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SIGLEC11 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q96RL6 |
|---|---|
| Clone Names | 2101909 |
| Gene ID | 114132 |
|---|---|
| Other Names | Sialic acid-binding Ig-like lectin 11, Sialic acid-binding lectin 11, Siglec-11, SIGLEC11 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1629a was selected from the N-term region of human SIGLEC11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SIGLEC11 |
|---|---|
| Function | Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,8-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may 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. |
| Cellular Location | Membrane; Single-pass type I membrane protein. |
| Tissue Location | Expressed by macrophages in various tissues including Kupffer cells. Also found in brain microglia |
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Provided below are standard protocols that you may find useful for product applications.
Background
SIGLECs are members of the immunoglobulin superfamily that are expressed on the cell surface. Most SIGLECs have one or more cytoplasmic immune receptor tyrosine-based inhibitory motifs (ITIM). SIGLECs are typically expressed on cells of the innate immune system, with the exception of the B-cell expressed SIGLEC6. Sequence analysis predicted that the 697-amino acid SIGLEC10 protein contains a signal peptide, an N-terminal V-set Ig-like domain and four C2-set Ig-like domains, five potential N-linked glycosylation sites, a transmembrane region, and a 126-residue cytoplasmic tail with 3 putative ITIMs. Northern blot analysis detected a major 3.0-kb SIGLEC10 transcript, with highest levels in spleen, lymph node, blood leukocytes, and appendix. Little or no expression was observed in pancreas, thyroid, and testis. Flow cytometric analysis demonstrated eosinophil-specific expression of SIGLEC10, but at a lower level than that of SIGLEC8. Expression was also detected on monocytes and a CD16-positive/CD56-negative natural killer-like lymphocyte population. After sialidase treatment, which is necessary for unmasking the sialic acid-binding site on SIGLECs interacting with cell surface sialic acids, cells expressing SIGLEC10 bound to red blood cells. Immunoprecipitation analysis indicated expression of a 100- to 120-kD monomeric protein, higher than the predicted molecular mass, suggesting that SIGLEC10 is glycosylated.
References
Clark, H.F., et al., Genome Res. 13(10):2265-2270 (2003).Angata, T., et al., J. Biol. Chem. 277(27):24466-24474 (2002).
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