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Th1263 details
Primary information
ID11864
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesAmino Acids, Peptides, and Proteins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameDeschiens Sirop
CompanyRodeca Inc., Division Of Technilab Inc.
Brand DescriptionRodeca Inc., Division Of Technilab Inc.
Prescribed ForOral
Chemical Name8.3 g / 100 mL
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID11865
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesBlood Proteins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID11866
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesGlobins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID11867
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesHemeproteins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID11868
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesHemoglobins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA


Primary information
ID11869
Therapeutic IDTh1263
Protein NameHemoglobin
Sequence>Th1263_Hemoglobin MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
Molecular WeightNA
Chemical FormulaNA
Isoelectric PointNA
HydrophobicityNA
Melting pointNA
Half-lifeNA
DescriptionThe respiratory protein of the red blood cells. It consists primarily of globin and heme.
Indication/DiseaseInvestigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.
PharmacodynamicsNA
Mechanism of ActionA heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.
ToxicityNA
MetabolismThere is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis
AbsorptionNA
NA
ClearanceNA
CategoriesProteins
Patents NumberNA
Date of IssueNA
Date of ExpiryNA
Drug InteractionNA
TargetNA
Brand NameNA
CompanyNA
Brand DescriptionNA
Prescribed ForNA
Chemical NameNA
FormulationNA
Physical Appearance NA
Route of AdministrationNA
Recommended DosageNA
ContraindicationNA
Side EffectsNA
Useful Link 1Link
Useful Link 2NA
RemarksNA