Human Sialic Acid-Binding Ig-Like Lectin 8 (SIGLEC8) Protein
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Description
Human Sialic Acid-Binding Ig-Like Lectin 8 (SIGLEC8) 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 8 (SIGLEC8) |
| Host | Mammalian cells |
| Origin | Human |
| Observed MW | Molecular Weight: Calculated MW: 66.00 kDa Sequence Fragment: Met1-Ala363 Tag: C-terminal Fc tag |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Size 2 | 1 mg |
| Form | Lyophilized Reconstitute in sterile water to produce a stock solution. |
| Tested Applications | ELISA, WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| 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 | Q9NYZ4 |
| Alias | SAF2,SIGLEC-8,SIGLEC8L,Sialoadhesin family member 2 |
| Background | Protein SIGLEC8 |
| 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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SIGLEC8 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2, 3-linked sialic acid. and also binds to alpha2, 6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. SIGLEC8 is expressed specifically on eosinophils. The protein contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in downmodulation of cellular responses. The phosphorylated ITIM motif binds to the SH2 domain of PTPN6/SHP-1. The SIGLEC8 gene belongs to the immunoglobulin superfamily.
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