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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-7116R-CY5)
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-9440R-A680)
Fournisseur:
Bioss
Description:
MTA1 is a component of the NURD (nucleosome remodeling and histone deacetylation) complex, which is associated with ATP-dependent chromatin-remodeling and histone deacetylase activity. MTA1 functions in conjunction with other components of NURD to mediate transcriptional repression as it facilitates the association of repressor molecules with the chromatin. Structurally, MTA1 contains a single SH3-binding motif and a zinc finger domain, along with a region similar to the co-repressor protein N-Cor. MTA1 is normally expressed at low levels in various tissues and is more highly expressed in testis. Overexpression of MTA1 correlates with tumour invasion and metastasis in various carcinomas including colorectal, gastrointestinal and breast carcinomas. Elevation of MTA1 levels in these tumours appears to enhance the metastases to lymph nodes, increase mammary cell motility and potentiate growth, and therefore may be an indicator for assessing the potential malignancies of various tumours. A similar protein, MTA2, also designated MTA1-L1 (MTA1-like protein 1), shares more than 55% sequence homology with MTA1 and is ubiquitously expressed.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-10493R-A647)
Fournisseur:
Bioss
Description:
Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.[provided by RefSeq, Sep 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11224R-HRP)
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-9152R-A350)
Fournisseur:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12439R-CY3)
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-A555)
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-CY5)
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-11073R-A647)
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-9301R-A680)
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 localised 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-A750)
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 localised 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-11948R-A350)
Fournisseur:
Bioss
Description:
Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11948R-CY5)
Fournisseur:
Bioss
Description:
Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch signaling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumorigenic in SCID mice.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11073R-A488)
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-9301R-A488)
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-11948R-A750)
Fournisseur:
Bioss
Description:
Three mammalian fringe family members, Manic, Radical and Lunatic Fringe, have been identified as proteins related to Drosophila Fringe, a protein involved in development. Fringe proteins act upstream of the Notch Signalling pathway and are involved in boundary determination during segmentation. Each mammalian Fringe displays different patterns of expression, though all are expressed in the mouse embryo as well as in many adult tissues. Radical Fringe, also known as Beta-1,3-N-acetylglucosaminyltransferase Radical Fringe, is a 331 amino acid single-pass type II membrane protein that localizes to the membrane of the Golgi apparatus. Playing a key role in the development of the limb bud, Radical Fringe transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Lunatic Fringe is required for normal somite segmentation and patterning and is thought to be a target of the molecular clock. Manic Fringe, also involved in somatic development, has been shown to render mouse NIH/3T3 cells tumourigenic in SCID mice.
UOM:
1 * 100 µl
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