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Human Siglec-5/CD170 Protein 4574

$210.00$700.00

Summary

  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Glu17-Thr434
SKU: 4574parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

O15389

express system

HEK293

product tag

C-His-Avi

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by 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 68-78 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human Siglec-5/CD170 Protein 4574

protein
Size and concentration
100, 500µg and liquid
Form
Liquid
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 with dry ice.
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
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
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
Tissues
TISSUE SPECIFICITY: 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
DOMAIN: Co
Target Relevance information above includes information from UniProt accession : O15389
The UniProt Consortium

Data

HPLC of Human Siglec-5/CD170 Protein
The purity of Human Siglec-5 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human Siglec-5/CD170 Protein
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.




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