Recombinant Mouse Siglec-F 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. Kelm, S. et al. (1994) Current Biology 4:965. The ED50 for this effect is 8-48 ng/mL.
|
Source |
Mouse myeloma cell line, NS0-derived mouse Siglec-F protein Asp18-Thr437, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Asp18 |
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 |
46 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 |
59-68 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 MES and NaCl 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 water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Siglec-F His-tag Protein, CF
Background
Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins (2) belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type
domain which mediates sialic acid binding (3), followed by varying numbers of Ig-like C2-type domains (1, 4). Eleven human Siglecs have been cloned and
characterized (1, 4). They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglec 5 to 11 (4-6).
To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate
are important in mediating the biological functions of Siglecs. Siglec 5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular
and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression
pattern within the hematopoietic system (4, 5). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their
cytoplasmic tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system. Mouse Siglec-F cDNA encodes a
569 amino acid polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, three Ig-like C2-type domains, a transmembrane region and a
cytoplasmic tail (7). The expression of Siglec-F is restricted to the cells of myelomonocytic lineage. Mouse Siglec-F is likely an ortholog of human Siglec-5. Unlike
many human CD33-related Siglecs, which show similar binding to both alpha 2,3- and alpha 2,6-linked sialic acids, mouse Siglec-F preferentially recognize alpha 2,3-linked sialic acid.
- Crocker, P.R. et al. (1998) Glycobiology 8:v.
- Powell, L.D. et al. (1995) J. Biol. Chem. 270:14243.
- May, A.R. et al. (1998) Mol. Cell 1998. 1:719.
- Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
- Crocker, P.R. et al. (2001) Immunology 103:137.
- Angata, T. et al. (2002) J. Biol Chem. 277:24466.
- Angata, T. et al. (2001) J. Biol Chem. 276:45128.
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