acids+and+salts+high+purity
Numéro de catalogue:
(IMMRIR2667)
Fournisseur:
ImmunoReagents
Description:
TRITC (Tetramethylrhodamine isothiocyanate) is a popular rhodamine derivative pink in color but emits a red-orange color upon Emission at 580nm. TRITC is frequently paired with FITC in double labeling experiments and conjugated antibodies are often used in immunofluorescence microscopy, flow cytometry, FLISA (fluorescent ELISA) and high throughput screening assays. These conjugates are best excited with the 532 nm spectral line of the He-Ne laser and are also recommended as a second color detection reagent in in situ hybridization applications. (Excitation/Emission = 555nm / 580nm Emission Color = Orange to Red (Similar Dyes: Alexa Fluor 555, Cy3, DyLight 550)
UOM:
1 * 1 mg
Fournisseur:
Biotium
Description:
Recognizes a protein of 70 kDa, which is identified as CD86. CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
Fournisseur:
Biotium
Description:
Recognizes a protein of 70 kDa, which is identified as CD86. CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
Numéro de catalogue:
(BNUM1146-50)
Fournisseur:
Biotium
Description:
Recognizes a protein of 70 kDa, which is identified as CD86. CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-12873R-A750)
Fournisseur:
Bioss
Description:
Bone morphogenic proteins (BMPs) are members of the TGF Beta superfamily. BMPs are involved in the induction of cartilage and bone formation. In vivo studies have shown that BMP-2 (also designated BMP-2A) and BMP-3 can independently induce cartilage formation. Smad3 association with the TGF Beta receptor complex and Smad1 translocation to the nucleus are observed after the addition of BMP-4 (also designated BMP-2B), suggesting that BMP-4 may play a role in activation of the Smad pathway. BMP-5, BMP-6 and BMP-7 all share high sequence homology with BMP-2, indicating that they each may be able to induce cartilage formation. BMP-8 (also designated OP-2) is thought to be involved in early development, as detectable expression has not been found in adult organs.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2015R-A750)
Fournisseur:
Bioss
Description:
Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localisation. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2015R-A647)
Fournisseur:
Bioss
Description:
Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2015R-A680)
Fournisseur:
Bioss
Description:
Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localisation. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
UOM:
1 * 100 µl
Fournisseur:
Sartorius Balances
Description:
Entris® II Advanced precision balances feature isoCAL, intuitive graphic touch display and 13 built-in applications. Highly accurate results are guaranteed via the monolithic weigh cell technology. High chemical resistance is ensured by using parts made from hard wearing PBT, stainless steel and glass. Integrated protection systems increase reliability of weighing results: Three configurable levels determine valid weighing data and ensure only valid data is transferred to external devices.
Numéro de catalogue:
(BOSSBS-9366R-CY3)
Fournisseur:
Bioss
Description:
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. A pseudogene has been identified on chromosome 17.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9366R-A647)
Fournisseur:
Bioss
Description:
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. A pseudogene has been identified on chromosome 17.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6210R-A350)
Fournisseur:
Bioss
Description:
WD-repeat proteins are a large family of eukaryotic proteins coordinating multi-protein complex assemblies. Their role has been implicated in multiple cellular processes including signal transduction, transcriptional regulation, cell cycle control and apoptosis. NRIP is a novel 860a.a nuclear protein consisting of seven conserved WD40 domains and one NLS motif. It binds to androgen and glucocorticoid receptors and up-regulates their transcriptional activity, thereby functioning as a nuclear receptor co-activator. Role of NRIP has been implicated in cell growth and also in cervical and prostrate cancer, thus indicating a potential therapeutic intervention. Northern Blot analysis detects a high expression of NRIP in skeletal muscle and testis and low expression in heart, prostrate and adrenal gland.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6210R-A647)
Fournisseur:
Bioss
Description:
WD-repeat proteins are a large family of eukaryotic proteins coordinating multi-protein complex assemblies. Their role has been implicated in multiple cellular processes including signal transduction, transcriptional regulation, cell cycle control and apoptosis. NRIP is a novel 860a.a nuclear protein consisting of seven conserved WD40 domains and one NLS motif. It binds to androgen and glucocorticoid receptors and up-regulates their transcriptional activity, thereby functioning as a nuclear receptor co-activator. Role of NRIP has been implicated in cell growth and also in cervical and prostrate cancer, thus indicating a potential therapeutic intervention. Northern Blot analysis detects a high expression of NRIP in skeletal muscle and testis and low expression in heart, prostrate and adrenal gland.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11040R-HRP)
Fournisseur:
Bioss
Description:
Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11040R-A555)
Fournisseur:
Bioss
Description:
Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11040R-A350)
Fournisseur:
Bioss
Description:
Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.
UOM:
1 * 100 µl
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