H_Products

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. PTH is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is secreted as a C-terminal fragment (7-84) when extracellular calcium levels are high, offsetting the effects of PTH. PTH (7-84) acts as an antagonist for PTH1R, as well as a possible carboxy-terminus interacting PTH receptor. PTH and truncated PTH fragments play a major role in bone metabolism and calcium homeostasis, as well as renal excretion. This particular product has been labeled with the stable 15N isotope to help track its activity.

Human Parathyroid Hormone (PTH) is a hormone expressed and secreted as preproPTH by chief cells of the parathyroid glands when extracellular calcium levels are low. PTH is coexpressed with furin, the enzyme believed to be responsible for processing proPTH to PTH. PTH is secreted as a C-terminal fragment (7-84) when extracellular calcium levels are high, offsetting the effects of PTH. PTH (7-84) acts as an antagonist for PTH1R, as well as a possible carboxy-terminus interacting PTH receptor. PTH and truncated PTH fragments play a major role in bone metabolism and calcium homeostasis, as well as renal excretion.

Sterile Filtered White lyophilized powder. Purified and tested for use in cell culture.

Parathyroid hormone (PTH) is a single polypeptide of 84 amino acids. It is a critical hormone in the regulation of Ca2+ homeostasis and is secreted by the parathyroid glands. These glands promote the release of calcium from bone into the blood stream by activating osteoblasts and inhibiting osteoclasts. Secretion of PTH increases when the level of calcium in the extracellular fluid is low. When there is more Ca2+ in the blood, there is increased intestinal absorption of calcium, renal tubular reabsorption of calcium and increased renal excretion of phosphates. Therefore, PTH is a major regulator of bone metabolism.

Human parathyroid hormone-like hormone (PTHLH) is a hormone that is expressed in mammary glands, as well as cancer cells. Alternative splicing results in different length isoforms of PTHLH. It is involved in a diverse array of processes. PTHLH plays a key role during endochondral ossification by regulating chondrocyte proliferation, differentiation, and apoptosis. It also regulates epithelial-mesenchymal interactions during development of mammary glands and teeth and interacts with dermal fibroblasts to modulate routine skin cell growth and maintenance. PTHLH is a ligand for the PTH1 receptor that is also affected by PTH. This particular product has been labeled with the stable 15N isotope to help track its activity.

Human parathyroid hormone-like hormone (PTHLH) is expressed in mammary glands as well as cancer cells. Alternative splicing results in different length isoforms of PTHLH. It is involved in a diverse array of processes. PTHLH plays a key role during endochondral ossification by regulating chondrocyte proliferation, differentiation, and apoptosis. It also regulates epithelial-mesenchymal interactions during development of mammary glands and teeth and interacts with dermal fibroblasts to modulate routine skin cell growth and maintenance. PTHLH is a ligand for the PTH1 receptor that is also affected by PTH.

Pleiotrophin (PTN) is a heparin-binding protein, expression of which is developmentally regulated. It is expressed primarily in brain tissues, but is also expressed in lung, kidney, gut, and bone tissues and can be induced by PDGF. PTN is expressed in some tumor cells as well. PTN is involved in a diverse array of functions including mitogenesis, angiogenesis, tissue repair, and neurite outgrowth. It exhibits strong mitogenic activity towards hepatocytes and plays a role in liver regeneration. PTN binds to several different receptors including syndecan-3, PTP-zeta, and ALK. The nucleotide sequence of Human pleiotrophin is about 50% homologous to human midkine (MDK).

Serpin Peptidase Inhibitory, clade F (SERPINF1), previously called Pigment epithelium-derived factor (PEDF), is encoded by the SERPINF1 gene in humans and found in vertebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. SERPINF1 is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 amino acid, ~50 kDa precursor that contains a 19 amino acid signal sequence and a 399 amino acid mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity, SERPINF1 has induces extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. SERPINF1 is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer.

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. Each Hh protein has a unique expression pattern and distinct biological role within its respective region of secretion. All Hh proteins use the same signaling pathway and can substitute for each other in experimental systems. Shh has been found to have a critical role in development, acting as a morphogen in the patterning of limbs, brain structure, spinal cord, thalamus and the teeth. Shh has been shown to attract commissural axons in the developing spinal cord by attracting or repelling retinal ganglion cell (RGC) axons depending on concentration.

Sodium 3-hydroxybutyrate is a biochemical used in proteomics research.

Tumor necrosis factor (or TNF-α), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages, NK-cells, LAK-cells, astrocyte endothelial cells, smooth muscle cells and some transformed cells. TNF occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally occurring form of TNF is glycosylated, but nonglycosylated recombinant TNF has comparable biological activity. The biologically active native form of TNF is reportedly a trimer. Human and murine TNF has approximately 79% homology at the amino acid level and there is cross-reactivity between the two species. Two types of receptors for TNF, p55 and p75, have been described and virtually all cell types studied show the presence of one or both of these receptor types.

Tumor necrosis factor (or TNF-α), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages, NK-cells, LAK-cells, astrocyte endothelial cells, smooth muscle cells and some transformed cells. TNF occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally occurring form of TNF is glycosylated, but nonglycosylated recombinant TNF has comparable biological activity. The biologically active native form of TNF is reportedly a trimer. Human and murine TNF has approximately 79% homology at the amino acid level and there is cross-reactivity between the two species. Two types of receptors for TNF, p55 and p75, have been described and virtually all cell types studied show the presence of one or both of these receptor types.

The clinical use of the potent antitumor activity of TNF has been limited by the pro-inflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis and hemorrhage. Designing clinically applicable TNF mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF variants, which bind to the murine TNF-R55 but not to the murine TNF-R75, exhibit retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF, which binds to both murine TNF receptors. Based on these results, many TNF mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.

Tumor necrosis factor (or TNF-α), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages, NK-cells, LAK-cells, astrocyte endothelial cells, smooth muscle cells and some transformed cells. TNF occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF is glycosylated, but nonglycosylated recombinant TNF has comparable biological activity. The biologically active, native form of TNF is reportedly a trimer. Human and murine TNF has approximately 79% homology at the amino acid level and there is cross-reactivity between the two species. Two types of receptors for TNF, p55 and p75, have been described and virtually all cell types studied show the presence of one or both of these receptor types.

Thymic stromal lymphopoietin (TSLP) is a hemopoietic protein belonging to the cytokine family and is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. It is mainly expressed in tissues, including heart, liver and prostate. TSLP signals through a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor and the IL7R alpha chain. Like IL7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. After binding STAT5, phosphorylation is induced which results in the expression of downstream transcription factors. TSLP enhances the maturation of CD11c+ dendritic cells and induces allergic inflammation by directly activating mast cells. TSLP’s expression is linked to many disease states including asthma, inflammatory arthritis, atopic dermatitis, and eczema and other allergic states but the factors which induce the activation of TSLP release are not clearly defined. Human TSLP shares approximately 43 % amino acid sequence identity with mouse TSLP.

XCL1 is a chemokine lacking the first and third conserved cysteine residues usually found in chemokines. It is expressed in thymic and peripheral blood CD8+ T-cells and in natural killer cells. Highest levels of expression are seen in spleen, thymus, small intestine, and peripheral blood leukocytes. XCL1 is chemotactic for natural killer cells and CD4+ and CD8+ T-cells. It assumes two distinct conformations, one of which has been shown to inhibit HIV-1 isolates. XCL1 is a ligand for XCR1 as well as the virus-encoded viroreceptor M3.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!