GenScript Biotech

Neuregulins or neuroregulins are a family of four structurally related proteins (NRG1, NRG2, NRG3 and NRG4) that are members of the EGF family of proteins. Studies indicate neuregulins function in nervous system development with essential roles in vertebrate embryogenesis including: cardiac development, Schwann cell and oligodendrocyte differentiation, certain aspects of neuronal development, and the formation of neuromuscular synapses. Neuregulin 1 is essential for the normal development of the nervous system and the heart. It is produced in numerous isoforms by alternative splicing, allowing it to perform a variety of functions. All NRG1 isoforms contain an EGF-like domain that is required for direct binding to ErbB3 or ErbB4 receptor tyrosine kinases. The transmembrane NRG1 isoforms contain an extracellular domain that can be proteolytically cleaved to release soluble growth factors.

Neuregulins or neuroregulins are a family of four structurally related proteins (NRG1, NRG2, NRG3 and NRG4) that are members of the EGF family of proteins. Studies indicate neuregulins function in nervous system development with essential roles in vertebrate embryogenesis including: cardiac development, Schwann cell and oligodendrocyte differentiation, certain aspects of neuronal development, and the formation of neuromuscular synapses. Neuregulin 1 is essential for the normal development of the nervous system and the heart. It is produced in numerous isoforms by alternative splicing, allowing it to perform a variety of functions. All NRG1 isoforms contain an EGF-like domain that is required for direct binding to ErbB3 or ErbB4 receptor tyrosine kinases. The transmembrane NRG1 isoforms contain an extracellular domain that can be proteolytically cleaved to release soluble growth factors.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

Hepatocyte Growth Factor (HGF),also known as hepatopoietin-A and scatter factor, is a pleiotropic mitogen belonging to the peptidase S1 family (plasminogen subfamily). It is produced by mesenchymal cells and acts on epithelial cells, endothelial cells and haemopoietic progenitor cells. HGF binds to the proto-oncogenic c-Met receptor to activate a tyrosine kinase signaling cascade. It regulates cell growth, motility and morphogenesis, thus it plays a pivotal role in angiogenesis, tumorogenesis and tissue regeneration.

c-Met, also called tyrosine-protein kinase Met or hepatocyte growth factor receptor (HGFR), is a protein that in humans is encoded by the MET gene. The protein possesses tyrosine kinase activity. The primary single chain precursor protein is post-translationally cleaved to produce the alpha and beta subunits, which are disulfide linked to form the mature receptor. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling.

Histone H3 is one of the five main histones involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the “beads on a string” structure. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 – 43 and 178 – 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 – 43 and 178 – 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

Heregulin1-Beta1(HRG1-Beta1) is one of the isoforms encoded by Neuregulin (NRG) genes. NRGs are synthesized as large transmembrane precursor proteins, and the NRG family has 4 members and 26 isoforms. These isoforms provide large diversities, including different tissue distribution, variable potencies, and different biological functions. HRG1-β1 belongs to Type I HRG1, and is expressed in neural tissue, respiratory epithelia, and heart. In vivo, HRG1 binds and activates both ErbB3 and ErbB4, the transmembrane receptor tyrosine kinase, and is involved in the proliferation, differentiation, and survival of cells. Aberrantly produced HRG1 could be used in the constitute activation of the ErbB receptors; therefore, the upregulation of HRG1 contributes to the development of tumors, including breast cancer.

Heregulin1-Beta1(HRG1-Beta1) is one of the isoforms encoded by Neuregulin (NRG) genes. NRGs are synthesized as large transmembrane precursor proteins, and the NRG family has 4 members and 26 isoforms. These isoforms provide large diversities, including different tissue distribution, variable potencies, and different biological functions. HRG1-β1 belongs to Type I HRG1, and is expressed in neural tissue, respiratory epithelia, and heart. In vivo, HRG1 binds and activates both ErbB3 and ErbB4, the transmembrane receptor tyrosine kinase, and is involved in the proliferation, differentiation, and survival of cells. Aberrantly produced HRG1 could be used in the constitute activation of the ErbB receptors; therefore, the upregulation of HRG1 contributes to the development of tumors, including breast cancer.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.