11641 Results for: "Ethyl-11-bromodecanoate"

Supplier: Huber

The Unistat range inspires with unique thermodynamic properties and a range of functions to meet the highest demands

Supplier: Bioss

This gene encodes coagulation factor XI of the blood coagulation cascade. This protein is present in plasma as a zymogen, which is a unique plasma coagulation enzyme because it exists as a homodimer consisting of two identical polypeptide chains linked by disulfide bonds. During activation of the plasma factor XI, an internal peptide bond is cleaved by factor XIIa (or XII) in each of the two chains, resulting in activated factor XIa, a serine protease composed of two heavy and two light chains held together by disulfide bonds. This activated plasma factor XI triggers the middle phase of the intrisic pathway of blood coagulation by activating factor IX. Defects in this factor lead to Rosenthal syndrome, a blood coagulation abnormality. [provided by RefSeq, Jul 2008].

Supplier: Prosci

RDH12 is an NADPH-dependent retinal reductase whose highest activity is toward 9-cis and all-trans-retinol. RDH12 also plays a role in the metabolism of short-chain aldehydes but does not exhibit steroid dehydrogenase activity. Defects in this gene are a cause of Leber congenital amaurosis type 3 (LCA3).The protein encoded by this gene is an NADPH-dependent retinal reductase whose highest activity is toward 9-cis and all-trans-retinol. The encoded enzyme also plays a role in the metabolism of short-chain aldehydes but does not exhibit steroid dehydrogenase activity. Defects in this gene are a cause of Leber congenital amaurosis type 3 (LCA3).

Supplier: Bioss

PCDHB11 is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. PCDHB11 clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections.

Supplier: Reichert Technologies

The Density4 is accurate to 4 places

Supplier: Prosci

Interleukin-33 (IL-33) is a recently identified member of the IL-1 family of cytokines whose other members include IL-1, IL-1Ra and IL-18 (1,2). Its receptor has been shown to be ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling (1,3) and IL-1R accessory protein (IL-1RAcP) (4). Receptor binding of IL-33 activates NF-B and MAP kinases and induces the expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine (2). Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties (5).

Supplier: Bioss

This gene encodes coagulation factor XI of the blood coagulation cascade. This protein is present in plasma as a zymogen, which is a unique plasma coagulation enzyme because it exists as a homodimer consisting of two identical polypeptide chains linked by disulfide bonds. During activation of the plasma factor XI, an internal peptide bond is cleaved by factor XIIa (or XII) in each of the two chains, resulting in activated factor XIa, a serine protease composed of two heavy and two light chains held together by disulfide bonds. This activated plasma factor XI triggers the middle phase of the intrisic pathway of blood coagulation by activating factor IX. Defects in this factor lead to Rosenthal syndrome, a blood coagulation abnormality. [provided by RefSeq, Jul 2008].

Supplier: Labconco

Designed for classroom use, these lightweight hoods feature an epoxy-coated aluminum frame with tempered safety glass front sash, sides, rear baffle, and top.

Supplier: ReVacc Scientific

This pseudotyped virus uses recombinant vesicular stomatitis virus (rVSV) to carry the S protein of SARS-CoV-2 (GenBank: MN908947) with multiple mutations initially identified in variant of Omicron XBB.1.5. The S has 18-aa cytoplasmic tail truncation for optimal infection.

Supplier: Greiner Bio-One

Tubes are suitable for collection, transport, and processing of capillary blood samples from infants, toddlers, children, geriatric patients, and patients in intensive care.

Supplier: Prosci

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Proteintech

ZCCHC11, also named as KIAA0191 and TUT4, is an uridylyltransferase that acts as a suppressor of microRNA (miRNA) biogenesis by specifically mediating the terminal uridylation of some miRNAs. ZCCHC11 catalyzes the 3' uridylation of precursor let-7 (pre-let-7), a miRNA precursor. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cells and is required for ES cells to maintain pluripotency. ZCCHC11 can’t bind RNA by itself, recruited to pre-let-7 miRNAs via its interaction with LIN28 and LIN28B. Also catalyzes the 3' uridylation of miR-26A, a miRNA that represses IL6 transcript, leading to abrogate IL6 transcript repression and promote cytokine expression. ZCCHC11 may also suppress Toll-like receptor-induced NF-kappa-B activity via binding to T2BP.

Supplier: Prosci

SLC22A11 is involved in the sodium-independent transport and excretion of organic anions, some of which are potentially toxic. SLC22A11 is an integral membrane protein and is found mainly in the kidney and in the placenta, where it may act to prevent potentially harmful organic anions from reaching the fetus.The protein encoded by this gene is involved in the sodium-independent transport and excretion of organic anions, some of which are potentially toxic. The encoded protein is an integral membrane protein and is found mainly in the kidney and in the placenta, where it may act to prevent potentially harmful organic anions from reaching the fetus. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: VWR International

The VWR® Advanced 3500 Orbital Shaker is designed for a wide range of applications including cell cultures that require accurate and repeatable results. The microprocessor control provides consistent uniform shaking while safely ramping the set speed.

Supplier: Restek

Contains 1 ml each of the following mixtures, SV calibration mix #1 (anilines), SV calibration mix #2 (phenols), SV calibration mix #3 (base neutrals), SV calibration mix #4 (base neutrals), SV calibration mix #5 (PAHs), SV calibration mix #7 (dichlorobenzenes) and 605 benzidines calibration mix (benzidine and 3,3'-dichlorobenzidine).

Supplier: Bioss

PCDHB11 is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. PCDHB11 clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections.

Supplier: Prosci

SPG11 Antibody: Hereditary spastic paraplegias (HSPs) are genetically and phenotypically heterogeneous disorders.  Spastic paraplegia with thinning of the corpus callosum (ARHSP-TCC) is a relatively frequent form of complicated hereditary spastic paraplegia (cHSP) in which mental retardation and muscle stiffness at onset are followed by slowly progressive paraparesis and cognitive deterioration. Mutations of the SPG11 gene encoding the spatacsin protein have been identified as a major cause of HSP-TCC. Spatacsin is a potential transmembrane protein that is phosphorylated upon DNA damage. It is expressed in all structures of the brain, with a high expression in the cerebellum. SPG11 mutations may occur more frequently in familial than sporadic forms of cHSP without TCC. Kjellin syndrome is found to be associated with mutations in not only the SPG15 gene but also SPG11 gene.  Recent studies show Parkinsonism may initiate SPG11-linked HSP TCC and that SPG11 may cause juvenile Parkinsonism.

Supplier: Prosci

SHP2 Antibody: Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Bioss

Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

Supplier: Bioss

PCDHB11 is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. PCDHB11 clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections.

Supplier: Prosci

STK11is a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in its gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms.This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.

Supplier: Prosci

Interleukin-33 (IL-33) is a recently identified member of the IL-1 family of cytokines whose other members include IL-1, IL-1Ra and IL-18 (1,2). Its receptor has been shown to be ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling (1,3) and IL-1R accessory protein (IL-1RAcP) (4). Receptor binding of IL-33 activates NF-B and MAP kinases and induces the expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine (2). Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties (5). This recombinant protein represents the cleaved and presumably activated form of IL-33, but has not been tested in any biological assays.

Supplier: Bioss

PCDHB11 is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. PCDHB11 clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3' exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections.

Supplier: LONZA PHARMA - BIOSCIENCE CA

The SF Cell Line 96-well Nucleofector® kit is one of our three kits suited for medium-throughput transfection of cell lines when working with the 4D-Nucleofector® 96-well unit.

Supplier: Prosci

SHP2 Antibody: Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.