Recombinant Rat 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. The ED50 for this effect is 0.15-1.8 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived rat Siglec-2/CD22 protein Rat Siglec-2/CD22 (Trp24-Gly690) Accession # NP_001100973.1 | IEGRMDP | Mouse IgG2a (Glu98-Lys330) | N-terminus | | C-terminus | |
|
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 |
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 |
112-138 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 °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 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 Fc Chimera 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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