Human Sialic Acid-Binding Ig-Like Lectin 7 (SIGLEC7) Protein
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Description
Human Sialic Acid-Binding Ig-Like Lectin 7 (SIGLEC7) Protein is a recombinant Human protein produced in a Mammalian cell expression system.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Sialic Acid-Binding Ig-Like Lectin 7 (SIGLEC7) |
| Host | Mammalian cells |
| Origin | Human |
| Observed MW | Molecular Weight: Calculated MW: 65.45 kDa Sequence Fragment: Met1-leu353 Tag: C-terminal Fc tag |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Size 2 | 1 mg |
| Form | Liquid |
| Tested Applications | ELISA, WB, SDS-PAGE |
| Buffer | 0.01 M PBS, pH 7.4. |
| Availability | Shipped within 5-12 working days. |
| Storage | Store at 2-8 °C if the entire vial will be used within 1 week. Aliquot and store at -20 °C for long-term storage. Avoid repeated freeze-thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q9Y286 |
| Alias | p75,QA79,AIRM1,CD328,AIRM-1,CDw328,D-siglec,SIGLEC-7,SIGLECP2,SIGLEC19P,p75/AIRM1,Adhesion inhibitory receptor molecule 1 |
| Background | Protein SIGLEC7 |
| Note | This product is for research use only. This product is shipped with ice packs. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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anti- SIGLEC7 antibody
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).
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Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) Antibody
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.
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Sialic Acid Binding Ig Like Lectin 7 (SIGLEC7) Antibody
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.
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