Recombinant Human Siglec-3/CD33 His-tag Protein, CF Summary
Details of Functionality |
Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. The ED50 for this effect is 0.1-0.8 µg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human Siglec-3/CD33 protein Met17-His259, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Met17 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
28 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
44-49 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
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.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Siglec-3/CD33 His-tag Protein, CF
Background
Siglecs (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 (1-3). 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 (1, 2). This fact, together
with the presence of two conserved immunoreceptor tyrosine-based inhibition
motifs (ITIMs) in their cytoplasma tails, suggests that CD33related Siglecs are
involved in the regulation of cellular activation within the immune system. Human
Siglec-3 is alternatively known as myeloid cell surface antigen CD33 and GP67.
Human Siglec-3 cDNA encodes a 364 amino acid (aa) polypeptide with a hydrophobic
signal peptide, an N-terminal Ig-like V-type domain, one Ig-like C2-type domains,
a transmembrane region and a cytoplasmic tail (1, 4). Siglec-3 expression is
restricted to cells of myelomonocytic lineage (2). It binds sialic acid
preferring alpha 2,3-linkage over alpha 2,6-linkage (5). Studies indicated that Siglec-3 recruits
SHP-1 and SHP-2 to its ITIMs (6, 7). When co‑cross‑linking with Fc gamma R1, Siglec3- inhibits
tyrosine phosphorylation and calcium mobilization, suggesting Siglec-3 can
mediate inhibitory signals (7).
- 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.
- Simmons, D. and B. Seed (1988) J. Immunol. 141:2797.
- Freeman, S.D. et al. (1995) Blood 85:2002.
- Taylor, V.C. et al. (1999) J. Biol. Chem. 274:11505.
- Ulyanova, T. et al. (1999) Eur. J. Immunol. 29:3440.
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