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Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated | PKSH033985

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SKU:
575-PKSH033985
Weight:
1.00 KGS
€720.00
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Description

Recombinant Human Siglec-10 (C-Fc-Avi) Biotinylated | PKSH033985 | Gentaur US, UK & Europe Disrtribition

Synonyms: SIGLEC10; MGC126774; PRO940; Siglec10; SLG2; sialic acid-binding Ig-like lectin 10; Siglec-10; siglec-like gene 2; Siglec-like protein 2; SLG2sialic acid binding Ig-like lectin 10 Ig-like lectin 7

Active Protein: Active protein

Activity: Biotinylated Recombinant Human Sialic Acid-binding Ig-like Lectin 10 is produced by our Mammalian expression system and the target gene encoding Met17­Thr546 is expressed with a Fc, Avi tag at the C-terminus.

Protein Construction: Biotinylated Recombinant Human Sialic Acid-binding Ig-like Lectin 10 is produced by our Mammalian expression system and the target gene encoding Met17­Thr546 is expressed with a Fc, Avi tag at the C-terminus.

Fusion Tag: C-Fc-Avi

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 86.9 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5-11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system. Siglec-G is the apparent ortholog of human Siglec-10. We describe here a novel member of the siglec protein family that shares a similar structure including five Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing two ITIM-signaling motifs. Siglec-10 was identified through database mining of an asthmatic eosinophil EST library. Siglec-10 binds sialated proteins and lipids in alpha 2, 3 or alpha 2, 6 linkage and shows a preference for GT1b gangliosides. This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell. When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals. The Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products.

Research Area: Tags & Cell Markers

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