Biotinylated Human Siglec-8 Protein 4787

$525.00 – $1,750.00

Summary

Expression: HEK293
Pure: Yes (SDS-PAGE)
Amino Acid Range: Met17-Ala363

SKU: 4787parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE
background	Siglec-8, also known as SAF, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains.Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells. Preferentially binds to alpha-2, 3-linked sialic acid. Also binds to alpha-2, 6-linked sialic acid.
molecular weight	The protein has a predicted MW of 40.7 kDa. Due to glycosylation, the protein migrates to 50-60 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Human Siglec-8 Protein 4787

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Siglec-8, also known as SAF, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains.Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells. Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid.
Protein names Sialic acid-binding Ig-like lectin 8 (Siglec-8) (Sialoadhesin family member 2) (SAF-2)
Gene names SIGLEC8,SIGLEC8 SAF2
Protein family Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
Mass 9606Da
Function Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells (PubMed:10625619, PubMed:10856141). Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface (PubMed:10625619). Recognizes simultaneously epitopes having a terminal N-acetylneuraminic acid (sialic acid) and an underlying 6-O-sulfated galactose. Preferentially binds to Gal-6-sulfated sialyl-Lewis X glycan epitopes (PubMed:27357658).
Catalytic activity BINDING 23; /ligand="a carbohydrate"; /ligand_id="ChEBI:CHEBI:16646"; /evidence="ECO:0000269\|PubMed:27357658, ECO:0007744\|PDB:2N7B"; BINDING 72..75; /ligand="a carbohydrate"; /ligand_id="ChEBI:CHEBI:16646"; /evidence="ECO:0000269\|PubMed:27357658, ECO:0007744\|PDB:2N7B"; BINDING 125; /ligand="a carbohydrate"; /ligand_id="ChEBI:CHEBI:16646"; /evidence="ECO:0000269\|PubMed:27357658, ECO:0007744\|PDB:2N7B"; BINDING 134..138; /ligand="a carbohydrate"; /ligand_id="ChEBI:CHEBI:16646"; /evidence="ECO:0000269\|PubMed:27357658, ECO:0007744\|PDB:2N7B"
Subellular location Membrane; Single-pass type I membrane protein.
Tissues Expressed specifically on red blood cells namely basophil, mast cells and eosinophils.
Domain Co
Target Relevance information above includes information from UniProt accession: Q9NYZ4
The UniProt Consortium

SDS-PAGE gel of Biotinylated Human Siglec-8 Protein

Biotinylated Human Siglec-8 on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.