Recombinant Mouse Siglec-2/CD22 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Kelm, S. et al. (1994) Current Biology 4:965. The ED 50 for this effect is 0.08-0.4 µg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Siglec-2/CD22 protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
103 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
140-150 kDa, reducing conditions
Publications
Read Publications using 2296-SL in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Siglec-2/CD22 Fc Chimera Protein, CF
B-cell receptor CD22
BL-CAM
B-lymphocyte cell adhesion molecule
CD22 antigenMGC130020
CD22 molecule
CD22
sialic acid binding Ig-like lectin 2
Sialic acid-binding Ig-like lectin 2
Siglec2
Siglec-2
SIGLEC2FLJ22814
T-cell surface antigen Leu-14
Background
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 (1, 2). Eleven human Siglecs have been cloned and characterized. Among these are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2 and CD33/Siglec-3. 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. The cDNA of mouse Siglec-2 (also known as B-cell antigen CD22), encodes an 862 amino acid (aa) protein that contains a 21 aa signal peptide, a 681 aa extracellular region, a 19 aa transmembrane region and a 141 aa cytoplasmic tail (3, 4). The extracellular region contains one N-terminal V-type Ig-like domain followed by six Ig-like C2-type domains. The cytoplasmic domain has 3 immunoreceptor tyrosine-based inhibition motifs (ITIMs). Two splice forms exist, both showing deletions in the V-type Ig domain of 30 aa and 60 aa each. There are also two alleles in mouse that account for a difference of 10 aa in the extracellular region. The extracellular region of mouse Siglec-2 is 60% aa identity to human extracellular Siglec-2. Expression of mouse Siglec-2/CD22 generates a 140 kDa integral membrane glycoprotein that is limited to the B cell compartment of lymphoid tissues. Its expression is upregulated by LPS activtion (5, 6). 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 (7).
Nitschke, L. et al. (2001) Scand. J. Immunol. 53:227.
Crocker, P.R. and A. Varki (2001) Immunology 103:137.
Law, C-L. et al. (1993) J. Immunol. 151:175.
Wienands, Y.J. et al. (1999) J. Biol. Chem. 274:18769.
Wilson, G.L et al. (1991) J. Exp. Med. 173:137.
Torres, P.M. (1992) J. Immunol. 194:2641.
Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. 101:6104.
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FAQs for Siglec-2/CD22 (2296-SL). (Showing 1 - 1 of 1 FAQs).
I am interested in buying a CD22 antibody for fluorescence microscopy and FACS I red on your web page that you also offer to label your antibodies, if required, is that correct?
We do have the ability to perform custom conjugations on certain antibodies, including some to the CD22 protein. If you send me the conjugate you are interested in I can provide you with a quote.
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