Recombinant Rat Kremen-2 Protein, CF Summary
Product Specifications
Gly53-Arg395, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4295-KR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Kremen-2
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 with no conserved motifs (1). Two related molecules, Kremen-1 and -2, have been identified. Kremens bind with high affinity to a subset of the secreted Dickkopf proteins (Dkk-1, -2, and -4) to modulate the canonical Wnt signaling pathway (2). This pathway is transduced by a ternary receptor complex composed of Wnt, the seven-transmembrane domain receptor Frizzled, and the LDL-receptor-related protein 5/6 (LRP5/6) coreceptor (3, 4). Dkk-1 and -4 bind directly to the LRP5/6 coreceptor to antagonize the canonical Wnt/ beta -catenin signaling pathway. The planar cell polarity (PCP) signaling pathway is not affected as it does not involve LRP5/6 (2). In contrast, Dkk-3 has no effect on Wnt signaling. Dkk-2 can function either as an LRP agonist or antagonist, depending on whether or not the cell expresses Kremen (5). Kremen cooperates with Dkk to antagonize Wnt signaling via formation of a Kremen-Dkk-LRP ternary complex which is internalized and cleared from the cell surface (4). Binding requires all three extracellular domains of Kremen, and the second cysteine-rich domain of Dkk (4). The predicted rat Kremen-2 cDNA encodes a 490 amino acid (aa) glycosylated protein with a 51 aa signal peptide, a 340 aa extracellular domain, a 24 aa transmembrane domain, and a 75 aa cytoplasmic domain. Within the ECD, rat Kremen-2 shares 91% and 98% aa sequence identity with human and mouse Kremen-2, respectively, and 46% with rat Kremen-1.
- Nakamura, T. et al. (2001) Biochim. Biophys. Acta 1518:63.
- Niehrs, C. (2006) Oncogene 25:7469.
- Davidson G. et al. (2002) Development 129:5587.
- Mao, B. et al. (2002) Nature 417:664.
- Mao, B. and C. Niehrs (2003) Gene 302:179.
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