Recombinant Cynomolgus/Rhesus Siglec-3/CD33 His Protein, CF Summary
Details of Functionality |
Bioassay data are not available. |
Source |
Chinese Hamster Ovary cell line, CHO-derived Siglec-3/CD33 protein Met16-Gly248, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Met16 |
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 |
27 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 |
42-55 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 Cynomolgus/Rhesus Siglec-3/CD33 His Protein, CF
Background
Sialic acid-binding Ig-like lectin 3
(Siglec-3), also known myeloid cell surface antigen CD33 (CD33), is a I-type
(Ig-type) lectin belonging to the sialoadhesin subclass of the immunoglobulin
superfamily (1). Siglecs 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 in the extracellular domain (ECD). Fourteen human and
nine mouse Siglecs have been characterized and are divided into 2 families:
CD33 related and evolutionarily conserved (1-3). Mature Siglec-3 consists of an
ECD with one Ig-like V-type domain and one Ig-like C2 domain, a single
transmembrane and a cytoplasmic tail containing two immunoreceptor
tyrosine-based inhibitory motifs (ITIMs) (3). Within the ECD, cynomolgus/rhesus
Siglec-3 shares 89% amino acid sequence identity with human Siglec-3. An
isoform of Siglec-3 lacking the N-terminal V-type domain, generated by
alternative splicing, has been identified in humans (4). Siglec-3 is a
disulfide-linked homodimer expressed on neutrophils, monocytes, macrophages and
dendritic cells (2). Each Siglec family member has a distinct preference for
binding the various types of sialylated glycans found on the surface of
mammalian cells and they most likely evolved to regulate host immune responses
via the recognition of self-glycans (5). Siglec-3 may be implicated in the
regulation of both the innate but also the adaptive immunity and human Siglec-3
continues to be a therapeutic target for the treatment of acute myeloid
leukemia and is a high potential risk factor for Alzheimer's (6). Siglec-3's
ligands have yet to be classified, however terminal epitope preferences are
conserved between Siglec-3 and Siglec-9 when binding to glycans (7). R&D
Systems in-house testing indicates that Siglec-3 binds to LGALS3BP, consistent
with the demonstrated functional interactions between other members of these
protein families (8).
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