Recombinant Human Sialic acid-binding Ig-like lectin 15/Siglec-15/CD33L3 (C-mFC)

Cat.No.: CW59

Recombinant Human Sialic acid-binding Ig-like lectin 15 is produced by our Mammalian expression system and the target gene encoding Phe20-Thr263 is expressed with a mFc tag at the C-terminus.
Accession #:Q6ZMC9
Known as:Sialic acid-binding Ig-like lectin 15; Siglec-15; CD33 antigen-like 3; CD33L3
Lyophilized from a 0.2 μm filtered solution of PBS,150mMNacl,0.3%chaps,5% Trehalose, pH 7.4.
Quality Control
Purity:Greater than 95% as determined by reducing SDS-PAGE.
BioActivity:Immobilized Recombinant Human Siglec 15-mFc(Cat#CW59) at 5μg/ml (100 μl/well) can bind biotinylated Anti-Human Siglec 15 mAb(Cat#NC007).
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Human Siglec-15 is a transmembrane glycoprotein in the Siglec family. Siglecs are type I transmembrane proteins where the NH3+-terminus is in the extracellular space and the COO?-terminus is cytosolic. Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid. These lectins are placed into the group of I-type lectins because the lectin domain is an immunoglobulin fold. All Siglecs are extended from the cell surface by C2-type Ig domains which have no binding activity. Siglecs differ in the number of these C2-type domains. Human Siglec-15 consists of a 244 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 44 aa cytoplasmic domain. Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts

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