by-55

CD160 antigen is a Lipid-anchor that exists as a disulfide-linked homomultimer. CD160 contains one Ig-like V-type domain. The human CD160 precursor is a cysteine-rich, glycosylphosphatidylinositol-anchored protein of 181 amino acids with a single Ig-like domain. It is weakly homologous to KIR2DL4. CD160 is expressed in the spleen, peripheral blood, and small intestine. Its expression is tightly associated with peripheral blood NK cells and CD8 T lymphocytes with cytolytic effector activity. CD160 is a receptor showing broad specificity for both classical and non-classical MHC class I molecules.

CD160 (also Natural killer cell receptor BY55) is a 27 ‑ 30 kDa member of the Ig superfamily. In human, it is expressed principally on nonmyeloid hematopoietic cells. CD160 antigenis a receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247 CD3 zeta chain in activated T cells.

CD160 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 16.4 kDa and the accession number is O95971-1.

CD160 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 41.9 kDa and the accession number is O88875.

Expression system: E. coli
Length: 55-591, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 24-96, Partial
Activity: Not Tested

Placental growth factor is a protein that in humans is encoded by the PGF gene. It is a secreted protein and belongs to the PDGF VEGF growth factor family. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF‑1), 152 (PlGF‑2), and 203 (PlGF‑3) amino acids (aa) respectively. PlGF is mainly found as a variably glycosylated, secreted, 55 ‑ 60 kDa disulfide linked homodimer.The protein is a member of the VEGF (vascular endothelial growth factor) sub-family-a key molecule in angiogenesis and vasculogenesis, in particular during embryogenesis. The main source of PGF during pregnancy is the placental trophoblast. PGF is also expressed in many other tissues, including the villous trophoblast. PlGF (especially PlGF‑1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF‑2, like VEGF164 165, shows heparin‑dependent binding of neuropilin (Npn)‑1 and Npn‑2, and can inhibit nerve growth cone collapse. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic PlGF‑2 antibodies are being investigated for their ability to inhibit tumor growth and angiogenesis.

Expression system: HEK293 Cells
Length: 30-125, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 22-213, Partial
Activity: ELISA、SPR

Expression system: HEK293 Cells
Length: 22-213, Partial
Activity: ELISA

Expression system: HEK293 Cells
Length: 55-618, Extracellular Domain
Activity: Not Tested

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).

Expression system: HEK293 Cells
Length: 1-528, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-524, Partial
Activity: Cell Activity