Recombinant Human 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 ED50 for this effect is 0.03-0.15 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human Siglec-2/CD22 protein
Human Siglec-2 (Asp20-Arg687) Accession # CAA42006
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
101.9 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
122-127 kDa, reducing conditions
Publications
Read Publications using 1968-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 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 Human 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. 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 (1 ‑ 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.
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) (4). 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 (5). 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 (9). 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 (2, 7, 8).
Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
Crocker, P.R. and A. Varki (2001) Immunology 103:137.
Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
Wilson, G.L et al. (1991) J. Exp. Med. 173:137.
Stamenkovic, I. and B. Seed (1990) Nature 345:74.
Kelm, S. et al. (1994) Current Bio. 4:965.
Ravetch, J.V. and L.L. Lanier (2000) Science 290:84.
Wienands, Y.J. et al. (1999) J. Biol. Chem. 274:18769.
Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. 101:6104.
There are no reviews for Siglec-2/CD22 (1968-SL).
By submitting a review you will receive an Amazon e-Gift Card or Novus Product Discount.
Review with no image -- $10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen
Review with an image -- $25/€18/£15/$25 CAD/¥150 Yuan/¥2500 Yen
FAQs for Siglec-2/CD22 (1968-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.
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.
=
÷
Review this Product
Be the first to review our Recombinant Human Siglec-2/CD22 Fc Chimera Protein, CF and receive a gift card or discount.