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Human Siglec-10 Protein 4524

$315.00$1,050.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Met17-Thr546
SKU: 4524parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q96LC7

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Siglec-10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. It is also reported to bind to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24 also known as HSA (Heat-stable antigen).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.

molecular weight

The protein has a predicted MW of 59.2 kDa. Due to glycosylation, the protein migrates to 70-79 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-10 Protein 4524

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-10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. It is also reported to bind to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24 also known as HSA (Heat-stable antigen).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.
Protein names
Sialic acid-binding Ig-like lectin 10 (Siglec-10) (Siglec-like protein 2)
Gene names
SIGLEC10,SIGLEC10 SLG2 UNQ477/PRO940
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. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (PubMed:11284738, PubMed:12163025). Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (By similarity). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (PubMed:25450598). Plays a role in the control of autoimmunity (By similarity). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (By similarity).
Subellular location
[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; [Isoform 3]: Cell membrane; Single-pass type I membrane protein.; [Isoform 4]: Cell membrane; Single-pass type I membrane protein.; [Isoform 5]: Secreted.
Tissues
Expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation). Isoform 5 is found to be the most abundant isoform. Found in lymph node, lung, ovary and appendix. Isoform 1 is found at high levels and isoform 2 at lower levels in bone marrow, spleen and spinal chord. Isoform 2 is also found in brain. Isoform 4 is specifically found in natural killer cells.
Structure
Interacts with PTPN6/SHP-1 upon phosphorylation (PubMed:12163025). Interacts with NCF1 (By similarity). Interacts with CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated tissue damage immune response. Interacts with HMGB1; the interaction is dependent on CD24 (PubMed:19264983). Interacts with RIGI, CBL and PTPN11 (By similarity).
Post-translational modification
Phosphorylation of Tyr-667 is involved in binding to PTPN6.
Domain
Co
Target Relevance information above includes information from UniProt accession: Q96LC7
The UniProt Consortium

Data

HPLC of Human Siglec-10 Protein
The purity of Human Siglec-10 is greater than 95% as determined by SEC-HPLC.
SPR with Human Siglec-10 Protein
Human Siglec-10, His Tag captured on CM5 Chip via Anti-His Antibody can bind Human CD52, mFc Tag with an affinity constant of 15.9µM as determined in SPR assay (Biacore T200).
ELISA with Human Siglec-10 Protein
Immobilized Human Siglec-10, His Tag at 1µg/ml (100µl/Well). Dose response curve for Anti-Siglec-10 Antibody, hFc Tag with the EC50 of 2.3ng/ml determined by ELISA (QC Test).
HPLC of Human Siglec-10 Protein
The purity of Human Siglec-10 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human Siglec-10 Protein
Human Siglec-10 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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Protocols

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Documents

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