You Searched For: Intrinsic+factor

Catalog Number: (BOSSBS-5453R-CY3)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

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Catalog Number: (BOSSBS-5453R-FITC)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

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Catalog Number: (BOSSBS-6216R)

Supplier: Bioss

Description: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity)

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Catalog Number: (BOSSBS-12876R-A488)

Supplier: Bioss

Description: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

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Catalog Number: (BOSSBS-12876R-CY5)

Supplier: Bioss

Description: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12876R-A350)

Supplier: Bioss

Description: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12876R-A680)

Supplier: Bioss

Description: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12876R-A750)

Supplier: Bioss

Description: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0290R-CY7)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0290R-HRP)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5453R-A750)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0290R-A555)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5453R-A350)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0290R-FITC)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-5453R-CY7)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-5453R-A680)

Supplier: Bioss

Description: The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

UOM: 1 * 100 µl

Sale