You Searched For: ankyrin

Catalog Number: (BOSSBS-7594R-A680)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialised membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified.

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Catalog Number: (BOSSBS-6967R)

Supplier: Bioss

Description: Members of the Ankyrin family of proteins mediate the attachment of integral membrane proteins to the cytoskeleton. ANK1, ANK2 and ANK3 genes encode for the proteins in this family, Ankyrin-1 (also designated Ankyrin R), Ankyrin B and Ankyrin G, respectively. The proteins are structured similarly each composed of an N-terminal domain with multiple Ankyrin repeats, a highly conserved central spectrin binding domain, and C-terminal regulatory domains which are susceptible to the most variance. Both Ankyrin B and Ankyrin G are essential for normal neuronal functions. Ankyrin B, or brain Ankyrin is predominantly expressed in the plasma membrane of neurons as well as glial cells throughout the brain. Two transcripts have been described with alternative splicing resulting in additional isoforms. The Ankyrin B protein associates with the spectrin-actin network, mediates axon fasciculation, and stabilizes axon bundles. Ankyrin B is required for coordinated assembly of Na/Ca exchanger, Na/K ATPase, and inositol trisphosphate (InsP(3)) receptor at transverse-tubule/sarcoplasmic reticulum sites in cardiomyocytes.

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Catalog Number: (BOSSBS-7594R-CY7)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

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Catalog Number: (BOSSBS-7594R)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-FITC)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-A488)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-A350)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

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Catalog Number: (BOSSBS-8728R)

Supplier: Bioss

Description: Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

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Catalog Number: (BOSSBS-8728R-A350)

Supplier: Bioss

Description: Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8728R-FITC)

Supplier: Bioss

Description: Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-HRP)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-CY5.5)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7961R-A350)

Supplier: Bioss

Description: Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal Ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The Ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7961R-CY5)

Supplier: Bioss

Description: Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal Ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The Ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-CY3)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7594R-A555)

Supplier: Bioss

Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of Ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most Ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple Ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic Ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of Ankyrin 1 have been described. Truncated muscle-specific isoforms of Ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

UOM: 1 * 100 µl

Sale