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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-7100R)
Fournisseur:
Bioss
Description:
RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11081R-A350)
Fournisseur:
Bioss
Description:
The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including ∫-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT3 (FAT tumor suppressor homolog 3, also known as CDHF15 or CDHR10, is a 4,589 amino acid single-pass type I membrane protein expressed in ES cells, primitive neuroectoderm, fetal brain, infant brain, adult neural tissues and prostate. Containing thirty-three cadherin domains, four EGF-like domains and one laminin G-like domain, FAT3 may participate in the interactions between neurites derived from specific subsets of neurons during development.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12323R-A350)
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:
(BTIUBNUM0994-50)
Fournisseur:
Biotium
Description:
This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production.
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production.
Fournisseur:
Biotium
Description:
This antibody neutralises HurTNFamediated cytotoxicity of L929 cells and inhibits tumour growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production.
Numéro de catalogue:
(BOSSBS-4182R-A350)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5693R-A350)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4182R-A750)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilises single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BRAU8713175)
Fournisseur:
B. Braun
Description:
Syringe Pump, Drop Sensor for Infusomat® Space (optional)
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-11878R-A680)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic / 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. The LRRTM protein family plays a role in the regulation of various cellular events during nervous system development. Localizing predominantly to the nervous system, LRRTM family members are known to exhibit synaptogenic activity. LRRTM4 (leucine-rich repeat transmembrane neuronal protein 4) is a 590 amino acid member of the LRRTM protein family. Expressed in neuronal tissues, LRRTM4 may play a role in the development and maintenance of the vertebrate nervous system. A single-pass type I membrane protein, LRRTM4 contains 10 LRR repeats. LRRTM4 is expressed as two isoforms produced by alternative splicing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8263R-A750)
Fournisseur:
Bioss
Description:
DHRSX (dehydrogenase/reductase SDR family member on chromosome X) is a 330 amino acid protein belonging to the short-chain dehydrogenases/reductases (SDR) family. Widely expressed, DHRSX is an oxidoreductase that contains a coenzyme binding site and a substrate binding site, indicating a possible role in cellular metabolism. The gene that encodes DHRSX is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes. The X and Y chromosomes are the human sex chromosomes. Chromosome X consists of about 153 million base pairs and nearly 1,000 genes. The combination of a X and Y chromosome lead to normal male development while two copies of X lead to normal female development. There are a number of conditions related to an unusual number and combination of sex chromosomes being inherited, including Turner's syndrome, Klinefelter's syndrome and Triple X syndrome. Color blindness, hemophilia, and Duchenne muscular dystrophy are well known X chromosome-linked conditions which affect males more frequently as males carry a single X chromosome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12533R-A555)
Fournisseur:
Bioss
Description:
Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3047R-A555)
Fournisseur:
Bioss
Description:
This gene encodes a receptor tyrosine kinase, which belongs to the insulin receptor superfamily. This protein comprises an extracellular domain, an hydrophobic stretch corresponding to a single pass transmembrane region, and an intracellular kinase domain. It plays an important role in the development of the brain and exerts its effects on specific neurons in the nervous system. This gene has been found to be rearranged, mutated, or amplified in a series of tumours including anaplastic large cell lymphomas, neuroblastoma, and non-small cell lung cancer. The chromosomal rearrangements are the most common genetic alterations in this gene, which result in creation of multiple fusion genes in tumourigenesis, including ALK (chromosome 2)/EML4 (chromosome 2), ALK/RANBP2 (chromosome 2), ALK/ATIC (chromosome 2), ALK/TFG (chromosome 3), ALK/NPM1 (chromosome 5), ALK/SQSTM1 (chromosome 5), LK/KIF5B (chromosome 10), ALK/CLTC (chromosome 17), ALK/TPM4 (chromosome 19), and ALK/MSN (chromosome X).[provided by RefSeq, Jan 2011].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11797R-A750)
Fournisseur:
Bioss
Description:
Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyses the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterised by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11898R-A750)
Fournisseur:
Bioss
Description:
NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM:
1 * 100 µl
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