Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated

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SKU:
RPES6333
Product Type:
Recombinant Protein
Species:
Human

Description

Product Name:Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated
Product Code:RPES6333
Size:20µg
Species:Human
Expression Host:HEK293 Cells
Synonyms:SIGLEC10, MGC126774, PRO940, Siglec10, SLG2, sialic acid-binding Ig-like lectin 10, Siglec-10, siglec-like gene 2, Siglec-like protein 2, SLG2sialic acid binding Ig-like lectin 10 Ig-like lectin 7
Mol Mass:86.9 kDa
AP Mol Mass:100-130 kDa
Tag:C-Fc-Avi
Purity:> 95 % as determined by reducing SDS-PAGE.
Endotoxin Level:< 1.0 EU per μg of the protein as determined by the LAL method.
Bio Activity:Immobilized Anti-Human Siglec10 mAb at 1μg/ml (100 μl/well) can bind Biotinylated Human Siglec-10-Fc-Avi. The ED50 of Biotinylated Human Siglec-10-Fc-Avi is 1. 45 ng/ml.
Sequence:Met17­-Thr546
Accession:Q96LC7
Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Shipping:This product is provided as lyophilized powder which is shipped with ice packs.
Formulation:Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution:Please refer to the printed manual for detailed information.
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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