Recombinant Human KIR3DL3/CD158z His-tag Protein, CF

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When Biotinylated Recombinant Human B7-H7/HHLA2 Fc Chimera is present at 0.5 μg/mL, the concentration of Recombinant Human KIR3D3L/CD158z His-tag that produces 50% of the optimal binding response is found to be ...read more
2 µg/lane of Recombinant Human KIR3DL3/CD158z (Catalog # 10454-KR ) was resolved by SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 42-47 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human KIR3DL3/CD158z His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human B7-H7/HHLA2 Fc Chimera is present at 0.5 μg/mL, the concentration of Recombinant Human KIR3D3L/CD158z His-tag that produces 50% of the optimal binding response is found to be approximately 7.5-45 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human KIR3DL3/CD158z protein
Gln26-Leu322, with a C-terminal 6-His tag
Accession #
N-terminal Sequence

Gln26, deduced from Asp27 upon deblocking

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
  • Bioactivity
Theoretical MW
33 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
42-47 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 KIR3DL3/CD158z His-tag Protein, CF

  • CD158z
  • CD158Z;Killer cell immunoglobulin-like receptor 3DL3;KIR2DL5B;KIR3DL7;KIR44;KIRC1
  • KIR3DL3
  • KIR3DL7
  • KIR44
  • KIRC1

Background

KIR3DL3 (also known as CD158z, KIR3DL7, KIR44, or KIRC1) is a type I transmembrane glycoprotein that belongs to the killer cell Ig-like receptor (KIR) family. KIRs are expressed on CD56dim NK cells and T cell subsets where they regulate effector functions in the innate immune system (1 - 4). 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. Human KIR3DL3 cDNA encodes a 410 amino acid (aa) polypeptide precursor with a 25 aa signal peptide, a 297 aa extracellular domain (ECD) with 3 Ig-like domains (3D), a 21 aa transmembrane domain, and a 67 aa cytoplasmic domain (long). Within ECD human KIR3DL3 shares 47% and 44% aa sequence identity with mouse and rat KIR3DL3, respectively. KIR3DL3 is ubiquitously present in every individual across diverse populations, however little is known about specific functions (5). The limited knowledge of KIR3DL3 expression does suggest involvement in reproduction, likely during placentation (4). KIR3DL3 likely encodes an NK cell inhibitory receptor (6). Recent studies have shown that KIR3DL3 binding and function require both receptor aggregation and inhibitory signal attenuation (7).
  1. Colonna, M. and J. Samaridis (1995) Science 268:405.
  2. Lanier, L. L. (2005) Annu. Rev. Immunol. 23:225.
  3. Uhrberg, M. et al. (1997) Immunity 7:753.
  4. Trundley, A. E. et al. (2006) Immunogenetics 57:904.
  5. Hollenbach, J. A. et al. (2012) Immunogenetics 64:719.
  6. Torkar, M. et al. (1998) Eur. J. Immunol. 28:3959.
  7. Leaton, L. A. et al. (2019) Front. Immunol. 10:24.

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