Recombinant Human Kremen-2 Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human Kremen-2 Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhKremen-2/his at 4 µg/mL (100 µL/well) can bind rhDkk-1 with an apparent KD <10 nM.
Source
Mouse myeloma cell line, NS0-derived human Kremen-2 protein
Gln19-Ala364, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
No results obtained: Gln19 predicted
Protein/Peptide Type
Recombinant Proteins
Gene
KREMEN2
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.

Applications/Dilutions

Theoretical MW
38 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
59-63 kDa, 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 BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Kremen-2 Protein

  • Dickkopf receptor 2
  • kremen protein 2
  • Kremen2
  • Kremen-2
  • kringle containing transmembrane protein 2
  • Kringle domain-containing transmembrane protein 2
  • KRM2Kringle-containing protein marking the eye and the nose
  • MGC10791
  • MGC16709

Background

Kremen (Kringle-containing protein marking the eye and the nose) proteins are type I transmembrane proteins that contain extracellular kringle, WSC and CUB domains and an intracellular region without any conserved motifs (1). Two related members, Kremen-1 and -2, have been identified. Kremens bind a subset of the secreted Dickkopf (Dkk) proteins (Dkk-1, -2, and -4) with high affinity to modulate the canonical Wnt signaling pathway that is transduced by the ternary receptor complex composed of Wnt, the seven-transmembrane domain receptor Frizzled, and the LDL-receptor-related protein 5/6 (LRP5/6) coreceptor (2, 3). Within the Dkk family, Dkk-1 and -4 bind directly to the LRP5/6 coreceptor to antagonize the canonical Wnt/ beta -catenin signaling pathway, but not the planar cell polarity (PCP) signaling pathway that does not involve LRP5/6 (4). In contrast, Dkk-3 has no effect on Wnt signaling and Dkk-2 can function either as an LRP agonist or antagonist, depending on whether the cell expresses Kremen (5). Kremen cooperates with Dkk to antagonize Wnt signaling via formation of a Kremen-Dkk-LRP ternary complex that triggers the internalization and clearance of the complex from the cell surface (3). All three extracellular domains but not the cytoplasmic region of a membrane anchored Kremen are needed for binding to the second cysteine-rich domain of Dkks (3). Human Kremen-2 cDNA encodes a 462 amino acid (aa) glycosylated protein with a putative 18 aa signal peptide, a 353 aa extracellular domain, a 17 aa transmembrane domain and a 75 aa cytoplasmic domain. In the extracellular domain, it shares 88% and 42% amino acid sequence identity with mouse Kremen-2 and human Kremen-1, respectively.

  1. Nakamura, T. et al. (2001) Biochim. Biophys. Acta 1518:63.
  2. Davidson G. et al. (2002) Development 129:5587.
  3. Mao, B. et al. (2002) Nature 417:664.
  4. Zorn, A.M. (2001) Curr. Biol. 11:R592.
  5. Mao, B. and C. Niehrs (2003) Gene 302:179.

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Bioinformatics

Gene Symbol KREMEN2
Uniprot