Recombinant Mouse Siglec‑F Fc Chimera (Catalog # 1706-SF), immobilized onto a microplate, supports the adhesion of human red blood cells in a dose-dependent manner (orange line). Adhesion elicited by Recombinant Mouse ...read more
Detects mouse Siglec-F in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant mouse Siglec-2 or -3, or recombinant human Siglec-5, -7, -9, -10, or -11 is observed.
Source
N/A
Isotype
IgG2a
Clonality
Monoclonal
Host
Rat
Gene
Siglecf
Purity Statement
Protein A or G purified from hybridoma culture supernatant
Endotoxin Note
<0.10 EU per 1 μg of the antibody by the LAL method.
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.5 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Siglec-F Antibody (238047) [Unconjugated]
SAF2
sialic acid binding Ig like lectin 8
SIGLEC-8
SIGLEC8L
SiglecF
Siglec-F
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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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