Description: Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains. Eleven human Siglecs have been cloned and characterized. To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Human Siglec-7 encodes a 467 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail. Siglec-7 exists as a monomer on the cell surface and is expressed on natural killer cells, CD8+ T cells and monocytes. It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid.

Description: ELISA

Description: A competitive ELISA for quantitative measurement of Rat True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Rat True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Rat True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: Siglecs are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal, Ig-like V-type domain that mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains (2 to 17), a single transmembrane region, and a cytoplasmic tail. The siglecs can be broadly classified into two subgroups: siglecs-1, -2, and -4, and a siglec-3/CD33-related subgroup (siglecs-3, and -5 through -13 in primates) defined by sequence similarity and clustered gene localization. They are widely expressed on hematopoietic cells, often in a cell-type-specific manner, and siglec-4/MAG is a myelin component in Schwann cells and oligodendrocytes. Their ligands, sialic acids, are negatively charged monosaccharides found on cell-surface glycoproteins and glycolipids. Although siglec functions continue to be defined, most have intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIM), implicating them in the suppression of immunoreceptor signaling. They may also participate in cell/cell interactions or act as receptors for the entry of viral or bacterial pathogens.

Description: Siglecs are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal, Ig-like V-type domain that mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains (2 to 17), a single transmembrane region, and a cytoplasmic tail. The siglecs can be broadly classified into two subgroups: siglecs-1, -2, and -4, and a siglec-3/CD33-related subgroup (siglecs-3, and -5 through -13 in primates) defined by sequence similarity and clustered gene localization. They are widely expressed on hematopoietic cells, often in a cell-type-specific manner, and siglec-4/MAG is a myelin component in Schwann cells and oligodendrocytes. Their ligands, sialic acids, are negatively charged monosaccharides found on cell-surface glycoproteins and glycolipids. Although siglec functions continue to be defined, most have intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIM), implicating them in the suppression of immunoreceptor signaling. They may also participate in cell/cell interactions or act as receptors for the entry of viral or bacterial pathogens.

Description: A polyclonal antibody for detection of Siglec-5/14 from Human. This Siglec-5/14 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Siglec-5/14

Description: A polyclonal antibody for detection of Siglec-5/14 from Human. This Siglec-5/14 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Siglec-5/14

Description: A polyclonal antibody for detection of Siglec-5/14 from Human. This Siglec-5/14 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Siglec-5/14

Description: Available in various conjugation types.

Description: Available in various conjugation types.

Description: SIGLEC5 encodes a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. These cell surface lectins are characterized by structural motifs in the immunoglobulin (Ig)-like domains and sialic acid recognition sites in the first Ig V set domain. The sialic acid binding Ig like lectin 5 is a member of the CD33-related subset of Siglecs and inhibits the activation of several cell types including monocytes, macrophages and neutrophils. Binding of group B Streptococcus (GBS) to the encoded protein plays a role in GBS immune evasion.

Description: SIGLEC5 encodes a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. These cell surface lectins are characterized by structural motifs in the immunoglobulin (Ig)-like domains and sialic acid recognition sites in the first Ig V set domain. The sialic acid binding Ig like lectin 5 is a member of the CD33-related subset of Siglecs and inhibits the activation of several cell types including monocytes, macrophages and neutrophils. Binding of group B Streptococcus (GBS) to the encoded protein plays a role in GBS immune evasion.