1mg
Showing 4101–4150 of 7910 results
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dTAG-13
Molecular Formula : C57H68N4O15
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Duloxetine-d3 Di-p-toluoyl-L-tartaric Acid Salt
Molecular Formula : C38H34D3NO9S
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Duloxetine-d3 Maleate
Molecular Formula : C18 D3 H16 N O S . C4 H4 O4
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Duloxetine-d7
Molecular Formula : C18H12D7NOS
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Duramycin (~90%)
Molecular Formula : C89H125N23O25S3
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Dutasteride Alpha-Dimer (~90%)
Molecular Formula : C46H55F6N3O4
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Dutasteride Beta-Dimer
Molecular Formula : C46 H55 F6 N3 O4
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Dutasteride-13C6
Molecular Formula : C2113C6H30F6N2O2
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Dydrogesterone-d6 (Major)
Molecular Formula : C21H22D6O2
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E- Ajoene (~20% in Ethyl Acetate)
Molecular Formula : C9H14OS3
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E-4-(Dimethylamino)cinnamaldehyde
Molecular Formula : C11H13NO
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E-Ceftazidime
Molecular Formula : C22H22N6O7S2
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E-N-Methyl-L-lysine-D4 Hydrochloride
Molecular Formula : C7H12D4N2O2.HCl
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Ebastine-d5
Molecular Formula : C32H34D5NO2
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Econazole-d6
Molecular Formula : C18 H9 D6 Cl3 N2 O
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Edaravone D5
Molecular Formula : C10 D5 H5 N2 O
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Edoxaban 4-Carboxylic Acid Hydrochloride
Molecular Formula : C22H25ClN6O5S . xHCl
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Efavirenz 1-Desamine
Molecular Formula : C26 H37 Cl O6
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Efavirenz 1-Desamine-1-oxy
Molecular Formula : C14H8ClF3O3
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Efinaconazole
Molecular Formula : C18 H22 F2 N4 O
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EGF Fc Chimera, Human
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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EGF R, His, Human
EGF Receptor, also known as ERBB, ERBB1 and HER1, is a type I transmembrane protein belonging to the tyrosine protein kinase family. It belongs to a family of tyrosine kinase receptors including Human EGF Receptors (HER) 2, 3, and 4 which all play important roles in cell growth and differentiation. Their primary ligands are EGF, Heparin-Binding EGF and Transforming Growth Factor α. Upon ligand binding, EGFR undergoes asymmetric dimerization, composed of an “activator” and a “receiver”. EGFR and its family members are disregulated in numerous cancers. In particular, EGFR is overexpressed in many epithelial solid tumors. Evidence suggests EGFR is an excellent target for pharmacologic intervention in Non Small Cell Lung Cancer (NSCLC) due to its high level of expression and prominent role in tumor growth and metastasis.
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EGF, His, Human
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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EGF, Human
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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EGF, Human
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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EGF, Mouse
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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EGF, Rat
Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. It is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature rat EGF shares 70 % a.a. sequence identity with mature human EGF.
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EGF, Rat (CHO-expressed)
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
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Eicosapentaenoic Acid-d5 (Technical)
Molecular Formula : C20 2H5 H25 O2
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EIDD 2801-D7
Molecular Formula : C13 D7 H12 N3 O7
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Elacridar-d4 (Major)
Molecular Formula : C34H29D4N3O5
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Elagolix Methoxy-d3 Sodium Salt
Molecular Formula : C32H26D3F5N3NaO5
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Elagolix-d6 Sodium Salt (Major)
Molecular Formula : C32H23D6F5N3NaO5
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Elaiophylin (>85%)
Molecular Formula : C54H88O18
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Elexacaftor-D3
Molecular Formula : C26 D3 H31 F3 N7 O4 S
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Eltenac
Molecular Formula : C12 H9 Cl2 N O2 S
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Eltenac-13C,d3
Molecular Formula : C12 H9 Cl2 N O2 S
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Eltrombopag-13C4
Molecular Formula : C2113C4H22N4O4
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Elvitegravir-d6 (Major)
Molecular Formula : C23H17D6ClFNO5
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Emamectin B1a
Molecular Formula : C49 H75 N O13
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Emamectin-D3
Molecular Formula : C49H72D3NO13
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Emetine (>90%)
Molecular Formula : C29 H40 N2 O4
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Emodin 1-Beta-D-Glucoside
Molecular Formula : C21H20O10
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Emodin 8-Beta-D-Glucoside
Molecular Formula : C21 H20 O10
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Emodin-d4
Molecular Formula : C15H6D4O5
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Empagliflozin R/S-Furanose
Molecular Formula : C23H27ClO7
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Emtricitabine Monophosphate Triethylammonium Salt
Molecular Formula : C8H11FN3O6PS . (C6H15N)ₓ
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Emtricitabine O-Beta-D-Glucuronide Sodium Salt
Molecular Formula : C14H17FN3NaO9S
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Emtricitabine Phosphonic Acid Triethylammonium Salt
Molecular Formula : C8 H10 F N3 O5 P S . C6 H13 N
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Emtricitabine Tenofovir Monosoproxil
Molecular Formula : C23H32FN8O10PS