Mouse Kremen-1 Antibody Summary
Accession # Q640Q6
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Mouse Kremen‑1 by Western Blot. Western blot shows lysates of mouse liver tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse Kremen‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1647) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Kremen‑1 at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 7.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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) co-receptor (2, 3). Within the Dkk family, Dkk-1 and -4 bind directly to the LRP5/6 co-receptor 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 co-operates 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). Mouse Kremen-1 cDNA encodes a 473 amino acid (aa) glycosylated protein with a putative 19 aa signal peptide, a 372 aa extracellular domain, a 21 aa transmembrane domain and a 60 aa cytoplasmic domain. In the extracellular domain, it shares 92% and 41% amino acid sequence identity with human Kremen-1 and mouse Kremen-2, respectively. Mouse Kremen-1 is widely expressed in diverse embryonic (apical ectodermal ridge of the developing fore- and hindlimb buds, telencephalon and the first brachial arch, myotome and sensory tissues) and adult (lung, heart, kidney, skeletal muscle and testis) tissues (1).
- Nakamura, T. et al. (2001) Biochim Biophys Acta 1518:63.
- Davidson G. et al. (2002) Development 129:5587.
- Mao, B. et al. (2002) Nature 417:664.
- Zorn, A.M. (2001) Curr. Biol. 11:R592.
- Mao, B. and C. Niehrs (2003) Gene 302:179.
Citations for Mouse Kremen-1 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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miRNA-431 Prevents Amyloid-?-Induced Synapse Loss in Neuronal Cell Culture Model of Alzheimer's Disease by Silencing Kremen1
Authors: SP Ross, KE Baker, A Fisher, L Hoff, ES Pak, AK Murashov
Front Cell Neurosci, 2018;12(0):87.
Sample Types: Whole Cells
Dickkopf-1 is a master regulator of joint remodeling.
Authors: Diarra D, Stolina M, Polzer K, Zwerina J, Ominsky MS, Dwyer D, Korb A, Smolen J, Hoffmann M, Scheinecker C, van der Heide D, Landewe R, Lacey D, Richards WG, Schett G
Nat. Med., 2007;13(2):156-63.
Sample Types: Tissue Homogenates
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