269 Results for: "Mrazáky"

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (Biotin)

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (APC (Allophycocyanin))

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (AP (Alkaline Phosphatase))

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (PE (Phycoerythrin))

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilisation of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subcellular Filamin 2 localisation, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody

Supplier: ABGENT

Anti-KY Rabbit Polyclonal Antibody

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilization of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subceullular Filamin 2 localization, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: BIOSS INC

KY peptidase (Kyphoscoliosis peptidase) is a 561 amino acid cytoskeleton protease that interacts with several sarcomeric cytoskeletal proteins, including Filamin 2. KY peptidase probably plays a role in the maturation, function and stabilisation of the neuromuscular junction. KY-null mouse mutants exhibit distinct irregular subcellular Filamin 2 localisation, suggesting that KY peptidase deficiency may be the cause of several types of limb-girdle muscular dystrophies.

Supplier: FUJIFILM WAKO CHEMICALS

The Limulus Color KY Series are quantitative kinetic chromogenic assays (KCA) that are endotoxin-specific and unreactive to (1→3)-β-D-glucan. This series includes both a multi-test kit and a single-test kit, which utilise a synthetic substrate that produces a yellow color to detect endotoxin with high sensitivity.

Supplier: UNITED BIOCHEMICALS

Anti-KY Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Supplier: FUJIFILM WAKO CHEMICALS

The Limulus Color KY Series are quantitative kinetic chromogenic assays (KCA) that are endotoxin-specific and unreactive to (1→3)-β-D-glucan. This series includes both a multi-test kit and a single-test kit, which utilize a synthetic substrate that produces a yellow color to detect endotoxin with high sensitivity.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or -sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or -sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: BIOSS INC

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.