Description: A Rabbit Polyclonal antibody against Siglec-5/14 from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: A Rabbit Polyclonal antibody against Siglec-5/14 from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: Rabbit polyclonal to Siglec-5/14.

Description: Rat Monoclonal Siglec-H Antibody (Monoclonal, ABM2B55). Validated in WB and tested in Mouse.

Description: The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Description: siglec-9 (HGMW-approved symbol SIGLEC9) a member of the sialic acid-binding Ig-like lectin (Siglec) family, which belongs to the immunoglobulin superfamily (IgSF). SIGLEC9 shows a high degree of homology to many members of the siglec family, including siglec-7 (80%), siglec-8 (72%), siglec-5 (65%), and CD33 (64%). This high degree of homology is also conserved in the extracellular Ig-like domains. 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。Siglec-9 with a hydrophobic signal peptide, an N-terminal Ig-likeV-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail.

Description: The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Description: The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Description: The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Description: siglec-9 (HGMW-approved symbol SIGLEC9) a member of the sialic acid-binding Ig-like lectin (Siglec) family, which belongs to the immunoglobulin superfamily (IgSF). SIGLEC9 shows a high degree of homology to many members of the siglec family, including siglec-7 (80%), siglec-8 (72%), siglec-5 (65%), and CD33 (64%). This high degree of homology is also conserved in the extracellular Ig-like domains. 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。Siglec-9 with a hydrophobic signal peptide, an N-terminal Ig-likeV-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail.

Description: siglec-9 (HGMW-approved symbol SIGLEC9) a member of the sialic acid-binding Ig-like lectin (Siglec) family, which belongs to the immunoglobulin superfamily (IgSF). SIGLEC9 shows a high degree of homology to many members of the siglec family, including siglec-7 (80%), siglec-8 (72%), siglec-5 (65%), and CD33 (64%). This high degree of homology is also conserved in the extracellular Ig-like domains. 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。Siglec-9 with a hydrophobic signal peptide, an N-terminal Ig-likeV-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail.

Description: Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8. Siglec-8 was first identified by CD33 homology screening of ESTs from a cDNA library generated from a patient diagnosed with idiopathic hypereosinophilic syndrome and was originally termed SAF-2 (sialoadhesin family 2). At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Two splice variants of Siglec-8 exist. The initially characterized form contains 431 amino acid residues in total, subsequently, a longer form of Siglec-8, initially termed Siglec-8L. Both forms of Siglec-8 are found in eosinophils and contain a V-set domain with lectin activity and two C2-type Ig repeat domains in the extracellular region.

Description: Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8. Siglec-8 was first identified by CD33 homology screening of ESTs from a cDNA library generated from a patient diagnosed with idiopathic hypereosinophilic syndrome and was originally termed SAF-2 (sialoadhesin family 2). At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Two splice variants of Siglec-8 exist. The initially characterized form contains 431 amino acid residues in total, subsequently, a longer form of Siglec-8, initially termed Siglec-8L. Both forms of Siglec-8 are found in eosinophils and contain a V-set domain with lectin activity and two C2-type Ig repeat domains in the extracellular region.

Description: The siglecs (sialic acid-binding Ig-like lectins) are a distinct subset of the Ig superfamily with adhesion-molecule-like structure. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Description: CD33 is a type I Lectin belonging to the Ig superfamily. CD33 contains an N terminal Ig like V type domain, which mediates sialic acid binding, followed by one Ig like C2 type domain, a transmembrane region and a cytoplasmic tail containing two conserved immunoreceptor tyrosine based inhibition motifs (ITIMs). Eleven human Siglecs have been characterized. Siglecs 5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. They are collectively referred to as CD33 related Siglecs. CD33 related Siglecs have differential expression pattern within the hematopoietic system. They are involved in the regulation of cellular activation within the immune system. Siglec 3 expression is restricted to cells of myelomonocytic lineage. Siglec3 recruits SHP1 and SHP2 to its ITIMs upon phosphorylation.