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Masterflex+Single-use+Flow+Sensor
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-4917R-A680)
Fournisseur:
Bioss
Description:
Osteocalcin belongs to the osteocalcin/matrix Gla protein family and constitutes 1 to 2% of the total bone protein. It is a 49 amino acid single chain vitamin K dependent protein, made by osteoblasts, and is a major component of the noncollagenous bone matrix. Post translational modification by a vitamin K dependent carboxylase produces three gamma carboxyglutamic acid residues at positions 17, 21 and 24, giving it a high affinity for calcium. It also binds strongly to apatite.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4917R-A647)
Fournisseur:
Bioss
Description:
Osteocalcin belongs to the osteocalcin/matrix Gla protein family and constitutes 1 to 2% of the total bone protein. It is a 49 amino acid single chain vitamin K dependent protein, made by osteoblasts, and is a major component of the noncollagenous bone matrix. Post translational modification by a vitamin K dependent carboxylase produces three gamma carboxyglutamic acid residues at positions 17, 21 and 24, giving it a high affinity for calcium. It also binds strongly to apatite.
UOM:
1 * 100 µl
Numéro de catalogue:
(KNFA155872)
Fournisseur:
KNF
Description:
Drum pump accessory, Foot switch for version RC (RC= flow rate can be set both manually and via an external control device)
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-1677R-CY5.5)
Fournisseur:
Bioss
Description:
Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13352R-CY7)
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-11477R-HRP)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins that are conserved from insects to humans. Members of this family of proteins are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin†domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. Secreted and cell-bound semaphorins chemically attract and repel the growth of neural axons, guiding the development of intricate networks of neural tissue. SEMA4B (semaphorin-4B), also known as SemC or SEMAC, is an 832 amino acid single-pass type I membrane protein that belongs to the semaphorin family and exists as two alternatively spliced isoforms. Containing one Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a single sema domain, SEMA4B is encoded by a gene located on human chromosome 15.
UOM:
1 * 100 µl
Numéro de catalogue:
(90097.)
Fournisseur:
Biotium
Description:
6-TAMRA SE (full name: 6-Carboxytetramethylrhodamine succinimidyl ester) is the amine-reactive form of Amine-reactive form of Carboxytetramethylrhodamine (TAMRA) single isomer. Supplied at 90 mg/mL (0.17 M) in anhydrous DMSO. The solution is suitable for labeling oligonucleotides.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11719R-A647)
Fournisseur:
Bioss
Description:
Calcyon is a single transmembrane protein that interacts with D1 dopamine receptors. Dopamine is a neurotransmitter that regulates synaptic transmission involved in learning and memory. D1 receptors, the most abundant dopamine receptor in the central nervous system, appear to modulate the activity of D2 dopamine receptors, mediate various behavioural responses, and regulate neuron growth and differentiation. Calcyon is present in neuronal cell bodies and processes of the cortex and hippocampus, and it is especially abundant in pyramidal neurons. Interaction of Calcyon with D1 receptors results in a release of intracellular calcium.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13352R-A555)
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
Fournisseur:
Thermo Fisher Scientific
Description:
Fabriqués en polypropylène (PP).
Numéro de catalogue:
(BOSSBS-5453R-CY3)
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:
VWR Collection
Description:
Sonde à oxygène dissous, VWR®, Câble de 4 m
Numéro de catalogue:
(BOSSBS-5150R-CY3)
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-CY7)
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
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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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