2μg（R: reducing conditions）
Human SIGLEC7 Protein, His tag
Human SIGLEC7 Protein, His tag
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Product Details
Product Details
Product Specification
| Species | Human |
| Synonyms | Sialic acid-binding Ig-like lectin 7, Siglec-7, Adhesion inhibitory receptor molecule 1 (AIRM-1), CDw328, D-siglec, QA79 membrane protein, p75, CD328, AIRM1 |
| Accession | Q9Y286 |
| Amino Acid Sequence | Protein sequence (Q9Y286, Gln19-Leu353, with C-His tag) QKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRAGNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDAGRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLEGQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEFTCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLL |
| Expression System | HEK293 |
| Molecular Weight | Predicted MW: 38.6 kDa Observed MW: 55-70 kDa |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | with C-His tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4. |
| Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. |
Background
Siglecs (Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid. They are found primarily on the surface of immune cells and are a subset of the I-type lectins. There are 14 different mammalian Siglecs, providing an array of different functions based on cell surface receptor-ligand interactions. Sialic acid-binding Ig-like lectin 7 is a protein that in humans is encoded by the SIGLEC7 gene. SIGLEC7 has also been designated as CD328. 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. 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.
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