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4,4\'-Dibrombiphenyl (PBB Nr. 15)
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4,4\'-Dibrombiphenyl (PBB Nr. 15)
Artikel-Nr:
(BOSSBS-12193R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12193R-A555
Lokale Artikelnummer::
BOSSBS-12193R-A555
Beschreibung:
Transcription factor required for formation of positional identity in the developing retina, regionalization of the optic chiasm and morphogenesis of the kidney. Can neuralize ectodermal cells directly By similarity. Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. Probable transcription factor involved in embryogenesis and somatogenesis. FOXD1 is involved in regulating inflammation as well as kidney and retinal development. FOXD1 regulates the activity of NFAT and NFkB. Deficiency of FOXD1 results in multiorgan systemic inflammation, exaggerated Th cell-derived cytokine production, and T cell proliferation in autogolgous MLRs. In kidneys, FOXD1 controls the production of signals required for the normal transition of induced mesenchyme into tubular epithelium and full growth and branching of the collecting system. Deletion of FOXD1 results in renal abnormalities. FOXD2 acts as a modulator of T cell activation.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-3272R-A488)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3272R-A488
Lokale Artikelnummer::
BOSSBS-3272R-A488
Beschreibung:
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-3272R-A350)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3272R-A350
Lokale Artikelnummer::
BOSSBS-3272R-A350
Beschreibung:
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-8300R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-8300R-A647
Lokale Artikelnummer::
BOSSBS-8300R-A647
Beschreibung:
Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5966R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5966R-A647
Lokale Artikelnummer::
BOSSBS-5966R-A647
Beschreibung:
The LIM-only (LMO) proteins, LMO1 and LMO2, are nuclear factors that are characterized by a conserved LIM domain (1). The LIM domain consists of a cysteine-rich zinc-binding motif that is present in a variety of transcription factors, including the LIM homeobox (LHX) proteins expressed in the central nervous system and involved in cell differentiation (2). LMO1 and LMO2 are expressed in the adult CNS in a cell type-specific manner, where they are differentially regulated by neuronal activity and are involved in regulating the cellular differentiated phenotype of neurons (3). LMO2 lacks a specific DNA-binding homeobox domain but rather assembles into transcriptional regulatory complexes to mediate gene expression by interacting with the widely expressed nuclear LIM interactor (NLI) (4). NLI, known also as CLIM-1, and the related protein CLIM-2 facilitate the formation of heteromeric LIM complexes and also enhance the nuclear retention of LIM proteins (5). LMO2 and the related protein LMO4 are expressed in thymic precursor cells (6). LMO4 is also expressed in mature T cells, cranial neural crest cells, somite, dorsal limb bud mesenchyme, motor neurons, and Schwann cell progenitors (7).
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-0886R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-0886R-CY3
Lokale Artikelnummer::
BOSSBS-0886R-CY3
Beschreibung:
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12860R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12860R-CY5
Lokale Artikelnummer::
BOSSBS-12860R-CY5
Beschreibung:
Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12860R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12860R-FITC
Lokale Artikelnummer::
BOSSBS-12860R-FITC
Beschreibung:
Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-2777R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-2777R-HRP
Lokale Artikelnummer::
BOSSBS-2777R-HRP
Beschreibung:
Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV42H1 and SUV42H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-2' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV4 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13686R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13686R-FITC
Lokale Artikelnummer::
BOSSBS-13686R-FITC
Beschreibung:
MOZ (monocytic leukemia zinc finger protein) is a chromatin-associated histone acetyltransferase (HAT) that regulates chromatin remodeling and transcription. The MOZ gene was initially isolated as a consequence of two variant translocations that were identified in a distinct subtype of acute myeloid leukemias and resulted in the formation of MOZ fusion proteins. These fusions involve the HAT domain of MOZ with the activation domain of either transcriptional coactivator protein TIF2/GRIP1 or CBP, and lead to enhanced transcriptional activation by a mechanism involving aberrant histone acetylation. Additional MOZ related proteins, including MORF (MOZ related factor) and TIP60 (TAT interacting proteins 60), share significant similarities with MOZ including the putuative HAT domain. MORF also contains a strong transcriptional repression domain at its N terminus and a highly potent activation domain at the C terminus, suggesting that MORF has both HAT activity and contributes to the regulation of transcriptional activation. TIP60 was originally identified as a coactivator for the HIV TAT protein and also functions as a nuclear hormone receptor coactivator that enhances ligand dependent steroid receptor-mediated transactivation involving the androgen, estrogen and progesterone receptors.
VE:
1 * 100 µl
Lieferant:
Tonbo Biosciences
Beschreibung:
The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL-2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells. The PC61.5 antibody is used as a marker for T cells, B cells and dendritic cell subsets. Expression of CD25, CD4 and the transcription factor Foxp3 is regarded as a phenotypic signature for Treg cells. As such, this antibody is widely used to distinguish Treg cells from native or conventional T cells which are CD25-. This clone has also been reported for depletion of Treg cells in vivo (use format suitable for functional assays).
Artikel-Nr:
(BOSSBS-12860R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12860R-HRP
Lokale Artikelnummer::
BOSSBS-12860R-HRP
Beschreibung:
Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11104R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11104R-A680
Lokale Artikelnummer::
BOSSBS-11104R-A680
Beschreibung:
Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12860R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12860R-A555
Lokale Artikelnummer::
BOSSBS-12860R-A555
Beschreibung:
Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12330R-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12330R-CY7
Lokale Artikelnummer::
BOSSBS-12330R-CY7
Beschreibung:
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. Staf-50 (50 kDa-stimulated trans-acting factor), also known as TRIM22 (tripartite motif-containing 22), RNF94 or GPSTAF50, is a 498 amino acid cytoplasmic protein that belongs to the TRIM family and, characteristic of TRIM family members, contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Induced by IFN-å and IFN-∫, Staf-50 is strongly expressed in ovary, spleen, thymus and peripheral blood leukocytes where it is thought to mediate the antiviral effects of IFN proteins. Additionally, Staf-50 is present in leukemic cells, suggesting a role in cancer formation and metastasis. Staf-50 exists as two alternatively spliced isoforms which are encoded by a gene that maps to human chromosome 11.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12311R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12311R-CY5
Lokale Artikelnummer::
BOSSBS-12311R-CY5
Beschreibung:
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. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.
VE:
1 * 100 µl
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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