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Solid+Phase+Extraction
Numéro de catalogue:
(BOSSBS-11267R-A350)
Fournisseur:
Bioss
Description:
CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2993R-A647)
Fournisseur:
Bioss
Description:
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0534R-CY5)
Fournisseur:
Bioss
Description:
P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11267R-A680)
Fournisseur:
Bioss
Description:
CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesised polypeptides adopt the correct conformation. Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesised eukaryotic proteins. CCT2 is the _-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly. CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase. Each CCT subunit is thought to perform a specific function during protein folding and assembly; CCT2 exhibits both actin and tubulin binding activities but the exact molecular function on this subunit remains uncertain.
UOM:
1 * 100 µl
Numéro de catalogue:
(45533-250MG)
Fournisseur:
Merck
Description:
Organic Standard, 3-Indoleacetic acid, Type de conditionnement: Flacon verre pour solides
UOM:
1 * 250 mg
Numéro de catalogue:
(BOSSBS-8660R-CY7)
Fournisseur:
Bioss
Description:
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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8660R-CY5)
Fournisseur:
Bioss
Description:
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.
UOM:
1 * 100 µl
Numéro de catalogue:
(630-3346)
Fournisseur:
DISCOVER ECHO
Description:
Rebel is designed around the user to challenge the status quo. Designed from the ground up to improve microscopy.
UOM:
1 * 1 ST
Fournisseur:
Avantor
Description:
PEEK
Fournisseur:
Biotium
Description:
PAb122 binds to the C-terminus (aa370-378) of both wild type and mutated p53. When microinjected into nuclei, PAb122 blocked re-entry into the S-phase of the cell cycle. Mutation and/or allelic loss of p53 is one of the causes of a variety of mesenchymal and epithelial tumors. If it occurs in the germ line, such tumors run in families. p53 Binds to a DNA consensus sequence, the p53 response element, and it regulates normal cell growth cycle events by activating transcription of genes, involved either in progression through the cycle, or causing arrest in G1 when the genome is damaged. In most transformed and tumor cells the concentration of p53 is increased 51000 fold over the minute concentrations (1000 molecules cell) in normal cells, principally due to the increased half-life (4 h) compared to that of the wild-type (20 min). p53 Localizes in the nucleus, but is detectable at the plasma membrane during mitosis and when certain mutations modulate cytoplasmic/nuclear distribution. p53 Is the most commonly mutated gene in spontaneously occurring human cancers. Mutations arise with an average frequency of 70% but incidence varies from zero in carcinoid lung tumors to 97% in primary melanomas. High concentrations of p53 protein are transiently expressed in human epidermis and superficial dermal fibroblasts following mild ultraviolet irradiation.
Numéro de catalogue:
(BOSSBS-3804R-A350)
Fournisseur:
Bioss
Description:
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3804R-CY5)
Fournisseur:
Bioss
Description:
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7719R-A750)
Fournisseur:
Bioss
Description:
DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7719R-A488)
Fournisseur:
Bioss
Description:
DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5347R)
Fournisseur:
Bioss
Description:
The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5600R-A750)
Fournisseur:
Bioss
Description:
Hamartin, or TSC1, is a suspected tumor suppressor implicated in the disease tuberous sclerosis 1. It is a negative regulator of cell division controlling the transition from G0/G1 to S phase, and it seems to act through the phosphatidylinositol 3 kinase/Akt pathway. TSC1 interacts with tuberin m(TSC2), which is thought to be a GAP (GTPase Activating Protein) for the Rap1 and Rab5 small G Proteins. The Hamartin/Tuberin complex has been shown to inhibit mTor. Hamartin has also been shown to interact with ERM (Ezrin-Radixin-Moesin) proteins and with F-actin, suggesting a role for TSC proteins in modulation of cell adhesion and morphology.
UOM:
1 * 100 µl
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