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acids+and+salts+high+purity
Numéro de catalogue:
(BOSSBS-13032R-CY3)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11437R-CY5)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11427R-A647)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include the SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes, and including the human proteins Srb7, Med6 (also designated DRIP33) and Med7 (also designated DRIP34) (2,3). SMCC associates with the RNAPII (RNA polymerase II) holoenzyme through Srb7 and, in turn, enhances gene-specific activation or repression induced by DNA-binding transcription factors (4). Med6 and Med7, as well as other components of SMCC, associate with coactivator proteins from the TRAP (thyroid hormone receptor-activating protein) complex and DRIP (for vitamin D receptor interacting protein) complex to facilitate steroid receptor dependent transcriptional activation (4,5). Additionally, SMCC associates with PC4 (positive cofactor 4) to repress basal transcription independent of RNAPII activity (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0362R-HRP)
Fournisseur:
Bioss
Description:
Protein A is a 40-60 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus (SPA). SPA binds proteins from many of mammalian species, most notably IgGs, and helps inhibit phagocytic engulfment and acts as an immunological disguise via this type of interaction, thus the bacteria will disrupts opsonization and phagocytosis. SPA is known to bind with Fc region of immunoglobulins preferentially through interaction with the VH3 variable region of the heavy chain. SPA has been shown to bind with high affinity to human IgG1 and IgG2 as well as mouse IgG2a and IgG2b, whereas bind with moderate affinity to human IgM, IgA and IgE as well as mouse IgG3 and IgG1. SPA is often produced in E. coli and is practically coupled to other molecules such as enzymes, biotin, radioactive iodine for use in immunology and other biological research. SPA is also immobilized onto solid supports such as agarose beads for total IgG purifying or interest protein or protein complex identifying in immunoprecipitation studies.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1357R-HRP)
Fournisseur:
Bioss
Description:
The p70/p80 autoantigen is a nuclear complex consisting of two subunits with molecular masses of approximately 70 and 80 kDa. The complex functions as a single-stranded DNA-dependent ATP-dependent helicase. The complex may be involved in the repair of nonhomologous DNA ends such as that required for double-strand break repair, transposition, and V(D)J recombination. High levels of auto to p70 and p80 have been found in some patients with systemic lupus erythematosus. [provided by RefSeq]. Ku70 heterodimerises with Ku80 to form the ATP-dependent DNA helicase II, a single stranded helicase that binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. The heterodimer plays a role in non-homologous end-joining (NHEJ) required for double-strand break repair and V(D)J recombination. It acts as the regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit (PRKDC) for DNA. The Ku70/80 heterodimer is also required for osteocalcin gene expression.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11907R)
Fournisseur:
Bioss
Description:
ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. As the largest family of transmembrane proteins, ABC genes comprise several subfamilies (ABC1, ABCA, ABCE, ABCF, MDR/TAP, MRP, ALD, OABP, GCN20 and White (also known as ABCG)). In bacteria, ABC transporters are used to import compunds that cannot be obtained by diffusion. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process or outside the cell for transport to other organs, or for secretion from the body. ABCB9 (also designated Transporter associated with antigen processing (TAP)-like or TAPL) forms a homodimer, which is localized in lysosomes. It functions as an ATP-dependent peptide transporter that shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. ABCB9 transports these peptides with low affinity but high efficiency.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11562R-HRP)
Fournisseur:
Bioss
Description:
Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterized by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin2 (formerly known as SIP1 for SMN interacting protein) associates directly with SMN and is a part of the SMN complex containing Gemin3 (a DEAD-box RNA helicase), Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in splicesomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (Gemini of the coiled bodies). The SMN-Gemin2 complex is associated with spliceosomal snRNAs U1 and U5. Gemin2 is expressed in spinal cord. It can be induced by TGF∫ treatment and expression is high in several E-cadherin negative human carcinoma cell lines. SMN is expressed in a wide variety of tissues including brain, kidney, liver and spinal cord, and moderately in skeletal and cardiac muscle. The gene encoding Gemin2 maps to human chromosome 14q13.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11562R-A350)
Fournisseur:
Bioss
Description:
Spinal muscular atrophy (SMA) is an autosomal recessive neurodegenerative disease characterized by loss of motor neurons in the spinal cord. SMA is caused by deletion or loss-of-function mutations in the SMN (survival of motor neuron) gene. Gemin2 (formerly known as SIP1 for SMN interacting protein) associates directly with SMN and is a part of the SMN complex containing Gemin3 (a DEAD-box RNA helicase), Gemin4, Gemin5 and Gemin6, as well as several spliceosomal snRNP proteins. The SMN complex plays an essential role in splicesomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing of the nucleus. It is found in both the cytoplasm and the nucleus. The nuclear form is concentrated in subnuclear bodies called gems (Gemini of the coiled bodies). The SMN-Gemin2 complex is associated with spliceosomal snRNAs U1 and U5. Gemin2 is expressed in spinal cord. It can be induced by TGF∫ treatment and expression is high in several E-cadherin negative human carcinoma cell lines. SMN is expressed in a wide variety of tissues including brain, kidney, liver and spinal cord, and moderately in skeletal and cardiac muscle. The gene encoding Gemin2 maps to human chromosome 14q13.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
Numéro de catalogue:
(BTIUBNUM0879-50)
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
Numéro de catalogue:
(BOSSBS-9072R-FITC)
Fournisseur:
Bioss
Description:
Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9072R-A647)
Fournisseur:
Bioss
Description:
Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15371R-A488)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15371R-CY7)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
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