Biotinylated Human Siglec-5/CD170 Protein 3098

$525.00 – $1,750.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Glu17-Thr434

SKU: 3098parent 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;> 95% as determined by SEC-HPLC
background	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. Siglec 5 is putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2, 3-linked and 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.
molecular weight	The protein has a predicted MW of 49.3 kDa. Due to glycosylation, the protein migrates to 70-80 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-5/CD170 Protein 3098

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
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. Siglec 5 is putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and 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.
Protein names Sialic acid-binding Ig-like lectin 5 (Siglec-5) (CD33 antigen-like 2) (Obesity-binding protein 2) (OB-BP2) (OB-binding protein 2) (CD antigen CD170)
Gene names SIGLEC5,SIGLEC5 CD33L2 OBBP2
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 cells. Binds equally to alpha-2,3-linked and 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.
Catalytic activity BINDING 119; /ligand="N-acetylneuraminate"; /ligand_id="ChEBI:CHEBI:35418"; /evidence="ECO:0000269\|PubMed:18022638"; BINDING 127; /ligand="N-acetylneuraminate"; /ligand_id="ChEBI:CHEBI:35418"; /evidence="ECO:0000269\|PubMed:18022638"; BINDING 129; /ligand="N-acetylneuraminate"; /ligand_id="ChEBI:CHEBI:35418"; /evidence="ECO:0000269\|PubMed:18022638"
Subellular location Membrane; Single-pass type I membrane protein.
Tissues Expressed by monocytic/myeloid lineage cells. Found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. Expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation.
Domain Co
Target Relevance information above includes information from UniProt accession: O15389
The UniProt Consortium

Data

HPLC of Biotinylated Human Siglec-5/CD170 Protein

The purity of Biotinylated Human Siglec-5 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Human Siglec-5/CD170 Protein

Biotinylated Human Siglec-5 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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.