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Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated
Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated
Artikelnummer
ELSPKSH033985-100
Verpackungseinheit
100 µg
Hersteller
Elabscience Biotechnology
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Active protein: YES.
Activity: Immobilized Anti-Human Siglec10 mAb(Cat#NC035) at 1μg/ml (100 μl/well) can bind Biotinylated Human Siglec-10-Fc-Avi(Cat#CY47 ). The ED50 of Biotinylated Human Siglec-10-Fc-Avi(Cat#CY47 ) is 1.45 ng/ml.
Protein Construction: Biotinylated Recombinant Human Sialic Acid-binding Ig-like Lectin 10 is produced by our Mammalian expression system and the target gene encoding Met17Thr546 is expressed with a Fc, Avi tag at the C-terminus.
Sequence: Met17-Thr546.
Fusion tag: C-Fc-Avi.
Accession: Q96LC7.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Mol Mass: 86.9 kDa.
AP Mol Mass: 100-130 kDa.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Background: Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5-11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system. Siglec-G is the apparent ortholog of human Siglec-10. 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. Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides. This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell. When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals. 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.
Activity: Immobilized Anti-Human Siglec10 mAb(Cat#NC035) at 1μg/ml (100 μl/well) can bind Biotinylated Human Siglec-10-Fc-Avi(Cat#CY47 ). The ED50 of Biotinylated Human Siglec-10-Fc-Avi(Cat#CY47 ) is 1.45 ng/ml.
Protein Construction: Biotinylated Recombinant Human Sialic Acid-binding Ig-like Lectin 10 is produced by our Mammalian expression system and the target gene encoding Met17Thr546 is expressed with a Fc, Avi tag at the C-terminus.
Sequence: Met17-Thr546.
Fusion tag: C-Fc-Avi.
Accession: Q96LC7.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Mol Mass: 86.9 kDa.
AP Mol Mass: 100-130 kDa.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Background: Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5-11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system. Siglec-G is the apparent ortholog of human Siglec-10. 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. Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides. This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell. When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals. 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.
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Gernot Ensinger, M.Sc.
Laurent Haze
