Active protein: YES.
Activity: Immobilized Human Siglec-15-mFc (Cat#CW59) at 2μg/ml (100 μl/well) can bind Anti-Human Siglec15 mAb. The ED50 of Anti-Human Siglec15 mAb is 23.2 ng/ml.
Protein Construction: Recombinant Human Sialic Acid-binding Ig-like Lectin 15 is produced by our Mammalian expression system and the target gene encoding Phe19-Thr263 is expressed with a mFc tag at the C-terminus.
Sequence: Phe19-Thr263.
Fusion tag: C-mFc.
Accession: Q6ZMC9.
Purity: > 90 % as determined by reducing SDS-PAGE.
Endotoxin: < 1 IEU/µg as determined by LAL test.
Mol Mass: 52.1 kDa.
AP Mol Mass: 50-70 kDa.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, 150mM NaCl, 0.3% Chaps, 5% Trehalose, pH 7.4.
Background: 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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