Other Proteins

Recombinant Human R-Spondin-2 (Legacy Tebubio ref. 167120-43). The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally-related, secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. This activity effectively activates and increases the subsequent nuclear signaling of beta-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/beta-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant Human R-Spondin-2 is a 24.4 kDa protein consisting of 212 amino acid residues. Due to glycosylation, R-Spondin-2 migrates at

Recombinant Human R-Spondin-2 (Legacy Tebubio ref. 167120-43). The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally-related, secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. This activity effectively activates and increases the subsequent nuclear signaling of beta-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/beta-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant Human R-Spondin-2 is a 24.4 kDa protein consisting of 212 amino acid residues. Due to glycosylation, R-Spondin-2 migrates at

Recombinant Human R-Spondin-3 (Legacy Tebubio ref. 167120-44). The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally-related, secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. This activity effectively activates and increases the subsequent nuclear signaling of beta-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/beta-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant Human R-Spondin-3 is a 26.9 kDa protein consisting of 240 amino acid residues. Due to glycosylation, R-Spondin-3 migrates at

Recombinant Human R-Spondin-3 (Legacy Tebubio ref. 167120-44). The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally-related, secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. This activity effectively activates and increases the subsequent nuclear signaling of beta-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/beta-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant Human R-Spondin-3 is a 26.9 kDa protein consisting of 240 amino acid residues. Due to glycosylation, R-Spondin-3 migrates at

Recombinant Human DKK-2 (Legacy Tebubio ref. 167120-45). The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory co

Recombinant Human DKK-2 (Legacy Tebubio ref. 167120-45). The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory co

Recombinant Human DKK-3 (Legacy Tebubio ref. 167120-46). The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-L1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory co

Recombinant Human DKK-3 (Legacy Tebubio ref. 167120-46). The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-L1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory co

Recombinant Human Wnt-9b (Legacy Tebubio ref. 167120-49). Formerly known as Wnt-15 or Wnt-14b, Wnt-9b is a secreted glycoprotein belonging to the Wnt family of signaling proteins that are critically involved in maintaining the integrity of both embryonic and adult tissues. Wnt-9b is primarily expressed in adult kidneys and during late embryogenesis, and shares with other Wnt family members the same highly conserved lipid-modified, cysteine-rich domain essential for cell signaling. As is true for most Wnt family members, Wnt-9b functions through the biochemical process known as the canonical Wnt pathway. In this process, Wnt proteins bind to and activate seven-pass transmembrane receptors of the Frizzled family, and ultimately results in the disruption of beta-catenin degradation. Intracellular accumulation of beta-catenin increases translocation of the protein into the nucleus, where it binds to TCF/LEF transcription factors to promote the expression of numerous genes. In this manner,