Recombinant Rat Siglec-2/CD22 His-tag Protein, CF Summary
| Details of Functionality |
Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. The ED 50 for this effect is 0.6-5.4 μg/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived rat Siglec-2/CD22 protein Trp24-Gly690, with a C-terminal 6-His tag |
| Accession # |
|
| N-terminal Sequence |
Trp24 |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>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 |
|
| Theoretical MW |
76 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 |
98-114 kDa, under 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 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 with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 500 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 Rat Siglec-2/CD22 His-tag Protein, CF
Background
Sialic acid-binding immunoglobulin-like lectin 2 (Siglec-2), also known as B-cell receptor CD22 or B-lymphocyte cell adhesion molecule (BL-CAM), is a I-type (Ig-type) lectin belonging to the sialoadhesin subclass of the immunoglobulin superfamily (1). Fourteen human and nine mouse Siglecs have been characterized and are divided into 2 families: CD33 related and evolutionarily conserved (2, 3). The extracellular domain (ECD) of Siglecs 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 -3). The predominant form of human Siglec-2 contains a N-terminal Ig-like V-type domain, six Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail with six tyrosine residues and four immunoreceptor tyrosine-based inhibition motifs (ITIMs) (1-3). A variant form of Siglec-2 missing two Ig-like C2-type domains along with a truncated cytoplasmic tail has also been identified (4). The mature ECD of rat Siglec-2 shares 58% and 76% amino acid sequence identity with human and mouse 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 (5). Besides its role as an adhesion molecule, Siglec-2 is a coreceptor that physically interacts with B-cell receptor (BCR), negatively regulating 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 (2). Another function of Siglec-2 is that it mediates the anti-phagocytic effect of alpha 2,6-linked sialic acid, and inhibition of Siglec-2 promotes the clearance of myelin debris, amyloid-beta oligomers and alpha -synuclein fibrils in vivo (6). Siglec-2 also plays a role in autoimmunity and has great potential for Siglec-2-based immunotherapeutics for the treatment of autoimmune diseases such as systemic lupus erythematosus (SLE) (7).
- Sato, S. et al. (1996) Immunity. 5:551.
- Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
- Macauley, M.S. et al. (2014) Nature Rev Imm. 14:653.
- Stamenkovic, I. and B. Seed (1990) Nature 345:74.
- Collins, B.E. et al. (2004) Proc. Natl. Acad. Sci. 101:6104.
- Pluvinage, J.V. et al. (2019) Nature. 568:7751.
- Clark, E.A. et al. (2018) Front Immunol. 9:2235.
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