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Solid+Phase+Extraction
Numéro de catalogue:
(ENZOADIKAMSA100E)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Researchers cloned DJ-1 protein, consisting of 189 amino acids, from a HeLa cell cDNA library as a oncogene which weakly transformed NIH3T3 cells. Cotransfection with ras or c-myc enhances transformation by DJ-11. DJ-1 expression is induced by growth signals, and it is translocated from the cytoplasm to the nucleus during the S phase without the presence of any nuclear localization signals. In addition to its potential involvement in ras-mediated signal transduction pathways, DJ-1 is known to regulate transcription of androgen-responsive genes, and is sensitive to oxidative stress. DJ-1 is ubiquitously expressed in various human tissues including the brain, with high expression in astrocytes of the frontal cortex and substantia nigra. Homozygous mutations in the DJ-1 gene have been shown to cause early-onset autosomal recessive Parkinson’s disease.
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(BOSSBS-13160R-A680)
Fournisseur:
Bioss
Description:
Fibulin-1 and Fibulin-2 associate with Fibronectin and other extracellular matrix proteins. In bone marrow, Fibulin-1 and Fibulin-2 bind to Fibronectin in the adherent layer. Fibulin-1 expression is stimulated by estrogen in ovarian cancer cell lines and has been suggested as both an agent of metastasis in ovarian cancer cells and as an indicator for predicting cancer risk or aggressiveness in ovarian carcinomas. The mobility of cancer cells may be inhibited with increasing exposure to Fibulin-1. Fibulin-2 binds to the lectin domains of extracellular matrix proteins aggrecan, versican and brevican. Fibulin-2 is abundantly expressed in heart, placenta and ovarian tissue, where it localizes to basement membranes and connective tissue compartments. In mice, differential Fibulin-2 gene expression correlates with the early phase of diabetic kidneys and glomerulosclerosis. The gene encoding human Fibulin-2 maps to chromosome 3p25.1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0829R-A750)
Fournisseur:
Bioss
Description:
Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13160R-CY7)
Fournisseur:
Bioss
Description:
Fibulin-1 and Fibulin-2 associate with Fibronectin and other extracellular matrix proteins. In bone marrow, Fibulin-1 and Fibulin-2 bind to Fibronectin in the adherent layer. Fibulin-1 expression is stimulated by estrogen in ovarian cancer cell lines and has been suggested as both an agent of metastasis in ovarian cancer cells and as an indicator for predicting cancer risk or aggressiveness in ovarian carcinomas. The mobility of cancer cells may be inhibited with increasing exposure to Fibulin-1. Fibulin-2 binds to the lectin domains of extracellular matrix proteins aggrecan, versican and brevican. Fibulin-2 is abundantly expressed in heart, placenta and ovarian tissue, where it localizes to basement membranes and connective tissue compartments. In mice, differential Fibulin-2 gene expression correlates with the early phase of diabetic kidneys and glomerulosclerosis. The gene encoding human Fibulin-2 maps to chromosome 3p25.1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11286R-A750)
Fournisseur:
Bioss
Description:
Lipocalin-1 is a secretory protein that is highly expressed in fluids covering epithelial surfaces such as tears and respiratory secretions. This major lipid-binding protein in tears is also called tear lipocalin (TL) and von Ebner's gland protein (VEG), as it is also a major secretion of these lingual salivary glands. In addition to lacrimal glands and lingual glands, Lipocalin-1 is secreted by nasal mucosal glands, secretory glands of the tracheobronchial tract, sweat glands, mammary glands, adrenal gland, prostate, thymus, testis and corticotrophs of the pituitary gland. Specifically, Lipocalin-1 functions to stabilize the lipid film of human tear fluid by removing harmful lipids from the human corneal surface and delivering them to the aqueous phase of tears. Lipocalin-1 may also function as a transporter of hydrophobic molecules such as bitter substances on the tongue.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11286R-FITC)
Fournisseur:
Bioss
Description:
Lipocalin-1 is a secretory protein that is highly expressed in fluids covering epithelial surfaces such as tears and respiratory secretions. This major lipid-binding protein in tears is also called tear lipocalin (TL) and von Ebner’s gland protein (VEG), as it is also a major secretion of these lingual salivary glands. In addition to lacrimal glands and lingual glands, Lipocalin-1 is secreted by nasal mucosal glands, secretory glands of the tracheobronchial tract, sweat glands, mammary glands, adrenal gland, prostate, thymus, testis and corticotrophs of the pituitary gland. Specifically, Lipocalin-1 functions to stabilize the lipid film of human tear fluid by removing harmful lipids from the human corneal surface and delivering them to the aqueous phase of tears. Lipocalin-1 may also function as a transporter of hydrophobic molecules such as bitter substances on the tongue.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2969R-CY5)
Fournisseur:
Bioss
Description:
E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription (By similarity).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2969R-A680)
Fournisseur:
Bioss
Description:
E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription (By similarity).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5981R-A647)
Fournisseur:
Bioss
Description:
p107 is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5981R-CY7)
Fournisseur:
Bioss
Description:
p107 is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0633R-CY5.5)
Fournisseur:
Bioss
Description:
Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13229R-A350)
Fournisseur:
Bioss
Description:
FUSIP1 is a member of the Serine/Arginine (SR) family of splicing factors. Members of the SR family all contain one or more RNA recognition motifs (RRM) and an SR-rich domain. SR factors are not only essential for constitutive splicing but also regulate splicing in a concentration-dependent manner by influencing the selection of alternative splice sites. Expressed in a variety of tissues with low expression in kidney, liver and heart, FUSIP1 localizes to the cytoplasm and nuclear speckles. In its dephosphorylated form (occurring during M phase of the cell cycle), FUSIP1 functions as a potent general repressor of pre-mRNA splicing and can interact with U1 SnRNP 70. In its phosphorylated form, FUSIP1 interacts with Tra-2∫ and, together, they may cooperate in the regulation of splicing. Four isoforms exist for FUSIP1. In neurons, FUSIP1 isoforms may act to either positively or negatively regulate alternative splicing.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1234R-HRP)
Fournisseur:
Bioss
Description:
Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF1 stimulation. Isoform A interacts with CDC2, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8363R-A350)
Fournisseur:
Bioss
Description:
The regulated oscillation of protein expression is an essential mechanism of cell cycle control. The SCF class of E3 ubiquitin ligases is involved in this process by targeting cell cycle regulatory proteins for degradation by the proteasome, with the F-box subunit of the SCF specifically recruiting a given substrate to the SCF core. NIPA (nuclear interaction partner of ALK) is a human F-box-containing protein that defines an SCF-type E3 ligase (SCFNIPA) controlling mitotic entry. Assembly of this SCF complex is regulated by cell-cycle-dependent phosphorylation of NIPA, which restricts substrate ubiquitination activity to interphase. Nuclear cyclin B1 is a substrate of SCFNIPA. Inactivation of NIPA by RNAi results in nuclear accumulation of cyclin B1 in interphase, activation of cyclin B1-Cdk1 kinase activity, and premature mitotic entry. Thus, SCFNIPA-based ubiquitination may regulate S-phase completion and mitotic entry in the mammalian cell cycle.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4166R)
Fournisseur:
Bioss
Description:
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4166R-FITC)
Fournisseur:
Bioss
Description:
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.
UOM:
1 * 100 µl
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