Other Proteins

Recombinant Murine Wnt-3a (Legacy Tebubio ref. 167315-20). Wnt-3a belongs to the Wnt family of signaling proteins that play a key role in maintaining the integrity of embryonic and adult tissues. Expression of Wnt-3a occurs primarily along the dorsal midline across overlapping regions of the Central Nervous System (CNS). Wnt-3a signaling is essential for various morphogenetic events, including embryonic patterning, cell determination, cell proliferation, CNS development, and cytoskeletal formation. Like other members of this family, Wnt-3a contains a highly conserved lipid-modified, cysteine-rich domain that is essential for cell signaling. During a biochemical process called the canonical Wnt pathway, Wnt family members bind to and activate, seven-pass transmembrane receptors of the Frizzled family, ultimately leading to the disruption of beta-catenin degradation. Intracellular accumulation of beta-catenin increases translocation of the protein into the nucleus, where it binds to TCF/

Recombinant Murine Betacellulin (Legacy Tebubio ref. 167315-21). Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells.Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant Murine Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino acid residues, which comprises the mature EGF-homologous portion of the Betacellulin protein.

Recombinant Murine Betacellulin (Legacy Tebubio ref. 167315-21). Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells.Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant Murine Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino acid residues, which comprises the mature EGF-homologous portion of the Betacellulin protein.

Recombinant Murine Sonic Hedgehog (Shh) (Legacy Tebubio ref. 167315-22). Members of the Hedgehog (Hh) family are highly conserved proteins that are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh), are structurally related, and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93% identical). The biologically active form of each Hh molecule is obtained by autocatalytic cleavage of their precursor proteins, and each corresponds to approximately one half of the N-terminal portion of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can be substituted for one another in experimental systems. Recombinant Murine Sonic Hedgehog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted fo

Recombinant Murine Sonic Hedgehog (Shh) (Legacy Tebubio ref. 167315-22). Members of the Hedgehog (Hh) family are highly conserved proteins that are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh), are structurally related, and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93% identical). The biologically active form of each Hh molecule is obtained by autocatalytic cleavage of their precursor proteins, and each corresponds to approximately one half of the N-terminal portion of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can be substituted for one another in experimental systems. Recombinant Murine Sonic Hedgehog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted fo

Recombinant Murine HGF (Legacy Tebubio ref. 167315-23). HGF is a potent, mesenchymally-derived mitogen for mature parenchymal hepatocytes, and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include the induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Murine HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 696 amino acid residues. Proteolytic processing of this precursor generates the biologically active heterodimeric form of HGF, which consists of two polypeptide chains (alpha-chain and beta-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The alpha-chai

Recombinant Murine HGF (Legacy Tebubio ref. 167315-23). HGF is a potent, mesenchymally-derived mitogen for mature parenchymal hepatocytes, and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include the induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Murine HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 696 amino acid residues. Proteolytic processing of this precursor generates the biologically active heterodimeric form of HGF, which consists of two polypeptide chains (alpha-chain and beta-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The alpha-chai

Recombinant Murine GDF-5 (BMP-14/CDMP-1) (Legacy Tebubio ref. 167315-24). GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino acid polypeptide chains (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 348 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant Murine GDF-5 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Recombinant Murine GDF-5 (BMP-14/CDMP-1) (Legacy Tebubio ref. 167315-24). GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino acid polypeptide chains (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 348 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant Murine GDF-5 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.