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FGF-2/bFGF-4 inquiry  | Purity Not Available

Protheragen

FGF basic is a member of the FGF family, currently comprised of seven related mitogenic proteins which show 35 – 55% amino acid conservation. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF basic retains […]

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FGF-2/bFGF-2 inquiry  | Purity Not Available

Protheragen

FGF basic, also known as FGF-2 and HBGF-2, is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. Human FGF acidic shares 54% amino acid (aa) sequence identity with FGF basic and 17%-_x001F_33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, […]

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FGF-2/bFGF-3 inquiry  | Purity Not Available

Protheragen

FGF basic, also known as FGF-2 and HBGF-2, is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. Human FGF acidic shares 54% amino acid (aa) sequence identity with FGF basic and 17%-_x001F_33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, […]

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aFGF-2 inquiry  | Purity Not Available

Protheragen

Murine aFGF, encoded by the FGF1 gene, is a member of the fibroblast growth factor (FGF) family. Fibroblast growth factor was found in pituitary extracts in 1973 and then tested in a bioassay that caused fibroblasts to proliferate. After further fractionating the extract using acidic and basic pH, two different forms have isolated that named […]

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FGF-2/bFGF-1 inquiry  | Purity Not Available

Protheragen

FGF-2, also known as basic fibroblast growth factor, is a canonical FGF that belongs to the FGF-1 subfamily. It is a regulator of proliferation, migration, differentiation, cell survival, and stemness in human stem cells. More over,FGF-2 play a major role in skeletal development, bone formation, and fracture repair, which make FGF-2 an attractive molecule for […]

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aFGF-1 inquiry  | Purity Not Available

Protheragen

FGF-acidic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle […]

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GMF-β-2 inquiry  | Purity Not Available

Protheragen

The glia maturation factor beta belongs to the actin-binding proteins ADF family, GMF subfamily. It contains an ADF-H domain, but the research of crystallography and NMR reveals that there are structures different between human and mouse ADF-H domain. GMF-β is involved in the differentiation, maintenance, and regeneration of the nervous system. It also inhibition of […]

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GMF-β-1 inquiry  | Purity Not Available

Protheragen

The glia maturation factor beta belongs to the actin-binding proteins ADF family, GMF subfamily. It contains an ADF-H domain, but the research of crystallography and NMR reveals that there are structures different between human and mouse ADF-H domain. GMF-β is involved in the differentiation, maintenance, and regeneration of the nervous system. It also inhibition of […]

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Neuritin inquiry  | Purity Not Available

Protheragen

Neuritin also known as NRN1 and CPG15 is a neurotrophic factor, which is expressed in response to induction of neuronal activity by NGF, BDNF, NT3 and other neural stimulators. It promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. Recombinant Human Neuritin is a covalently disulfide-linked homodimer, consisting of […]

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NRG1-α inquiry  | Purity Not Available

Protheragen

The neuregulin family of structurally related glycoproteins comprises products from four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. All NRG1 isoforms contain an EGF-like domain that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in tyrosine […]

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