Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind biotinylated Recombinant Human CD229/SLAMF3 in a functional ELISA. Romero, X. et al. (2005) J. Immunol. 174:7033. |
Source | Mouse myeloma cell line, NS0-derived human CD229/SLAMF3 protein Lys48-Lys454, with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | Lys48 |
Protein/Peptide Type | Recombinant Proteins |
Gene | LY9 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 46.1 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. |
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SDS-PAGE | 71-77 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
CD229, also known as Ly9 and SLAMF3, is a 120 kDa type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family (1). Mature human CD229 consists of a 407 amino acid (aa) extracellular domain (ECD) with two Ig-like V-set and two Ig-like truncated C2-set domains. It also shows a 22 aa transmembrane segment, and a 179 aa cytoplasmic domain with two immunoreceptor tyrosine-based switch motifs ITSMs (2, 3). The ECD of human CD229 shares 57% - 59% aa sequence identity with mouse and rat CD229. Within the first two Ig-like domains that are common to all SLAM proteins, human CD229 shares 24% - 39% aa sequence identity with human 2B4, BLAME, CD2F-10, CD84, CRACC, NTB-A, and SLAM. Alternate splicing generates two additional isoforms that lack the juxtamembrane Ig-like domain or short cytoplasmic region (2). CD229 is expressed on T and B cells, thymocytes, and more weakly on NK cells (2 - 6). Homophilic binding between CD229 molecules is mediated by the N-terminal Ig-like domain (7). Human and mouse CD229 exhibit cross-species binding (7). Antigen stimulation of lymphocytes induces CD229 clustering to sites of T cell - B cell contact (7). Two tyrosines in the cytoplasmic domain are required for association of CD229 with the adaptor proteins AP-2 (μ2 chain) and GRB-2 and both are required for CD229 internalization (8, 9). In addition, there are two ITSMs which mediate phosphorylation-dependent CD229 association with SAP and SHP-2 (10). These four tyrosine-containing motifs are intact in the described CD229 splice variants. CD229 knockout mice show minimally impaired immune responses, suggesting functional redundancy with other molecules (11).
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