Recombinant Mouse Siglec-F His-tag Protein, CF Summary
Product Specifications
Asp18-Thr437, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
10171-SF
| Formulation | Lyophilized from a 0.2 μm filtered solution in MES and NaCl with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in water. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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When Recombinant Mouse Siglec-F His-tag (Catalog # 10171-SF) is immobilized onto a His Tag Antibody (Catalog # MAB050R) coated plate, it supports the adhesion of human red blood cells. The ED50 for this is 8-48 ng/mL.
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2 μg/lane of Recombinant Mouse Siglec‑F His-tag (Catalog # 10171-SF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 59-68 kDa.
Reconstitution Calculator
Background: Siglec-F
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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