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Single-use+Pressure+Sensor
Numéro de catalogue:
(BOSSBS-12096R-CY5)
Fournisseur:
Bioss
Description:
Peroxisomes are single-membrane bound organelles present in virtually all eukaryotic cells. They are involved in numerous catabolic and anabolic pathways, including beta-oxidation of very long chain fatty acids, metabolism of hydrogen peroxide, plasmalogen biosynthesis and bile acid synthesis. The Peroxin gene family, which includes more than 20 members, is required for peroxisome biogenesis. Peroxin 5R, also known as PEX5-related protein or Peroxisome biogenesis factor 5-like, is a 626 amino acid protein that is mainly expressed in brain, with some expression in testis and pancreas. Peroxin 5R contains five TPR repeats, which enable protein-protein interactions and assembly of large multiprotein complexes. There are three isoforms of Peroxin 5R that are produced as a result of alternative splicing events. These isoforms bind C-terminal peroxisome-targeting signals in a similar manner to Peroxin-5. Peroxin 5R interacts with Rab 8b, possibly playing a role in vesicular trafficking and neurotransmitter release.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11073R-CY3)
Fournisseur:
Bioss
Description:
The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumor suppressor.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12439R-A680)
Fournisseur:
Bioss
Description:
LRRFIP1 is an 738 amino acid human protein whose rodent counterpart is known as Lrrfip1 (also designated FLAP in mouse). LRRFIP1 is also believed to control smooth muscle cell proliferation following arterial injury through PDGF-A repression. The N-terminus of LRRFIP1 shows high homology to the coiled-coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I, and the interaction of LRRFIP1 with the LRR of Flightless I has been confirmed. LRRFIP1 does not bind single-stranded DNA or RNA significantly and binds double-stranded DNA weakly. In contrast, LRRFIP1 binds double-stranded RNA with high affinity, and two molecules of LRRFIP1 bind the TaR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. Flightless I has a C-terminal TaR-like domain which binds Actin and therefore the association of LRRFIP1 with the LRR of Flightless I may provide a link between the Actin cytoskeleton and RNA in mammalian cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12439R-A750)
Fournisseur:
Bioss
Description:
LRRFIP1 is an 738 amino acid human protein whose rodent counterpart is known as Lrrfip1 (also designated FLAP in mouse). LRRFIP1 is also believed to control smooth muscle cell proliferation following arterial injury through PDGF-A repression. The N-terminus of LRRFIP1 shows high homology to the coiled-coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I, and the interaction of LRRFIP1 with the LRR of Flightless I has been confirmed. LRRFIP1 does not bind single-stranded DNA or RNA significantly and binds double-stranded DNA weakly. In contrast, LRRFIP1 binds double-stranded RNA with high affinity, and two molecules of LRRFIP1 bind the TaR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. Flightless I has a C-terminal TaR-like domain which binds Actin and therefore the association of LRRFIP1 with the LRR of Flightless I may provide a link between the Actin cytoskeleton and RNA in mammalian cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12323R-A680)
Fournisseur:
Bioss
Description:
Cell adhesion molecule-related/down-regulated by oncogenes (CDO) and BOC (brother of CDO) are members of the immunoglobulin/fibronectin type III repeat family and act as cell surface receptors. CDO is a component of a cell-surface receptor complex which also contains BOC, NEO1, CTNNB1 and cadherins and which acts as a mediator of cell-cell interactions between muscle cells. CDO and BOC are single pass membrane proteins that play a role in myogenic cell differentiation. Together, CDO and BOC participate in a positive feedback loop with MyoD, a myogenic transcription factor. The 1,242 amino acid rat CDO protein has a 24 residue signal sequence, five Ig V-like repeats, a 25 residue membrane-spanning region, three FNIII-like repeats and a cytoplasmic region of 256 amino acids containing a proline-rich stretch. The human protein contains 1225 amino acid residues and shares significant homology with the domain structures of the rat protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12323R-A750)
Fournisseur:
Bioss
Description:
Cell adhesion molecule-related/down-regulated by oncogenes (CDO) and BOC (brother of CDO) are members of the immunoglobulin/fibronectin type III repeat family and act as cell surface receptors. CDO is a component of a cell-surface receptor complex which also contains BOC, NEO1, CTNNB1 and cadherins and which acts as a mediator of cell-cell interactions between muscle cells. CDO and BOC are single pass membrane proteins that play a role in myogenic cell differentiation. Together, CDO and BOC participate in a positive feedback loop with MyoD, a myogenic transcription factor. The 1,242 amino acid rat CDO protein has a 24 residue signal sequence, five Ig V-like repeats, a 25 residue membrane-spanning region, three FNIII-like repeats and a cytoplasmic region of 256 amino acids containing a proline-rich stretch. The human protein contains 1225 amino acid residues and shares significant homology with the domain structures of the rat protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11956R)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK3 (SLIT and NTRK-like family, member 3) is a 977 amino acid single-pass type I membrane protein that contains 20 LRR repeats and belongs to the SLITRK family. Expressed at highest levels in cerebral cortex, SLITRK3 is also found in adult and fetal neural tissues and some astrocytic brain tumors. SLITRK3 functions to suppress neurite outgrowth and plays a role in the regulation of neuronal function. SLITRK3 is encoded by a gene that maps to human chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11956R-A647)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK3 (SLIT and NTRK-like family, member 3) is a 977 amino acid single-pass type I membrane protein that contains 20 LRR repeats and belongs to the SLITRK family. Expressed at highest levels in cerebral cortex, SLITRK3 is also found in adult and fetal neural tissues and some astrocytic brain tumors. SLITRK3 functions to suppress neurite outgrowth and plays a role in the regulation of neuronal function. SLITRK3 is encoded by a gene that maps to human chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOHLV1830-07)
Fournisseur:
Bohlender
Description:
Cadre en aluminium avec système de chambre à 2 vitres (à l’intérieur verre, à l’extérieur verre acrylique), quatre étagères en polycarbonate inclus, peut être équipé avec jusqu’à 26 étagères. Chauffage intégré (850 W) avec capteur de température et ventilateur. Un branchement électrique (230 V/ 50 Hz) est nécessaire.
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-11073R)
Fournisseur:
Bioss
Description:
The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumor suppressor.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11224R-FITC)
Fournisseur:
Bioss
Description:
DNA damage or incomplete replication of DNA results in the inhibition of cell cycle progression at the G1 to S or the G2 to M phase transition by conserved regulatory mechanisms known as cell cycle checkpoints. Checkpoint proteins include Rad17, which is involved in regulating cell cycle progression at the G1 checkpoint as well as Chk1, Chk2, Rad1, Rad9 and Hus1, which are involved in regulating cell cycle arrest at the G2 checkpoint. In response to DNA damage, ATM and ATR kinases are important for cell cycle checkpoint response signalling. ATR-interacting protein (ATRIP), also designated ATM and Rad3-related-interacting protein, is required for checkpoint signaling after DNA damage. It is also important for ATR expression, which regulates DNA replication and damage checkpoint responses. ATRIP is a ubiquitously expressed protein that can form heterodimers with ATR. After dimerization they bind the RPA complex and are recruited to single stranded DNA. ATRIP is a nuclear protein that may also play a role in protein stabilization.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9301R-CY3)
Fournisseur:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9301R-CY5.5)
Fournisseur:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9301R-CY5)
Fournisseur:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12323R-CY5)
Fournisseur:
Bioss
Description:
Cell adhesion molecule-related/down-regulated by oncogenes (CDO) and BOC (brother of CDO) are members of the immunoglobulin/fibronectin type III repeat family and act as cell surface receptors. CDO is a component of a cell-surface receptor complex which also contains BOC, NEO1, CTNNB1 and cadherins and which acts as a mediator of cell-cell interactions between muscle cells. CDO and BOC are single pass membrane proteins that play a role in myogenic cell differentiation. Together, CDO and BOC participate in a positive feedback loop with MyoD, a myogenic transcription factor. The 1,242 amino acid rat CDO protein has a 24 residue signal sequence, five Ig V-like repeats, a 25 residue membrane-spanning region, three FNIII-like repeats and a cytoplasmic region of 256 amino acids containing a proline-rich stretch. The human protein contains 1,225 amino acid residues and shares significant homology with the domain structures of the rat protein.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12323R-HRP)
Fournisseur:
Bioss
Description:
Cell adhesion molecule-related/down-regulated by oncogenes (CDO) and BOC (brother of CDO) are members of the immunoglobulin/fibronectin type III repeat family and act as cell surface receptors. CDO is a component of a cell-surface receptor complex which also contains BOC, NEO1, CTNNB1 and cadherins and which acts as a mediator of cell-cell interactions between muscle cells. CDO and BOC are single pass membrane proteins that play a role in myogenic cell differentiation. Together, CDO and BOC participate in a positive feedback loop with MyoD, a myogenic transcription factor. The 1,242 amino acid rat CDO protein has a 24 residue signal sequence, five Ig V-like repeats, a 25 residue membrane-spanning region, three FNIII-like repeats and a cytoplasmic region of 256 amino acids containing a proline-rich stretch. The human protein contains 1,225 amino acid residues and shares significant homology with the domain structures of the rat protein.
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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