
Katalognummer: 209 - 103-M287
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 100 µg
103-M287
Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Hedgehogs are synthesized as 45 kDa precursors that are cleaved autocatalytically. The 19 kDa Nterminal fragment remains membrane associated due to its cholesterol and palmitate modifications. Binding of this fragment to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip). Within the N-terminal peptide, mouse Dhh shares 97% and 100% amino acid (aa) sequence identity with human and rat Dhh, respectively. It shares 74% aa seqeuence identity with mouse Indian (Ihh) and Sonic hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1 which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. In humans, mutations of Dhh are associated with pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corpus luteum. Its upregulation in human ovarian cancer correlates positively with proliferative index and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in nerve fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.
103-M228
Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Hedgehogs are synthesized as 45 kDa precursors that are cleaved autocatalytically. The 19 kDa Nterminal fragment remains membrane associated due to its cholesterol and palmitate modifications. Binding of this fragment to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip). Within the N-terminal peptide, mouse Dhh shares 97% and 100% amino acid (aa) sequence identity with human and rat Dhh, respectively. It shares 74% aa seqeuence identity with mouse Indian (Ihh) and Sonic hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1 which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. In humans, mutations of Dhh are associated with pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corpus luteum. Its upregulation in human ovarian cancer correlates positively with proliferative index and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in nerve fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.
103-M186
Axl (Ufo, Ark), Dtk (Sky, Tyro3, Rse, Brt) and Mer (human and mouse homologues of chicken cEyk) constitute a new receptor tyrosine kinase subfamily. The extracellular domain of these proteins contain two Ig-like motifs and two fibronectin type III motifs. This characteristic topology is also found in neural cell adhesion molecules and in receptor tyrosine phosphatases. All three receptors bind the vitamin K-dependent protein growth-arrest specific gene 6 (Gas6) which is structurally related to the anti-coagulation factor protein S. The binding affinities for Gas6 is in the order of Axl > Dtk > Mer. Gas6 binding induces tyrosine phosphorylation and downstream signaling pathways that can lead to cell proliferation, migration, or the prevention of apoptosis. Dtk is widely expressed during embryonic development. In adults, Dtk is predominantly expressed in neurons in restricted regions of the brain.
103-M188
Axl (Ufo, Ark), Dtk (Sky, Tyro3, Rse, Brt) and Mer (human and mouse homologues of chicken c-Eyk) constitute a receptor tyrosine kinase subfamily. The extracellular domains of these proteins contain two Ig-like motifs and two fibronectin type III motifs. This characteristic topology is also found in neural cell adhesion molecules and in receptor tyrosine phosphatases. These receptors bind the vitamin K-dependent protein growth-arrest-specific gene 6 (Gas6) which is structurally related to the anti-coagulation factor protein S. Binding of Gas6 induces receptor autophosphorylation and downstream signaling pathways that can lead to cell proliferation, migration or the prevention of apoptosis. Recent studies suggest that this family of tyrosine kinase receptors may be involved in hematopoiesis, embryonic development, tumorigenesis and regulation of testicular functions.
103-M192
The GDNF family of neurotrophic factors consititute a new family of factors within the TGFβ superfamily. These proteins are potent survival factors for various central and peripheral neurons during development and in the adult animal. The GDNF family members (GDNF, neurturin and persephin) signal through multicomponent receptors that consist of the Ret receptor tyrosine kinase and one of four glycosylphosphatidylinositol (GPI)linked ligandbinding subunits (GFRα14). GFRα1, 2, and 4 are the preferred ligandbinding subunits for GDNF, neurturin and persephin, respectively. To date, the preferred ligand for GFRα3 has not been identified. The Ret tyrosinekinase receptor is encoded by the cret protooncogene. Mutations of the ret gene have been associated with various human diseases affecting tissues derived from the neural crest, including Hirschsprung’s disease, multiple endocrine neoplasia MEN2A and MEN2B, and familial medullary thyroid carcinoma. Mouse Ret cDNA encodes a 1115 amino acid (aa) residue transmembrane tyrosine kinase with a 28 aa residue signal peptide, a 609 aa residue cysteine-rich extracellular domain and a 456 aa residue cytoplasmic domain. A cadherin-related sequence is also present in the extracellular domain of Ret. Human and mouse Ret share 83% amino acid sequence homology (77% homology in the extracellular domain and 93% homology in the cytoplasmic domain). Although Ret does not bind GDNF ligands directly, the extracellular domain of Ret binds the GDNFGFRα complex with high affinity and is a potent GDNF antagonist in the presence of soluble GFRα.

By: Author , 2 Comment
23 August 2025

By: Author , 2 Comment
16 August 2025

By: Author , 2 Comment
1 August 2025

By: Author , 2 Comment
22 July 2025

