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Single-use+Temperature+Sensor
Fournisseur:
BW TECHNOLOGIES GMBH
Description:
Accessoires pour systèmes de détection de gaz, Pour: Extreme, Replacement sensor, oxygen (O₂)
Numéro de catalogue:
(BOSSBS-5453R-A350)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-0290R-A555)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-0290R-FITC)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-5453R-A750)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-0290R-HRP)
Fournisseur:
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
Fournisseur:
Biotium
Description:
Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.
Numéro de catalogue:
(PRSI91-807)
Fournisseur:
ProSci Inc.
Description:
Tumor necrosis factor receptor superfamily member 19L (TNFRSF19L), also known as Receptor expressed in lymphoid tissues and RELT, is a member of the TNF-receptor superfamily. TNFRSF19L is a single-pass type membrane protein and contains one TNFR-Cys repeat. TNFRSF19L is highly expressed in spleen, lymph node, thymus, peripheral blood leukocytes, bone marrow and fetal liver. It has been shown TNFRSF19L activates the NF-kappaB pathway and selectively binds TNF receptor-associated factor 1 (TRAF1). TNFRSF19L is capable of stimulating T-cell proliferation in the presence of CD3 signaling, which suggests its regulatory role in immune response.
UOM:
1 * 0,05 mg
New Product
Numéro de catalogue:
(BOSSBS-5150R-A680)
Fournisseur:
Bioss
Description:
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5150R-FITC)
Fournisseur:
Bioss
Description:
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0787R-HRP)
Fournisseur:
Bioss
Description:
Interferon-Beta, IFN-Beta mainly by the fibroblast cell factor, belonging to a single gene encodes a protein that can interfere with the virus RNA or DNA replication and inhibit virus growth, and significantly enhance NK cell activity, through the promotion of MHC â… molecule expression and enhance the CTL of the virus-infected cells role in the identification and destruction.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5009R-A488)
Fournisseur:
Bioss
Description:
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5009R-CY5)
Fournisseur:
Bioss
Description:
Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3889R-A555)
Fournisseur:
Bioss
Description:
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0787R-A647)
Fournisseur:
Bioss
Description:
Interferon-Beta, IFN-Beta mainly by the fibroblast cell factor, belonging to a single gene encodes a protein that can interfere with the virus RNA or DNA replication and inhibit virus growth, and significantly enhance NK cell activity, through the promotion of MHC â… molecule expression and enhance the CTL of the virus-infected cells role in the identification and destruction.
UOM:
1 * 100 µl
Fournisseur:
NABERTHERM
Description:
The BO series is specially designed for processes in which larger sample quantities must be incinerated. Mainly used in the fields such as ashing of food, thermal cleaning of injection molding tools or determination of annealing loss.
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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