Votre recherche pour: 1,2,3,4,5-Pentam\u00E9thylcyclopentadiene

Fournisseur: Biotium

Description: Recognizes a protein of 75 kDa, identified as mu heavy chain of human immunoglobulins. It does not cross-react with alpha (IgA), gamma (IgG), epsilon (IgE), or delta (IgD), heavy chains, T-cells, monocytes, granulocytes, or erythrocytes. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. IgM antibody is prominent in early immune responses to most antigens. Aberrant levels are associated with immune deficiency states, hereditary deficiencies, myeloma, Waldenstrom's macroglobulinemia, chronic infection and hepatocellular disease. This MAb is useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkin's lymphomas. The most common feature of these malignancies is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Numéro de catalogue: (BOSSBS-11041R-A680)

Fournisseur: Bioss

Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterised channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.

UOM: 1 * 100 µl

Promotion

Fournisseur: Thermo Fisher Scientific

Description: D-(+)-Arabitol 99%

MSMD

Fournisseur: Biotium

Description: Recognizes a protein of 75 kDa, identified as mu heavy chain of human immunoglobulins. It does not cross-react with alpha (IgA), gamma (IgG), epsilon (IgE), or delta (IgD), heavy chains, T-cells, monocytes, granulocytes, or erythrocytes. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. IgM antibody is prominent in early immune responses to most antigens. Aberrant levels are associated with immune deficiency states, hereditary deficiencies, myeloma, Waldenstrom's macroglobulinemia, chronic infection and hepatocellular disease. This MAb is useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkin's lymphomas. The most common feature of these malignancies is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Fournisseur: TCI

Description: Allylpentafluorobenzène ≥98.0% (par GC)

Fournisseur: Thermo Fisher Scientific

Description: Perfluorotoluène ≥98%

MSMD Certificats

Numéro de catalogue: (BOSSBS-11041R-A350)

Fournisseur: Bioss

Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R-CY5.5)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R-CY7)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R-A750)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R-A555)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-4197R-HRP)

Fournisseur: Bioss

Description: The Sarco(endo)plasmic-reticulum (SER) regulatory protein, Phospholamban (PLB), is a small, plasma membrane-associated protein found in the SER of cardiac, smooth and slow-twitch muscle. Believed to assemble into a pentamer, PLB regulates cardiac contractility and Ca2+ affinity for cardiac SER Ca2+ ATPase (SERCA2a). Non-phosphorylated PLB associates with SERCA2a, and inhibits Ca2+ reuptake into the SER. PLB activation occurs when key Serine/Threonine residues in PLB (Ser-10, Ser-16, Thr-17) are phosphorylated by numerous effectors, which include PKC, PKA, PKG, and CaM kinase. Phosphorylation of PLB causes dissociation from SERCA2a and a subsequent increase in the rate of Ca2+ reuptake into the SER, which accelerates ventricular relaxation.

UOM: 1 * 100 µl

Promotion

Fournisseur: TCI

Description: Ribitol ≥97.0% (par GC)

Numéro de catalogue: (BOSSBS-11041R-HRP)

Fournisseur: Bioss

Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-11041R-CY5)

Fournisseur: Bioss

Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.

UOM: 1 * 100 µl

Promotion