234437 Results for: "Amberlyst® 15 H\u207A form"

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: Bioss

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodelling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Bioss

Ubiquitin-dependent proteolysis mediates selective destruction of various cell cycle regulators, transcription factors and tumor suppressors. In eukaryotic cells, selective breakdown of cellular proteins is ensured by their ubiquitination and subsequent degradation by the 26S proteasome. At specific stages of development, embryo- and tissue-specific components of the 26S proteasome form, facilitating proteolysis. 20S Proteasome ?, also designated macropain subunit C2 or PROS-30, is a prosomal protein involved in a non-lysosomal ATP/ubiquitin-dependent proteolytic pathway. The entire proteasome is composed of at least 15 non-identical subunits which form a highly-ordered ring-shaped structure.

Supplier: Biowest

Amphotericin B used in tissue culture to prevent growth of yeasts and fungi. It changes the function and integrity of eucaryotic cell membranes by forming complexes with sterols (cholesterol) hence having no effect on bacteria. Cause leakage of glucose.

Supplier: Bioss

RAS superfamily comprises around 50 related genes encoding GTP-binding domain (G-proteins) involved in signal transduction. The main genes are HRAS, NRAS and KRAS. Ras proteins are membrane-bound GTPases. The inactive form is GDP-bound. They are activated by ligand-binding receptor tyrosine kinases such as EGFR, PDGFR, colony-stimulating factor and fibroblast growth factor. These kinases transiently convert RAS-GDP to RAS-GTP, the active form of RAS. Single amino acid substitutions can activate RAS making it highly oncogenic. Such mutations generally reduce the GTPase activity of RAS, prolonging it in its active GTP-bound form. The consequence of this is sustained activation of the RAF1-MAPK signalling pathway. RAS mutations are found in 10-15% of tumours. A high incidence of RAS mutations is found in pancreatic cancers.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: GRANT INSTRUMENTS

Replacement platform for 22 tubes up to 15 mm Ø for PTR-25

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: ENZO LIFE SCIENCES

IL-21 is a cytokine identified in human and mouse that shows significant homology to IL-2, IL-4, and IL-15. The receptor for IL-21 (IL-21R) also termed NILR for novel interleukin receptor) is a member of the class I cytokine receptor family. IL-21R forms a complex with the common cytokine receptor gamma chain, gammac, and mediates IL-21 signaling via the JAK-Stat pathway. IL-21 is expressed in activated T-cells, as well as HL-60 and THP-1 cell lines. IL-21 plays a role in the proliferation and maturation of NK, B- and T-cell populations.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: KINEMATICA

Dispersing vessel, cloverleaf-like, without cap, Borosilicate glass, Capacity: 35 ml, Ext.Ø: 30 mm, Height: 100 mm, GS 15

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Supplier: TECHNICAL QUARTZ SOLUTIONS

Made of silica.

Supplier: Bioss

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.