Other Proteins

Recombinant Human sFRP-4 (Legacy Tebubio ref. 167120-50). Secreted Frizzled-Related Proteins (sFRPs) are a family of glycosylated Wnt antagonists characterized by a conserved cysteine-rich domain that shares homology with the cysteine-rich, extracellular domain Frizzled proteins use for the binding of Wnt proteins and receptors. Lacking the transmembrane and intracellular domains of the Frizzled proteins, sFRPs function as soluble modulators of the Wnt signaling pathway through the direct binding of Wnt proteins to this cysteine-rich domain, and the resultant inhibition of Wnt receptor binding and signaling capabilities. sFRP-4 is widely distributed in a variety of embryonic and adult tissues where it can function as a circulating antiangiogenic factor, a potent proapoptotic factor, an inhibitor of insulin secretion, and a suppressor of both tumor growth and metastatic potential through disruption of the Wnt signaling pathway. Research has demonstrated the existence of a direct correla

Recombinant Human sFRP-4 (Legacy Tebubio ref. 167120-50). Secreted Frizzled-Related Proteins (sFRPs) are a family of glycosylated Wnt antagonists characterized by a conserved cysteine-rich domain that shares homology with the cysteine-rich, extracellular domain Frizzled proteins use for the binding of Wnt proteins and receptors. Lacking the transmembrane and intracellular domains of the Frizzled proteins, sFRPs function as soluble modulators of the Wnt signaling pathway through the direct binding of Wnt proteins to this cysteine-rich domain, and the resultant inhibition of Wnt receptor binding and signaling capabilities. sFRP-4 is widely distributed in a variety of embryonic and adult tissues where it can function as a circulating antiangiogenic factor, a potent proapoptotic factor, an inhibitor of insulin secretion, and a suppressor of both tumor growth and metastatic potential through disruption of the Wnt signaling pathway. Research has demonstrated the existence of a direct correla

Recombinant Human sFRP-5 (Legacy Tebubio ref. 167120-53). Secreted Frizzled Related Proteins (sFRPs) are a family of glycosylated Wnt antagonists that inhibit Wnt signaling, either by directly binding to Wnt proteins to prevent their binding to Frizzled (Fz) family receptor proteins or by forming non‐functional interactions with Frizzled receptors. sFRPs share homology with the cysteine‐rich, extracellular domain of Frizzled proteins. sFRP‐5 is secreted in a variety of embryonic and adult tissues. During embryonic development, sFRP‐5 regulates formation of the retina, brain, trunk, foregut, anterior visceral endoderm, and epithelial structures through Wnt and BMP inhibition. In adults, sFRP‐5 is expressed by adipocytes, particularly in white adipose tissue, and acts as an anti‐inflammatory adipokine. Shown to improve metabolic function and reduce adipose tissue inflammation, sFRP‐5 also acts in a cardio‐protective manner after ischemia and reperfusion injury in the heart, suppressing t

Recombinant Human sFRP-5 (Legacy Tebubio ref. 167120-53). Secreted Frizzled Related Proteins (sFRPs) are a family of glycosylated Wnt antagonists that inhibit Wnt signaling, either by directly binding to Wnt proteins to prevent their binding to Frizzled (Fz) family receptor proteins or by forming non‐functional interactions with Frizzled receptors. sFRPs share homology with the cysteine‐rich, extracellular domain of Frizzled proteins. sFRP‐5 is secreted in a variety of embryonic and adult tissues. During embryonic development, sFRP‐5 regulates formation of the retina, brain, trunk, foregut, anterior visceral endoderm, and epithelial structures through Wnt and BMP inhibition. In adults, sFRP‐5 is expressed by adipocytes, particularly in white adipose tissue, and acts as an anti‐inflammatory adipokine. Shown to improve metabolic function and reduce adipose tissue inflammation, sFRP‐5 also acts in a cardio‐protective manner after ischemia and reperfusion injury in the heart, suppressing t

Recombinant Human INSL5/INSL7 Hybrid (Legacy Tebubio ref. 167130-05). The Insulin/Relaxin structural family of proteins consists of at least seven members, each containing an insulin-like heterodimeric structure of two polypeptide chains held together by two inter-chain disulfide bonds. The INSL5/INSL7 hybrid contains the beta-chain of INSL7 (Relaxin-3), linked to the alpha-chain of INSL5. The INSL5/INSL7 hybrid protein can specifically activate the G protein-coupled receptors, GPCR135 and GPCR142, but unlike Relaxin-3, does not induce significant activation of the LGR7 receptor. Recombinant Human INSL5/INSL7 hybrid is a heterodimeric, 5.2 kDa protein consisting of a 27 amino acid beta-chain linked to a 21 amino acid alpha-chain by two disulfide bonds.

Recombinant Human INSL5/INSL7 Hybrid (Legacy Tebubio ref. 167130-05). The Insulin/Relaxin structural family of proteins consists of at least seven members, each containing an insulin-like heterodimeric structure of two polypeptide chains held together by two inter-chain disulfide bonds. The INSL5/INSL7 hybrid contains the beta-chain of INSL7 (Relaxin-3), linked to the alpha-chain of INSL5. The INSL5/INSL7 hybrid protein can specifically activate the G protein-coupled receptors, GPCR135 and GPCR142, but unlike Relaxin-3, does not induce significant activation of the LGR7 receptor. Recombinant Human INSL5/INSL7 hybrid is a heterodimeric, 5.2 kDa protein consisting of a 27 amino acid beta-chain linked to a 21 amino acid alpha-chain by two disulfide bonds.

Recombinant Human ANG-1 (Legacy Tebubio ref. 167130-06). Angiopoietin-1 (ANG-1) is a secreted ligand for Tie-2, a tyrosine-kinase receptor expressed primarily on vascular endothelial cells and early hematopoietic cells. ANG-1/Tie-2 signaling promotes angiogenesis during the development, remodeling, and repair of the vascular system. Transgenic mice lacking expression of either ANG-1 or Tie-2 fail to develop a fully functional cardiovascular system and die before birth. Postnatally, the angiogenic activity of ANG-1/Tie-2 is required during normal tissue repair and remodeling of the female endometrium in the menstrual cycle. ANG-1/Tie-2 signaling appears to be regulated by Angiopoietin-2 (ANG-2), a natural antagonist for Tie-2 that exerts its effects through an internal autocrine loop mechanism. In addition to suppressing endothelial cell activation by inhibiting the expression of adhesion and inflammatory molecules, ANG-1 enhances endothelial cell survival and capillary morphogenesi

Recombinant Human ANG-1 (Legacy Tebubio ref. 167130-06). Angiopoietin-1 (ANG-1) is a secreted ligand for Tie-2, a tyrosine-kinase receptor expressed primarily on vascular endothelial cells and early hematopoietic cells. ANG-1/Tie-2 signaling promotes angiogenesis during the development, remodeling, and repair of the vascular system. Transgenic mice lacking expression of either ANG-1 or Tie-2 fail to develop a fully functional cardiovascular system and die before birth. Postnatally, the angiogenic activity of ANG-1/Tie-2 is required during normal tissue repair and remodeling of the female endometrium in the menstrual cycle. ANG-1/Tie-2 signaling appears to be regulated by Angiopoietin-2 (ANG-2), a natural antagonist for Tie-2 that exerts its effects through an internal autocrine loop mechanism. In addition to suppressing endothelial cell activation by inhibiting the expression of adhesion and inflammatory molecules, ANG-1 enhances endothelial cell survival and capillary morphogenesi

Recombinant Human ANG-2 (Legacy Tebubio ref. 167130-07). ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an alpha-helix-rich "coiled coil" N-terminal domain and fibrinogen-like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer. Recombinant Human ANG-2 is a C-terminal histidine-tagged glycoprot