IgG2a Protein, Mouse, Recombinant, Biotinylated is expressed in HEK293 mammalian cells. The predicted molecular weight is 26.4 kDa and the accession number is P01863.

Immunoglobulin G (IgG) is a type of antibody composed of four peptide chains—two identical heavy chains and two identical light chains arranged in a Y-shape typical of antibody monomers.There are four IgG subclasses (IgG1, 2, 3, and 4) in humans, named in order of their abundance in serum. The IgG2a isotype was able to interact very efficiently with FcgammaR, and share approximately 64-78% amino acid sequence identity with IgG1 and IgG2b in the heavy chain constant region domains, CH1, CH2 and CH3, which cause the diffrence in the interaction with complement, NK and mast cells, induction or inhibition by specific cytokines, and ability to cross the placenta.

IgG2a Protein, Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 26.4 kDa and the accession number is P01863.

SIRPα is a type I transmembrane glycoprotein.It contains two Ig-like C1-type domains and one Ig-like V-type domain. Mouse SIRP alpha ECD shares 61%, 75%, 62%, 61%, and 59% aa sequence identity with human, rat, equine, bovine, and porcine SIRP alpha, respectively.SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.

CD200Fc, a chimeric molecule including the extracellular domain of CD200 and a murine IgG2a Fc region, regulates immune responses following engagement of a cell surface receptor, CD200R, expressed on cells of the myeloid and T cell lineage. A recent report focused attention on a family of CD200Rs, but concluded that only one member used CD200 as its ligand. CD200R1/CRTR2 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 29.7 kDa and the accession number is AAQ19772.

Interleukin-18 is a secreted protein and it belongs to the IL-1 family. IL-18 is a proinflammatory cytokine and produced by macrophages and other cells. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL-4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity. After stimulation with IL-18, natural killer (NK) cells and certain T cells release another important cytokine called interferon-γ (IFN-γ) or type II interferon that plays an important role in activating the macrophages or other cells.

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).

CD200Fc, a chimeric molecule including the extracellular domain of CD200 and a murine IgG2a Fc region, regulates immune responses following engagement of a cell surface receptor, CD200R, expressed on cells of the myeloid and T cell lineage. A recent report focused attention on a family of CD200Rs, but concluded that only one member used CD200 as its ligand. CD200R1/CRTR2 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 53.7 kDa and the accession number is AAQ19772.

CD200Fc, a chimeric molecule including the extracellular domain of CD200 and a murine IgG2a Fc region, regulates immune responses following engagement of a cell surface receptor, CD200R, expressed on cells of the myeloid and T cell lineage. A recent report focused attention on a family of CD200Rs, but concluded that only one member used CD200 as its ligand. CD200R1/CRTR2 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 29.7 kDa and the accession number is AAQ19772.

CD200Fc, a chimeric molecule including the extracellular domain of CD200 and a murine IgG2a Fc region, regulates immune responses following engagement of a cell surface receptor, CD200R, expressed on cells of the myeloid and T cell lineage. A recent report focused attention on a family of CD200Rs, but concluded that only one member used CD200 as its ligand. CD200R1/CRTR2 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 28.09 kDa and the accession number is XP_005548207.1.

Protein A is surface protein originally found in the cell wall of the bacteria Staphylococcusaureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two component system called ArlS-ArlR. Protein A binds the Fc region of various mammalian IgG subclasses including: Human IgG1, IgG2, IgG3 (weakly), IgG4 Mouse IgG1 (weakly), IgG2a, IgG2b, IgG3 SPA also binds IgG from monkey, rabbit, pig, guinea pig, dog, rat and cat. It also weakly binds to streptavidin.