CD329 Recombinant Protein NCP0332
Specifications
| 500ug/1mg price = 500ug |
Host:
E.coli
Tag:
His-tag
AA Sequence:
SELDPKGQHVCVASSPSAELQCCAGWRQKDQECTIPICEGPDACQKDEVCVKPGLCRCKP GFFGAHCSSRCPGQYWGPDCRESCPCHPHGQCEPATGACQCQADRWGARCEFPCACGPHG RCDPATGVCHCEPGWWSSTCRRPCQCNTAAARCEQATGACVCKPGWWGRRCSFRCNCHGS PCEQDSGRCACRPGWWGPECQQQCECVRGRCSAASGECTCPPGFRGARCELPCPAGSHGV QCAHSCGRCKHNEPCSPDTGSCESCEPGWNGTQCQQPCLPGTFGESCEQQCPHCRHGEAC EPDTGHCQRCDPGWLGPRCEDPCPTGTFGEDCGSTCPTCVQGSCDTVTGDCVCSAGYWGP SCNASCPAGFHGNNCSVPCECPEGLCHPVSGSCQPGSGSRDT
Expression vector:
pet-22b(+)
Soluble:
PBS, 4M Urea, PH7.4
BiowMW:
~42kDa
Purification & Purity:
Transferred into competent cells and the supernatant was purified by NI column affinity chromatography and the purity is > 85% (by SDS-PAGE).
Storage & Stability:
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
Background:
Two families of mammalian lectin-like adhesion molecules bind glycoconjugate ligands in a sialic acid-dependent manner: the selectins and the sialoadhesins. The sialic acid-binding immunoglobulin superfamily lectins, designated siglecs or sialoadhesins, are immunoglobulin superfamily members recognizing sialylated ligands. The common sialic acids of mammalian cells are N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc). Siglec-1 mediates local cell-cell interactions in lymphoid tissues and can be detected at contact points of macrophages with other macrophages, sinus-lining cells and reticulum cells. Siglec-7, highly expressed in monocytes and resident blood cells but not in parenchymatous cells, mediates inhibition of natural killer cell cytotoxicity. Siglec-9 is closely homologous to Siglec-7. It is highly expressed in peripheral blood leukocytes (not eosinophils), liver, bone marrow, placenta and spleen. Siglec-8, a type I membrane protein, is selectively expressed on human eosinophils, basophils and mast cells, where it regulates their function and survival.
Note:
For research use only, not for use in diagnostic procedure.
