|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_114434, 24041012|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||54 kDa|
|Application Notes||KREMEN1 antibody can be used for detection of KREMEN1 by Western blot at 0.125 - 0.25 µg/mL.|
|Target/Specificity||KREMEN1; Three isoforms of KREMEN1 exists as a result of alternative splicing event.|
|Reconstitution & Storage||KREMEN1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||KREMEN1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Receptor for Dickkopf protein. Cooperates with Dickkopf to block Wnt/beta-catenin signaling (By similarity).|
|Cellular Location||Membrane; Single-pass type I membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
KREMEN1 Antibody: 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. Kremens bind a subset of the secreted Dickkopf 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, Frizzled, and the LDL receptor related protein 5/6 (LRP5/6) coreceptor. KREMEN1 is a receptor for the Dickkopf protein which blocks Wnt/beta catenin signaling. It is necessary to ensure normal spatial and temporal patterns of Wnt activity during developmental processes.
Nakamura T, Aoki S, Kitajima K, et al. Molecular cloning and characterization of Kremen, a novel kringle-containing transmembrane protein. Biochim. Biophys. Acta. 2001; 1518:63-72.
Mao B, Wu W, Davidson G, et al. Kremen proteins are Dickkopf receptors that regulate Wnt/beta-catenin signalling. Nature 2002; 417:664-7.
Li J, Liu WM, Cao YJ, et al. Roles of Dickkopf-1 and its receptor Kremen1 during embryonic implantation in mice. Fertil. Steril. 2008; 90:1470-9.
Wang K, Zhang Y, Li X, et al. Characterization of the Kremen-binding site on Dkk1 and elucidation of the role of Kremen in Dkk-mediated Wnt antagonism. J. Biol. Chem. 2008; 283:23371-5.
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