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Fournisseur:  Bioss
Description:   This gene encodes a member of the gamma-glutamyl transpeptidase (GGT) family, which are important in the metabolism of glutathione. The most ubiquitously expressed human GGT gene, GGT1, encodes a single transmembrane polypeptide that is post-translationally processed to form a heavy and a light chain. In contrast, the product of this gene only contains homology to the light chain region, and lacks a transmembrane domain. Multiple alternatively spliced variants, encoding the same protein, have been identified.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-5990R)

Fournisseur:  Bioss
Description:   This gene encodes a member of the ALEX family of proteins which may play a role in tumor suppression. The encoded protein contains a potential N-terminal transmembrane domain and a single Armadillo (arm) repeat. Other proteins containing the arm repeat are involved in development, maintenance of tissue integrity, and tumorigenesis. This gene is closely localized with other family members on the X chromosome. Three transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008].
UOM:  1 * 100 µl

Fournisseur:  Corning
Description:   HTS insert plates are arrays of individual cell culture inserts connected by a rigid, robotics-friendly holder. This single-unit design makes insert plates ideal for running automated, high throughput drug transport (Caco-2 cells) cell toxicity studies or cell migration and invasion studies.
UOM:  1 * 5 ST
Numéro de catalogue: (BOSSBS-0290R-CY7)

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:  Avantor Fluid Handling
Description:   Instantly shuts down the drive if the pump head is opened during operation.
UOM:  1 * 1 ST
ETL listed ISO9001 CE Compliant
Numéro de catalogue: (BOSSBS-11328R-A555)

Fournisseur:  Bioss
Description:   The brain-specific STEP (striatal enriched phosphatase) family of protein tyrosine phosphatases (PTPs) comprises both transmembrane and cytosolic protein members which are the products of alternative splicing. STEP family members are expressed in the dopaminoceptive neurons of the CNS, with highest expression in the basal ganglia and related structures. The STEP protein regulates the N-methyl-d-aspartate receptor (NMDAR) complex; STEP depresses both NMDAR single-channel activity and synaptic currents. The membrane-associated STEP61 isoform localizes in the postsynaptic densities (PSDs) of striatal neurons. STEP61 contains a single tyrosine phosphatase domain, two proline-rich domains and two transmembrane domains. The STEP61 protein associates with the Src family kinase member Fyn when Fyn is phosphorylated at Tyr-420 and not Tyr-431. Upon association, STEP61 dephosphorylates Tyr-420 residue and may thus regulate Fyn activity in PSDs. Isolated from mouse brain, the STEP20 isoform lacks the conserved tyrosine phosphatase domain. The human STEP gene maps to chromosome 11p15.2-p15.1.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-9546R-CY5)

Fournisseur:  Bioss
Description:   FIBCD1 is a 461 amino acid single-pass membrane protein that contains one fibrinogen C-terminal domain and exists as multiple alternatively spliced isoforms. The gene encoding FIBCD1 maps to human chromosome 9, which contains 145 million base pairs, comprises 4% of the human genome and encodes nearly 900 genes.
UOM:  1 * 100 µl
Fournisseur:  WTW
Description:   Tripod foot, Sta-ST, for OxiCal®-ST calibration and storage vessel for StirrOx® G oxygen sensor, Pour: Dissolved oxygen probe, StirrOx® G, Sonde à oxygène dissous
Fournisseur:  JOUR RESEARCH (VICI)
Description:   Precolumn filter kit has a standard 10 to 32 fitting and fits direct to most column types without introducing an additional dead volume.
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

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:  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:  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-7855R-A350)

Fournisseur:  Bioss
Description:   Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   FIBCD1 is a 461 amino acid single-pass membrane protein that contains one fibrinogen C-terminal domain and exists as multiple alternatively spliced isoforms. The gene encoding FIBCD1 maps to human chromosome 9, which contains 145 million base pairs, comprises 4% of the human genome and encodes nearly 900 genes.
UOM:  1 * 100 µl
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