Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind HLA on MDA‑MB‑231 human breast cancer cells. The ED50 for this effect is 0.03-0.18 μg/mL. |
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Source | Chinese Hamster Ovary cell line, CHO-derived human KIR3DS1/CD158e2 protein
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Accession # | |||||||
N-terminal Sequence | His22 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | KIR3DS1 |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
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Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 61.9 kDa (monomer). 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 | 75-90 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 | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
KIR3DS1 (3DS1, CD158e2) is a type I transmembrane protein that belongs to the killer cell Ig-like receptor (KIR) family. KIRs are expressed on CD56dim NK cells and T cell subsets where they differentiate normal from abnormal cells, and regulate effector functions in the innate immune system (1 - 3). KIRs are named for the number of Ig-like domains (2D or 3D) in the extracellular domain (ECD), and whether they have long or short (L, S) cytoplasmic tails. Like other activating KIRs, KIR3DS1 has a short cytoplasmic tail and a positively charged amino acid (aa) within the transmembrane domain that interacts with the ITAM-bearing signaling adaptor, DAP12 (2, 4). Crosslinking of KIR3DS1 activates cytolysis and induces IFN-gamma production, confirming it to be an activating receptor (4). Approximately 38% of the population expresses KIR3DS1 on the surface of NK cells (1, 4, 5). Variants lacking the N-terminal Ig-like domain and/or with substitutions in the cytoplasmic tail have been described (1, 6). The 50 kDa, 387 aa KIR3DS1 shows 97% aa identity with KIR3DL1 within the ECD, and the two segregate as alleles (3, 7). Some activating KIRs bind weakly to the ligands recognized by their corresponding inhibitory KIR. KIR3DS1 does not bind appreciably to cells transfected with ligands for HLA-Bw4 KIR3DL1 (4, 5). However, HIV-infected people who express the combined phenotype of KIR3DS1 with Bw4 alleles that contain an isoleucine at aa 80, show delayed progression to AIDS and fewer AIDS-related opportunistic infections (7, 8). KIR receptors have no structural orthologs in nonprimates, although mouse Ly-49 proteins perform similar functions (2).
Diseases for KIR3DS1/CD158e2 (4136-KR)Discover more about diseases related to KIR3DS1/CD158e2 (4136-KR).
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PTMs for KIR3DS1/CD158e2 (4136-KR)Learn more about PTMs related to KIR3DS1/CD158e2 (4136-KR).
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