Recombinant Mouse Wnt-3a (High Purity) Protein Summary
Product Specifications
Protein concentrations should be titrated based on cell type and if appropriate, passage number of the cell line.
Optimal concentrations should be determined by each laboratory for each application.
Ser19-Lys352
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.
1324-WNP
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS, NaCl, EDTA and CHAPS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
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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1324-WNP/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS, NaCl, EDTA and CHAPS. |
Reconstitution | Reconstitute at 100 μg/mL in 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.
|
Reconstitution Calculator
Background: Wnt-3a
Wnt-3a is one of 19 vertebrate members of the Wingless-type MMTV integration site (Wnt) family of highly conserved cysteine-rich secreted glycoproteins important for normal developmental processes (1). Wnts bind to the cell surface Frizzled family receptors in conjunction with low-density lipoprotein receptor-related protein family receptors (LRP5 or 6) resulting in the stabilization of intracellular beta -catenin levels (2). As intracellular beta -catenin levels rise, beta -catenin binds to TCF/LEF transcription factors leading to expression of Wnt target genes (3). Endo-IWR 1 (Catalog # 3532, # PSM1324) is a cell-permeant small molecule inhibitor of Axin turnover that suppresses Wnt signal transduction by stabilizing the beta -catenin destruction complex (4). Wnt-3a is a 44 kDa secreted hydrophobic glycoprotein containing a conserved pattern of 24 cysteine residues (5). Wnt-3a has two N-linked glycosylation sites (Asn 87, Asn 298), and Ser 209 is modified with palmitoleic acid (6). Glycosylation and acylation are essential for efficient Wnt secretion and biological activity, respectively (6, 7). Mouse Wnt-3a shares 96% amino acid (aa) identity with human Wnt-3a, and 97% with bovine and canine Wnt-3a. The rat Wnt-3a precursor shares 100% aa identity with mouse Wnt-3a aa 63-352 (8), and also shares 87% aa identity with Wnt3. During embryonic development, Wnt-3a is necessary for proper development of the hippocampus, anterior-posterior patterning, somite development, and tailbud formation (9-12). Wnt-3a also promotes self-renewal of hematopoietic stem cells, neural stem cells, and embryonic stem cells (13-15).
- Willert, K. and Nusse, R. (2012) Cold Spring Harb. Perspect. Biol. 4:a007864.
- MacDonald, B.T. and X. He (2012) Cold Spring Harb. Perspect. Biol. 4:a007880.
- Korinek, V. et al. (1997) Science 275:1784.
- Chen, B. et al. (2009) Nat. Chem. Biol. 5:100.
- Smolich, B.D. et al. (1993) Mol. Biol. Cell 4:1267.
- Takada, R. et al. (2006) Dev. Cell 11:791.
- Komekado, H. (2007) Genes Cells 12:521.
- Entrez Accession # NP_001100475.
- Dunty Jr. W. C. et al. (2008) Development 135:85.
- Ikeya, M. and S. Takada (2001) Mech. Dev. 103:27.
- Lee, S. M. et al. (2000) Development 127:457.
- Takada, S. et al. (1994) Genes Dev. 8:174.
- Willert, K. et al. (2003) Nature 423:6938.
- Kalani, M.Y. et al. (2008) Proc. Natl. Acad. Sci. USA 105:16970.
- Ten Berge, D. et al. (2011) Nat. Cell Biol. 13:1070.
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