Bioactivity: Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind Inotuzumab (anti-CD22) (Ab176429) with the EC50 of 20.1 ng/mL. Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind bind Epratuzumab (ant
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rp169575-50μg
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Purity: ≥90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains. Eleven human Siglecs have been cloned and characterized. They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and the identified Siglecs 5 to 11. To date, no Siglec has been shown to recognize any cell surface ligand other than sialic acid, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Human Siglec-2, also known as B-cell antigen CD22 or B-lymphocyte cell adhesion molecule (BL-CAM), is a B-cell restricted glycoprotein that is expressed in the cytoplasm of progenitor B and pre-B cells and on the surface of mature B cells. Two distinct human Siglec-2/CD22 cDNAs that arise from differential RNA processing of the same gene have been isolated. The predominant Siglec-2/CD22 beta encodes an 847 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, six Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail with 4 immunoreceptor tyrosine-based inhibition motifs (ITIMs). The variant Siglec-2/CD22 alpha encodes a 647 aa polypeptide missing two Ig-like C2-type domains and has a truncated (23 aa) cytoplasmic tail. Siglec-2/CD22 is an adhesion molecule that preferentially binds alpha 2,6- linked sialic acid on the same (cis) or adjacent (trans) cells. Interaction of CD22 with trans ligands on opposing cells was found to be favored over the binding of ligands in cis. Besides its role as an adhesion molecule, Siglec-2/CD22 is a coreceptor that physically interacts with B-cell receptor (BCR) and is rapidly phosphorylated upon BCR ligation. It negatively regulates BCR signals by recruiting tyrosine phosphatase SHP-1 to its ITIMs. Phosphorylated Siglec-2/CD22 can also interact with other intracellular effector proteins such as Syk, PLC gamma, PI3 kinase and Grb-2, suggesting it may play a role in positive signaling.
Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind Inotuzumab (anti-CD22) (Ab176429) with the EC50 of 20.1 ng/mL. Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind bind Epratuzumab (ant
115.2 kDa, under reducing conditions; 106.3 kDa, under non-reducing conditions
Images
Recombinant Human Siglec-2/CD22 Protein (rp169575) - ELISA Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind Inotuzumab (anti-CD22) (Ab176429) with the EC50 of 20.1 ng/mL.
Recombinant Human Siglec-2/CD22 Protein (rp169575) - ELISA Immobilized Recombinant Human Siglec-2/CD22 Protein (rp169575) at 1.0 μg/mL can bind bind Epratuzumab (anti-CD22) (Ab175532) with the EC50 of 207.0 ng/mL.
Recombinant Human Siglec-2/CD22 Protein (rp169575) - SDS-PAGE 3 μg/lane of Recombinant Human Siglec-2/CD22 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 115.2 kDa under reducing conditions and 106.3 kDa under non-reducing conditions.
Product Specifications
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 1.0 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilu
Storage Temp
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20°C for 1 year. Avoid freeze / thaw cycle.
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