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Artikel-Nr: (PRSI91-252)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 91-252
Beschreibung: Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) is a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. During apoptosis, it is translocated from the mitochondria to the nucleus to function as a proapoptotic factor in a caspase-independent pathway, while in normal mitochondria, it functions as an antiapoptotic factor via its oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces parthanatos i.e., caspase-independent fragmentation of chromosomal DNA. AIFM1 interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. It binds to DNA in a sequence-independent manner and plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells.
UOM: 1 * 50 µG


Artikel-Nr: (PRSI92-519)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 92-519
Beschreibung: Hemoglobin subunit theta-1 is a protein that in humans is encoded by the HBQ1 gene. Theta-globin mRNA is originally found in human fetal erythroid tissue but not in adult erythroid or other nonerythroid tissue. Theta-1 is a member of the human alpha-globin gene cluster that includes five functional genes and two pseudogenes. Research supports a transcriptionally active role for the gene and a functional role for the peptide in specific cells, possibly those of early erythroid tissue. Hemoglobin has a quaternary structure characteristically composed of many multi-subunit globular proteins. Most of the amino acids in hemoglobin form alpha helices, connected by short non-helical segments. Hydrogen bonds stabilize the helical sections inside this protein, causing attractions within the molecule, folding each polypeptide chain into a specific shape. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.
UOM: 1 * 50 µG


Artikel-Nr: (ABFRLF-PA0187)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0187
Beschreibung: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a
redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cystein residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide –isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NFkB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0077)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0077
Beschreibung: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/ dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide–isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).
UOM: 1 * 0,1 mL


Lieferant: MP Biomedicals
Beschreibung: Storage: Room Temperature
Guanidine hydrochloride consists of a network of guanidinium cations and chloride anions linked by N–H•••Cl hydrogen bonds, it is a strong chaotropic agent. Guanidine HCl may agglomerate upon storage. It may appear as a free-flowing crystalline powder, a free flowing powder with solid material dispersed throughout, or a solid. The quality of the product does not appear to be affected and solutions prepared from the free-flowing and lumpy guanidine HCl appear identical.
Guanidine hydrochloride can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary. Also used in the isolation of RNA. Guanidine hydrochloride is a strong chaotropic agent useful for the denaturation and subsequent refolding of protein, it can solubilize insoluble or denatured proteins such as inclusion bodies and be used for the recovery of periplasmic proteins.

Lieferant: MP Biomedicals
Beschreibung: Guanidine Hydrochloride is a protein denaturant and thus having an important role in molecular weight determinations.
Guanidine Hydrochloride is a strong chaotropic agent useful for the denaturation and subsequent refolding of proteins. This strong denaturant can solubilize insoluble or denatured proteins such as inclusion bodies. This can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary. Guanidine HCl is used in the isolation of RNA to dissociate the nucleoprotein into its nucleic acid and protein moieties. It is an inhibitor of RNase. Highly concentrated (6 - 8 M) Guanidine HCl solutions are used to denature native globular proteins. It apparently disrupts hydrogen bonds which hold the protein in its unique structure. However, there also is evidence suggesting that guanidine hydrocholoride may disrupt hydrophobic interactions by promoting the solubility of hydrophobic residues in aqueous solutions.
Artikel-Nr: (ABFRLF-PA0012)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0012
Beschreibung: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cystein residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide –isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).
UOM: 1 * 0,1 mL


Artikel-Nr: (PRSI96-367)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 96-367
Beschreibung: Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.
UOM: 1 * 100 µG


Artikel-Nr: (PRSI96-366)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 96-366
Beschreibung: Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.
UOM: 1 * 100 µG


Artikel-Nr: (ABFRLF-MA0080)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0080
Beschreibung: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/ dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide–isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0079)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0079
Beschreibung: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/ dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide–isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).
UOM: 1 * 0,1 mL


Artikel-Nr: (PRSI96-365)
Lieferant: ProSci Inc.
Hersteller Artikel Nummer : 96-365
Beschreibung: Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.
UOM: 1 * 100 µG


Artikel-Nr: (95293-0.1ML)
Lieferant: Merck
Hersteller Artikel Nummer : 95293-0.1ML
Beschreibung: Hydrogen ionophore I - cocktail B, Selectophore™ Ionophor, Supelco®
UOM: 1 * 0,1 mL


Artikel-Nr: (8.18068.0100)
Lieferant: Merck
Hersteller Artikel Nummer : 8.18068.0100
Beschreibung: Hydrogen fluoride pyridine complex (HF 65%) zur Synthese, Sigma-Aldrich®
UOM: 1 * 100 mL

Lieferant: Merck
Beschreibung: Poly(methyl hydrogen siloxane) zur Synthese, Sigma-Aldrich®
Lieferant: Merck
Beschreibung: Tetrahexylammoniumhydrogensulfat, Supelco®

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