CD328 (Siglec-7) antibodies, human

CD328 (Siglec-7) antibodies, human

Clone: REA214 | Dilution: 1:11
Clone REA214 recognizes CD328, which is a member of sialic acid-binding immunoglobulin-like lectins (siglecs) family of trans-membrane proteins. Upon recognizing their natural ligands, the sialylated carbohydrates, siglecs generally transmit an inhibitory signal. CD328 is a 75 kDa type I trans-membrane protein and further belongs to the human CD33-related siglec receptors with sialic acid binding N-terminal Ig domain, two C2-set Ig domains, and a cytoplasmic region containing one immune-receptor tyrosine based inhibitory motif (ITIM) and one ITIM-like motif. Expression of CD328 is found on natural killer (NK) cells, monocytes, and on a small subset of CD8
+
/CD3
+
T cells and it preferentially binds (2,8)-linked disialic acids and branched 2,6-sialyl residues.
Additional information: Clone REA214 displays negligible binding to Fc receptors.

Alternative names

AIRM1, CDw328, D-siglec, QA79, Siglec-7, SIGLEC19P, SIGLECP2, p75, p75/AIRM1

Technical specifications

  • Antigen: CD328 (Siglec-7)
  • Clone: REA214
  • Isotype: recombinant human IgG1
  • Isotype control: REA Control (S) antibodies
  • Alternative names of antigen: AIRM1, CDw328, D-siglec, QA79, Siglec-7, SIGLEC19P, SIGLECP2, p75, p75/AIRM1
  • Distribution of antigen: NK cells, monocytes
  • Product format: Reagents are supplied in buffer containing stabilizer and 0.05% sodium azide.
  • Fixation: The antibody is suited for staining of formaldehyde-fixed cells.
  • Storage: Store protected from light at 2–8 °C. Do not freeze.
  • Available conjugates: FITC, PE, APC, VioBlue, PE-Vio770, APC-Vio770, PerCP-Vio700, Biotin
  • Selected references

    1. Attrill, H. et al. (2006) Siglec-7 undergoes a major conformational change when complexed with the (2,8)-disialylganglioside GT1. J. Biol. Chem. 281: 32774-32783
    2. Angata, T. et al. (2000) Siglec-7: a sialic acid-binding lectin of the immunoglobulin superfamily. Glycobiology 10: 431-438
    3. Madge, PD. et al. (2016) Structural characterisation of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt's lymphoma (BL) Daudi cells by NMR spectroscopy. Sci. Rep. 6: 36012
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