Recombinant Human Siglec‑7 Fc Chimera (Catalog # 1138-SL), immobilized onto a microplate, supports the adhesion of human red blood cells in a dose-dependent manner (orange line). Adhesion elicited by Recombinant Human ...read more
Mouse myeloma cell line NS0-derived recombinant human Siglec-7/CD328 Gln19-Gly357 Accession # Q9Y286
Detects human Siglec‑7/CD328 in direct ELISAs and Western blots. In direct ELISAs, approximately 15% cross‑reactivity with recombinant human (rh) Siglec-9 is observed and approximately 5% cross-reactivity with recombinant mouse Siglec-E, rhSiglec-6, and rhSiglec-8 is observed.
<0.10 EU per 1 μg of the antibody by the LAL method.
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.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Siglec-7/CD328 Antibody [Unconjugated]
Adhesion inhibitory receptor molecule 1
adhesion inhibitory receptor molecule 1, siglec-7
AIRM1QA79 membrane protein
sialic acid binding Ig-like lectin 7
sialic acid binding immunoglobulin-like lectin 7
sialic acid-binding Ig-like lectin 7
Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They 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, 2). Eleven human Siglecs have been cloned and characterized. They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglecs 5 to 11 (1‑4). 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. Siglecs 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 (2, 3). 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.
Human Siglec-7 encodes a 467 amino acid (aa) polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, two Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail (5). Siglec-7 exists as a monomer on the cell surface and is expressed on natural killer cells, CD8+ T cells and monocytes (3, 5). It binds equally well to both alpha 2,3- and alpha 2,6-linked sialic acid (5). The gene encoding Siglec-7 was mapped to chromosome 19q13.3.
Crocker, P.R. et al. (1998) Glycobiology 8:v.
Crocker, P.R. and A. Varki (2001) Trends Immunol. 22:337.
Crocker, P.R. and A. Varki (2001) Immunology 103:137.
Angata, T. et al. (2002) J. Biol. Chem. 277:24466.
Nicoll, G. et al. (1999) J. Biol. Chem. 274:34089.
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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