SDS-PAGE gel of Biotinylated Human Siglec-5/CD170 Protein (Primary Amin 4044

Biotinylated Human Siglec-5/CD170 Protein (Primary Amine Labeling) 4044

$525.00 – $1,750.00

Summary

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

available size

Clear

SKU: 4044parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-hFc
purity	> 95% as determined by Tris-Bis PAGE
background	Group B Streptococcus (GBS) causes invasive infections in human newborns. the GBS β-protein attenuates innate immune responses by binding to sialic acid-binding immunoglobulin-like lectin 5 (Siglec-5), an inhibitory receptor on phagocytes.the polymorphism could influence the risk of prematurity among human fetuses of mothers colonized with GBS. This first functionally proven example of a paired receptor system in the Siglec family has multiple implications for regulation of host immunity.
molecular weight	The protein has a predicted MW of 73.1 kDa. Due to glycosylation, the protein migrates to 90-115 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 (Primary Amine Labeling) 4044

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
Group B Streptococcus (GBS) causes invasive infections in human newborns. the GBS β-protein attenuates innate immune responses by binding to sialic acid-binding immunoglobulin-like lectin 5 (Siglec-5), an inhibitory receptor on phagocytes.the polymorphism could influence the risk of prematurity among human fetuses of mothers colonized with GBS. This first functionally proven example of a paired receptor system in the Siglec family has multiple implications for regulation of host immunity.
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 60715Da
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.
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: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Target Relevance information above includes information from UniProt accession: O15389
The UniProt Consortium

Data

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

Biotinylated Human Siglec-5 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.