20634 Results for: "Acetylthio-PEG3-C2-Azide&amp"

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

PIPPIN is a Y-box protein (also called cold-shock (CSD) domain-containing protein) and belongs to a family of highly conserved RNA-binding transcriptional regulators. Predominantly expressed in brain cells and localizing to the nucleus and the cytoplasm, PIPPIN contains two RNA-binding motifs, namely PIP1 and PIP2, and one CSD domain. PIPPIN functions as a nucleic acid binding regulatory factor and is believed to participate in brain maturation. More specifically, PIPPIN binds to the 3’-UTR ends of the mRNAs encoding Histone H1 and Histone H3.3. This interaction requires all of the PIPPIN domains to work in concert as one functional protein. In addition, PIPPIN can be sumoylated in a thyroid hormone (T3)-dependent manner. This suggests that PIPPIN modification in response to extracellular stimuli may modulate the regulation of protein synthesis.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Novus Biologicals

Recommended dilutions: ELISA 1:10000 to 1:50000; Western blot 1:1000 to 1:5000.

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Ansell

Apron with protective barrier to low concentration liquid chemicals, liquid and particulate biological hazards.

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

FOXC2 is a member of forkhead/winged helix transcription factor family, whose members serve as key regulators in embryogenesis and cell differentiation (3). FOXC2 functions as a key regulator of adipocyte metabolism by increasing the sensitivity of the beta-adrenergic-cAMP-protein kinase A (PKA) signaling pathway through alteration of adipocyte PKA holoenzyme composition (4). Increased FOXC2 levels, induced by high fat diet, seem to counteract most of the symptoms associated with obesity (4). FOXC2 expression is also associated with the early stage of chondrogenic differentiation both in vivo and in vitro (3). FOXC2 haploinsufficiency results in Lymphedema-distichiasis (LD), an autosomal dominant disorder that classically presents as lymphedema of the limbs, and double rows of eyelashes (distichiasis) (5). Mutant mice null for FOXC2 show defects in axial and cranial skeletogenesis, suggesting a requirement of FOXC2 for skeletal tissue development (3). FOXC2 interacts with FOXC1 in the Notch signaling pathway (1) and in kidney and heart development (2).

Supplier: Bioss

The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: Bioss

Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).

Supplier: ProSci Inc.

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene can act as a tetramer and is involved in the assembly of 40S hnRNP particles. Multiple transcript variants encoding at least two different isoforms have been described for this gene. [provided by RefSeq].

Supplier: Abcam

Rabbit monoclonal [EPR26978-39] to HMGCS2.

Supplier: Abcam

Rabbit monoclonal [EPR24992-18] to Calcineurin B/PPP3R1.