Other Proteins

Recombinant Human BMP-3 (Legacy Tebubio ref. 167120-24B). TGF-beta family members are key modulators of cell proliferation, differentiation, matrix synthesis, and apoptosis. As implied by their name, BMPs initiate, promote, and regulate the development, growth, and remodeling of bone and cartilage. In addition to this role, BMPs are also involved in prenatal development and postnatal growth, remodeling and maintenance of a variety of other tissues and organs. BMP-3 is abundantly found in adult bone and, to a lesser extent, fetal cartilage. BMP-3 inhibits osteogenesis and bone formation by activating a signaling cascade that antagonizes the signaling of pro-osteogenic BMPs. Recombinant Human BMP-3 is a disulfide-linked homodimeric protein that corresponds to residues 361 to 472 of the 472 amino acid BMP-3 precursor protein. The calculated molecular weight of Recombinant Human BMP-3 is 25.2 kDa.

Recombinant Human CYR61 (Legacy Tebubio ref. 167120-25). CYR61 is a member of the CCN family of secreted cysteine-rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant Human CYR61 is a 39.5 kDa protein containing 357 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-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).

Recombinant Human CYR61 (Legacy Tebubio ref. 167120-25). CYR61 is a member of the CCN family of secreted cysteine-rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant Human CYR61 is a 39.5 kDa protein containing 357 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-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).

Recombinant Human NOV (Legacy Tebubio ref. 167120-26). NOV is a member of the CCN family of secreted, cysteine-rich regulatory proteins. The full-length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm's tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorigenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell-surface integrins, and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant Human NOV is a 36.2 kDa protein containing 331 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

Recombinant Human NOV (Legacy Tebubio ref. 167120-26). NOV is a member of the CCN family of secreted, cysteine-rich regulatory proteins. The full-length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm's tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorigenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell-surface integrins, and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant Human NOV is a 36.2 kDa protein containing 331 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

Recombinant Human sFRP-1 (Legacy Tebubio ref. 167120-29). Secreted Frizzled Related Proteins (sFRPs) modulate WNT signaling by binding directly to WNT proteins in a manner that affects their receptor binding and signaling capabilities. sFRP-1 is a widely distributed protein that can bind directly to WNT1, WNT2, and possibly other WNT proteins, and generally exerts anti-proliferative effects consistent with activity as a WNT antagonist. It also inhibits apoptosis, and has been found to be down-regulated in many solid tumors, but up-regulated in uterine leiomyomas. Recombinant Human sFRP-1 is a glycosylated 283 amino acid protein containing a cysteine-rich Frizzled homologous domain. The calculated molecular weight of Recombinant Human sFRP-1 is 32.5 kDa.

Recombinant Human sFRP-1 (Legacy Tebubio ref. 167120-29). Secreted Frizzled Related Proteins (sFRPs) modulate WNT signaling by binding directly to WNT proteins in a manner that affects their receptor binding and signaling capabilities. sFRP-1 is a widely distributed protein that can bind directly to WNT1, WNT2, and possibly other WNT proteins, and generally exerts anti-proliferative effects consistent with activity as a WNT antagonist. It also inhibits apoptosis, and has been found to be down-regulated in many solid tumors, but up-regulated in uterine leiomyomas. Recombinant Human sFRP-1 is a glycosylated 283 amino acid protein containing a cysteine-rich Frizzled homologous domain. The calculated molecular weight of Recombinant Human sFRP-1 is 32.5 kDa.

Recombinant Human DKK-1 (Legacy Tebubio ref. 167120-30). DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head-forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play important regulatory roles in the Wnt/beta-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/beta-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/beta-catenin signaling cascade. It has been suggested that by inhibiting Wnt/beta-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis

Recombinant Human DKK-1 (Legacy Tebubio ref. 167120-30). DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head-forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play important regulatory roles in the Wnt/beta-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/beta-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/beta-catenin signaling cascade. It has been suggested that by inhibiting Wnt/beta-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis