Other Proteins

Recombinant Murine BMP-4 (Legacy Tebubio ref. 167315-27). Bone morphogenetic proteins (BMPs) constitute a subfamily within the TGF-beta superfamily of structurally related signaling proteins. Members of this superfamily are widely distributed throughout the body, and are involved in diverse physiological processes during both pre- and postnatal life. Like BMP-7, BMP-4 is involved in the development and maintenance of bone and cartilage. Reduced expression of BMP-4 is associated with a number of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. PeproTech's E.coli derived murine BMP-4 is a fully active homodimeric protein consisting of two 106 amino acid subunits which correspond to amino acids 303-408 of the full length BMP-4 precursor. The calculated molecular weight of Recombinant Murine BMP-4 is 23.9 kDa.

Recombinant Murine EG-VEGF (Legacy Tebubio ref. 167315-29). EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The murine EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Murine EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Murine EG-VEGF (Legacy Tebubio ref. 167315-29). EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The murine EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Murine EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Murine TFF-2 (Legacy Tebubio ref. 167315-30). The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma (Nikolaidis, N.M. et al. Am. Journal Respir. Cell Mol. Biol.(2003) 4: 458-464). Recombinant Murine TFF-2 is an 11.9 kDa polypeptide of 106 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

Recombinant Murine TFF-2 (Legacy Tebubio ref. 167315-30). The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma (Nikolaidis, N.M. et al. Am. Journal Respir. Cell Mol. Biol.(2003) 4: 458-464). Recombinant Murine TFF-2 is an 11.9 kDa polypeptide of 106 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

Recombinant Murine TFF-1 (Legacy Tebubio ref. 167315-31). The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF1 is essential for normal differentiation of the antral and pyloric gastric mucosa, and functions as a gastric-specific tumor suppressor gene. Recombinant Murine TFF-1 is a 7.4 kDa monomeric protein consisting of a 66 amino acid polypeptide chain, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

Recombinant Murine TFF-1 (Legacy Tebubio ref. 167315-31). The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF1 is essential for normal differentiation of the antral and pyloric gastric mucosa, and functions as a gastric-specific tumor suppressor gene. Recombinant Murine TFF-1 is a 7.4 kDa monomeric protein consisting of a 66 amino acid polypeptide chain, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.

Recombinant Murine R-Spondin-1 (Legacy Tebubio ref. 167315-32). R-Spondin-1 (Rspo-1) belongs to the (Rspo) family of Wnt modulators. Currently, the family consists of four structurally related secreted ligands (Rspo 1-4), all containing the furin-like and thrombospondin structural domains. Rspo-1 is expressed in certain areas of the developing central nervous system, as well as in the adrenal glands, ovary, testis, thyroid, and trachea. Rspo can interact with the Frizzled/LRP6 receptor complex in a manner that stimulates the Wnt/beta-catenin signaling pathway. Recombinant Murine R-Spondin-1 is a 27.1 kDa protein consisting of 245 amino acid residues. Due to glycosylation, R-Spondin-1 migrates at an apparent molecular weight of approximately 40.0 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Murine R-Spondin-1 (Legacy Tebubio ref. 167315-32). R-Spondin-1 (Rspo-1) belongs to the (Rspo) family of Wnt modulators. Currently, the family consists of four structurally related secreted ligands (Rspo 1-4), all containing the furin-like and thrombospondin structural domains. Rspo-1 is expressed in certain areas of the developing central nervous system, as well as in the adrenal glands, ovary, testis, thyroid, and trachea. Rspo can interact with the Frizzled/LRP6 receptor complex in a manner that stimulates the Wnt/beta-catenin signaling pathway. Recombinant Murine R-Spondin-1 is a 27.1 kDa protein consisting of 245 amino acid residues. Due to glycosylation, R-Spondin-1 migrates at an apparent molecular weight of approximately 40.0 kDa by SDS-PAGE analysis under reducing conditions.