Recombinant Cynomolgus 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 0.07-0.42 μg/mL.
|
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey Siglec-2/CD22 protein Cynomolgus Monkey Siglec-2/CD22 (Asp20-Arg687) Accession # EHH59463 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Asp20 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
102 kDa. 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 |
115-134 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
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 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Siglec-2/CD22 Fc Chimera Protein, CF
Background
Siglecs are sialic acid specific I‑type lectins that are characterized
by an extracellular domain (ECD) with an N‑terminal Ig‑like V-type domain
followed by varying numbers of Ig‑like C2-type domains (1, 2). 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. In humans, two distinct Siglec-2 cDNAs that arise from
differential RNA processing of the same gene have been isolated. The
predominant Siglec-2 (Isoform 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 four immunoreceptor tyrosine-based inhibition motifs (ITIMs) (3). The
variant Siglec-2 (Isoform CD22-alpha) encodes a 647 aa polypeptide missing two
Ig-like C2-type domains and has a truncated (23 aa) cytoplasmic tail (4).
Within the ECD, cynomolgus Siglec-2 shares 84%, 55%, and 56% aa sequence
identity with human, mouse, and rat Siglec-2, respectively. Siglec-2 is an
adhesion molecule that preferentially binds alpha 2,6- linked sialic acid on
the same (cis) or adjacent (trans) cells. Interaction of Siglec-2 with
trans ligands on opposing cells is found to be favored over the binding of
ligands
in cis (5). Consistent with a single ligand-binding region, the
first two N-terminal Ig-like domains mediated CD22 adhesion with lymphocytes,
neutrophils, monocytes, and erythrocytes (6). Besides its role as an adhesion
molecule, Siglec-2 is a co-receptor 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 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 (7, 8).
- Varki, A. and T. Angata (2006) Glycobiology 16:1R.
- Crocker, P.R. et al. (2007) Nat. Rev. Immunol. 7:255.
- Wilson, G.L et al. (1991) J. Exp. Med. 173:137.
- Stamenkovic, I. and B. Seed (1990) Nature 345:74.
- Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. 101:6104.
- Engel, P. et al. (1995) J Exp Med. 181:1581
- Ravetch, J.V. and L.L. Lanier (2000) Science 290:84.
- Wienands, Y.J. et al. (1999) J. Biol. Chem. 274:18769.
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