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Single-use+Pressure+Sensor
Numéro de catalogue:
(BOSSBS-13176R-A647)
Fournisseur:
Bioss
Description:
The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13176R-A750)
Fournisseur:
Bioss
Description:
The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11?s peptidyl-prolyl isomerase activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11951R-A750)
Fournisseur:
Bioss
Description:
The Per-Arnt-Sim (PAS) domain was identified as a 270 amino acid motif that mediates associations between various PAS family transcription factors. Several PAS domain family members have been identified including AhR, Arnt 1, and single-minded proteins (SIM1 and SIM2). The aromatic (aryl) hydrocarbon receptor, AhR, is a ligand dependent transcription factor that interacts with specific DNA sequences termed xenobiotic responsive elements (XREs) to activate several genes including CYP1A1, glutathione S-transferase Ya subunit and DT-diaphorase. The Ah receptor nuclear translocator protein 1 (Arnt 1) is required for ligand- dependent nuclear translocation of the Ah receptor and is also necessary for Ah receptor binding to the XRE element. Both SIM1 and SIM2 inhibit AhR/Arnt dimerization, thus inhibiting transcriptional activation. The SIM genes are thought to be involved in the directing and regionalization of tissues during development and the SIM2 gene, which is located on chromosome 21, is a candidate for the gene responsible for Down syndrome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12439R-A488)
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-10493R-A350)
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-A555)
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-11081R-A488)
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-7116R-CY7)
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-11698R-CY7)
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-9152R-CY5.5)
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-9152R-A488)
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-CY7)
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-13752R-A488)
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-13752R-HRP)
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-12305R-A555)
Fournisseur:
Bioss
Description:
In eukaryotic cells, the Golgi apparatus receives newly synthesized proteins from the endoplasmic reticulum (ER) and, after covalent modification, delivers them to their destination in the cell. For membrane-directed proteins this process is believed to be carried out via vesicular transport. Correct vesicular transport is determined by specific pairing of vesicle-associated SNAREs (v-SNAREs) with those on the target membrane (t-SNAREs). Unconventional SNARE in the ER 1, also known as USE1 or protein p31, is a 259 amino acid t-SNARE that forms a larger complex with ZW10, RINT-1 and Syntaxin 18. Upon Mg2+-AP treatment in the presence of NSF and ?SNAP, ZW10, RINT-1 and USE1 dissociate from Syntaxin 18. USE1 is a single-pass type IV membrane protein that is localized to the endoplasmic reticulum membrane. Three named isoforms exist for USE1 as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11227R-A647)
Fournisseur:
Bioss
Description:
Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.
UOM:
1 * 100 µl
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