SIGLEC7 (D-siglec) Antibody (C-term H422) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9Y286 |
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Other Accession | Q9NZQ1 |
Clone Names | 2102302 |
Gene ID | 27036 |
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Other Names | Sialic acid-binding Ig-like lectin 7, Siglec-7, Adhesion inhibitory receptor molecule 1, AIRM-1, CDw328, D-siglec, QA79 membrane protein, p75, CD328, SIGLEC7, AIRM1 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1633c was selected from the C-term region of human D-siglec . 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 | SIGLEC7 |
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Synonyms | AIRM1 |
Function | Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). 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. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro). |
Cellular Location | Membrane; Single-pass type I membrane protein. |
Tissue Location | Predominantly expressed by resting and activated natural killer cells and at lower levels by granulocytes and monocytes High expression found in placenta, liver, lung, spleen, and peripheral blood leukocytes |
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Background
SIGLECs are cell surface proteins of the Ig superfamily. Most SIGLECs have 1 or more cytoplasmic immune receptor tyrosine-based inhibitory motifs, or ITIMs. A large subgroup of SIGLECs share high homology with SIGLEC3 (CD33) and are localized to 19q13.4. The cDNA for the SLG gene encodes 2 variants, SLG-long (SLGL) and SLG-short (SLGS). The 595-amino acid SLGL protein contains a signal peptide and 2 V-set N-terminal Ig-like domains. The 477-amino acid SLGS protein has a weak signal sequence and, like most SIGLEC3-like SIGLECs, has only 1 V-set N-terminal Ig-like domain. Both variants contain 2 C2-set N-terminal Ig-like domains, a transmembrane domain, and a cytoplasmic tail with a putative ITIM and a putative SLAM-like tyrosine-based motif. The conserved arginine residue thought to be essential for sialic acid binding in other SIGLECs is replaced by a glutamine in SLGS and by a cysteine in SLGL. RT-PCR analysis detected high expression of both variants in spleen and small intestine, and SLGS was highly expressed in adrenal gland and SLGL was highly expressed in bone marrow.
References
Nicoll, G., et al., Eur. J. Immunol. 33(6):1642-1648 (2003).Alphey, M.S., et al., J. Biol. Chem. 278(5):3372-3377 (2003).Angata, T., et al., Glycobiology 10(4):431-438 (2000).Falco, M., et al., J. Exp. Med. 190(6):793-802 (1999).Nicoll, G., et al., J. Biol. Chem. 274(48):34089-34095 (1999).
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