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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-13752R-A555)
Fournisseur:
Bioss
Description:
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11420R-CY3)
Fournisseur:
Bioss
Description:
Neuromedin U is a neuropeptide with high activity on smooth muscle. It is widely expressed in gastrointestinal systems and central nervous system (CNS). Peripheral activities of neuromedin U include smooth muscle stimulation, ion transport alterations in the gut and the regulation of local blood flow and adrenocortical function. Neuromedin U receptors 1 and 2 (NMUR1 and NMUR2) are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family of proteins. Both NMUR1 and NMUR2 act as receptors for the neuromedin U neuropeptide. NMUR1 is detected in peripheral organs, particularly in urogenital and gastrointestinal systems, with highest levels in testis. It’s expression in CNS is low, but the protein has been detected in cerebellum, hippocampus, dorsal root ganglia and spinal cord. NMUR2 is predominantly detected in central nervous system with highest levels detected in medulla oblongata, spinal cord and thalamus. It may also be detected in testis but has low levels of expression in peripheral tissues.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11420R-PE)
Fournisseur:
Bioss
Description:
Neuromedin U is a neuropeptide with high activity on smooth muscle. It is widely expressed in gastrointestinal systems and central nervous system (CNS). Peripheral activities of neuromedin U include smooth muscle stimulation, ion transport alterations in the gut and the regulation of local blood flow and adrenocortical function. Neuromedin U receptors 1 and 2 (NMUR1 and NMUR2) are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family of proteins. Both NMUR1 and NMUR2 act as receptors for the neuromedin U neuropeptide. NMUR1 is detected in peripheral organs, particularly in urogenital and gastrointestinal systems, with highest levels in testis. It’s expression in CNS is low, but the protein has been detected in cerebellum, hippocampus, dorsal root ganglia and spinal cord. NMUR2 is predominantly detected in central nervous system with highest levels detected in medulla oblongata, spinal cord and thalamus. It may also be detected in testis but has low levels of expression in peripheral tissues.
UOM:
1 * 100 µl
Fournisseur:
ENTEGRIS INC
Description:
Ces filtres sont conçus pour éliminer de manière constante les particules d'une large gamme d'acides, de bases et d'autres matériaux de traitement. Parfaits pour les applications de débit moyen à élevé, ils représentent un faible coût de possession, comme un dispositif ou un produit pré-humidifié prêt pour une installation rapide. Les cartouches pré-humidifiées éliminent les interactions entre alcool et produits chimiques ainsi que les sources de contamination potentielles et minimisent les temps d'arrêt du processus.
Numéro de catalogue:
(BOSSBS-3027R-A555)
Fournisseur:
Bioss
Description:
Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-20237R-A680)
Fournisseur:
Bioss
Description:
Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11277R-CY3)
Fournisseur:
Bioss
Description:
DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11277R-CY5)
Fournisseur:
Bioss
Description:
DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM:
1 * 100 µl
Numéro de catalogue:
(516-7030)
Fournisseur:
Sartorius
Description:
Le système Combisart® permet de sélectionner le matériel et les consommables répondant le mieux aux besoins en matière d'assurance qualité. Il présente une conception modulaire et des accessoires standard éprouvés sur le terrain, pour faciliter le choix.
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-7116R-A555)
Fournisseur:
Bioss
Description:
Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7116R-A647)
Fournisseur:
Bioss
Description:
Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11073R-HRP)
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-11698R-A647)
Fournisseur:
Bioss
Description:
Huntingtin yeast partner E is a 458 amino acid single-pass membrane protein. HYPE is thought to interact with Huntingtin, a protein which induces neurodegeneration when mutated. HYPE also contains two tetratricopeptide repeats (TPR), which may be involved in protein-protein interaction. The gene that encodes HYPE is located on chromosome 12, which encodes over 1,100 genes within 132 million bases and makes up about 4.5% of the human genome. A number of skeletal deformities are linked to chromosome 12 including hypochondrogenesis, achondrogenesis and Kniest dysplasia. Chromosome 12 is also home to a homeobox gene cluster which encodes crucial transcription factors for morphogenesis, and the natural killer complex gene cluster encoding C-type lectin proteins which mediate the NK cell response to MHC I interaction. Trisomy 12p leads to facial development defects, seizure disorders and a host of other symptoms varying in severity depending on the extent of mosaicism and is most severe in cases of complete trisomy.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9492R)
Fournisseur:
Bioss
Description:
C9orf4 is a 344 amino acid single-pass membrane protein that is primarily expressed in adult and fetal brain and is weakly expressed in spinal cord, adult ovary and medulla. C9orf4 contains one DOMON domain, a predominantly β-sheet domain that is thought to aide in extracellular adhesion. The gene encoding C9orf4 maps to human chromosome 9, which consists of about 145 million bases and 4% of the human genome and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype. Hereditary hemorrhagic telangiectasia, which is characterized by harmful vascular defects, is associated with the chromosome 9 gene encoding endoglin protein, ENG. Familial dysautonomia is also associated with chromosome 9 though through the gene IKBKAP. Notably, chromosome 9 encompasses the largest interferon family gene cluster. Chromosome 9 is partnered with chromosome 22 in the translocation leading to the aberrant production of BCR-ABL fusion protein often found in leukemias.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9238R-CY7)
Fournisseur:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9238R-A555)
Fournisseur:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
UOM:
1 * 100 µl
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