Other Proteins

Recombinant Human/Murine/Rat Activin A (CHO derived) (Legacy Tebubio ref. 167120-14P). Activin A is a TGF-beta family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-beta antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different beta subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodimer of t

Recombinant Human CTGFL/WISP-2 (Legacy Tebubio ref. 167120-16). CTGFL/WISP-2 is a 28.6 kDa protein that belongs to the CCN family of cysteine-rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, the ovaries, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant Human CTGFL/WISP-2 is a 24.3 kDa protein consisting of 228 amino acid residues. Mature human CTGFL/WISP-2 is a 24.8 kDa polypeptide protein containing 227 amino acids. It is composed of 3 distinct domains; the IGF-Binding Protein domain (IGF-BP), the Thrombospondin type I repeat (TSP type I), and von Willebrand Factor C motif (VWFC).

Recombinant Human CTGFL/WISP-2 (Legacy Tebubio ref. 167120-16). CTGFL/WISP-2 is a 28.6 kDa protein that belongs to the CCN family of cysteine-rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, the ovaries, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant Human CTGFL/WISP-2 is a 24.3 kDa protein consisting of 228 amino acid residues. Mature human CTGFL/WISP-2 is a 24.8 kDa polypeptide protein containing 227 amino acids. It is composed of 3 distinct domains; the IGF-Binding Protein domain (IGF-BP), the Thrombospondin type I repeat (TSP type I), and von Willebrand Factor C motif (VWFC).

Recombinant Human Wnt-1 (Legacy Tebubio ref. 167120-17). Wnt-1 is a secreted protein that signals through the Frizzled family of cell surface receptors, and is required for normal embryonic development. Wnt-1 activation induces a complex signaling cascade that ultimately leads to the increased expression of over fifty genes. An important component of Wnt-1 signaling is the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. Wnt signaling induces and maintains the transformed phenotype, and, in certain embryonic cell lines, supports self-renewal in the absence of significant differentiation. Elevated levels of Wnt proteins are associated with tumorigenesis, and are present in numerous human breast cancers. Mature human Wnt-1 is a glycosylated protein containing 343 amino acid residues. Recombinant Human Wnt-1 is a 38.4 kDa, non-glycosylated protein containing 343 amino acid residues.

Recombinant Human Wnt-1 (Legacy Tebubio ref. 167120-17). Wnt-1 is a secreted protein that signals through the Frizzled family of cell surface receptors, and is required for normal embryonic development. Wnt-1 activation induces a complex signaling cascade that ultimately leads to the increased expression of over fifty genes. An important component of Wnt-1 signaling is the stabilization, and resulting accumulation, of the intracellular signaling protein, beta-catenin. Wnt signaling induces and maintains the transformed phenotype, and, in certain embryonic cell lines, supports self-renewal in the absence of significant differentiation. Elevated levels of Wnt proteins are associated with tumorigenesis, and are present in numerous human breast cancers. Mature human Wnt-1 is a glycosylated protein containing 343 amino acid residues. Recombinant Human Wnt-1 is a 38.4 kDa, non-glycosylated protein containing 343 amino acid residues.

Recombinant Human WISP-1 (Legacy Tebubio ref. 167120-18). WISP-1 is a member of the CCN family of secreted, cysteine-rich regulatory proteins. It is expressed in the heart, kidney, lung, pancreas, placenta, ovary, small intestine and spleen. WISP-1 is a beta-catenin-regulated protein that can contribute to tumorigenesis, and has also been shown to play a role in bone development and fracture repair. Recombinant Human WISP-1 is a 38.1 kDa protein containing 345 amino acid residues. It is composed of four distinct structural domains (modules): the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the thrombospondin type-1 repeat (TSP type-1) domain, and a C-terminal cysteine knot-like (CTCK) domain.

Recombinant Human WISP-1 (Legacy Tebubio ref. 167120-18). WISP-1 is a member of the CCN family of secreted, cysteine-rich regulatory proteins. It is expressed in the heart, kidney, lung, pancreas, placenta, ovary, small intestine and spleen. WISP-1 is a beta-catenin-regulated protein that can contribute to tumorigenesis, and has also been shown to play a role in bone development and fracture repair. Recombinant Human WISP-1 is a 38.1 kDa protein containing 345 amino acid residues. It is composed of four distinct structural domains (modules): the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the thrombospondin type-1 repeat (TSP type-1) domain, and a C-terminal cysteine knot-like (CTCK) domain.

Recombinant Human CTGF (Legacy Tebubio ref. 167120-19). CTGF is a member of the CCN family of secreted cysteine-rich regulatory proteins, and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial and epithelial cells, and binds to IGF, TGF-beta1 and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans. CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Mature Human CTGF is a 38.0 kDa secreted protein containing 323 amino acid residues. CTGF is comprised of four distinct structural domains (modules), which are identified as IGF-Binding Protein (IGF-BP), von Willebrand Facto

Recombinant Human CTGF (Legacy Tebubio ref. 167120-19). CTGF is a member of the CCN family of secreted cysteine-rich regulatory proteins, and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial and epithelial cells, and binds to IGF, TGF-beta1 and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans. CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Mature Human CTGF is a 38.0 kDa secreted protein containing 323 amino acid residues. CTGF is comprised of four distinct structural domains (modules), which are identified as IGF-Binding Protein (IGF-BP), von Willebrand Facto