Recombinant Human NKp65/KLRF2 Fc Chimera Protein, CF

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When Recombinant Human NKp65/KLRF2 Fc Chimera (Catalog # 10371-NK) is immobilized at 0.1 μg/mL, 100 μL/well, the concentration for Recombinant Human CLEC-2A (Catalog # 8435-CL) that produces 50% of the optimal ...read more
2 μg/lane of Recombinant Human NKp65/KLRF2 Fc Chimera (Catalog # 10371-NK) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human NKp65/KLRF2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human NKp65/KLRF2 Fc Chimera (Catalog # 10371-NK) is immobilized 0.1 μg the concentration of Recombinant Human CLEC-2A (Catalog # 8435-CL) the optimal binding response is approximately 0.5-3 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human NKp65/KLRF2 protein
MDHuman IgG1
(Pro100-Lys330)
IEGR Human NKp65/KLRF2
(Asp52-Val207)
Accession # D3W0D1.1
N-terminusC-terminus
Accession #
N-terminal Sequence
Met Asp - Pro100
Structure / Form
Disulfide-linked homodimer
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
45 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
50-65 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 NKp65/KLRF2 Fc Chimera Protein, CF

  • KLRF 2
  • KLRF2
  • NKp65

Background

Killer cell lectin-like receptor subfamily F member 2, also known as KLRF2 and NKp65, is a C-type lectin-like receptor and a member of the NKRP1 (NK receptor protein) subfamily (1-3). KLRF2, along with the related KLRF1, is an activating receptor for the C-type-lectin-like-2 (CLEC2) family of ligands (1-3). KLRF2 is a type II transmembrane glycoprotein with a short N-terminal cytoplasmic domain, a single transmembrane region and an extracellular domain (ECD) consisting of 26-residue stalk and 130-residue C-type lectin-like domain (CTLD) (1, 3). Unlike other members of the NKRP1 family such as KLRF1, KLRF2 is a non-disulfide-linked homodimer (1, 2). While sharing subfamily-specific traits classifying them as members of the NKRP1 subfamily, there does not appear to be a direct homolog of KLRF2 in mouse (2). KLRF2 is minimally expressed on peripheral blood NK cells and its ligand, Keratinocyte-associated C-type lectin (KACL), is restricted to human keratinocytes (1-3). This expression of KACL indicates potential implications in skin-affecting diseases such as psoriasis and wound healing (1). The signaling pathway of KLRF2 is distinct from most NK receptors because it does not utilize immunoreceptor tyrosine-based activating motif (ITAM)-containing signaling adaptors, but rather uses an activating signaling motif with only one tyrosine module referred to as hemITAM (1, 3).
  1. Spreu, J. et al. (2010) Proc Natl Acad Sci USA 107:5100.
  2. Bartel, Y. et al. (2013) Front Immunol 4:362.
  3. Li, Y. et al. (2013) Proc Natl Acad Sci USA 110:11505.

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