外,Clindamycin hydrochloride monohydrate能显著减少杀白细胞毒素(PVL)、毒性休克-葡萄球菌毒素(TSST-1)或α-溶血素(Hla)的产生。 | |||
T41142 | IL Receptor p38 MAPK MyD88 | ||
EM 163是一种 TIR-TIR 相互作用抑制剂,它是MyD88蛋白的TIR(Toll/白细胞介素-1受体)结构域拟态。EM 163针对IL-1受体中的TIR 结构域,阻断与MyD88的相互作用。EM 163抑制葡萄球菌肠毒素B(SEB)引起的体内炎症细胞因子的产生。EM 163能保护小鼠免受SEB 冲击引起的死亡。在体外的大鼠海马神经元中,EM 163阻断p38的激活和IL-1β对化学诱导的长期电位(LTP)引发的蛋白质合成的抑制作用。 | |||
TP1699 | |||
This peptide is Staphylococcal Enterotoxin B domain amino acid residue 163-172. It has been shown to inhibit transcytosis of multiple staphylococcal enterotoxins, SEA, SEE, and TSST-1. | |||
T27559 | |||
HT-61, a pyrroloquinolone antibiotic, is used potentially for the treatment of staphylococcal infections. |
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-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-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-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-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-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-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-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-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-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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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-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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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-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-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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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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