You Searched For: Bafilomycin+B1

Catalog Number: (BOSSBS-10342R-A680)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10342R-A350)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11246R-A488)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10342R-A647)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11246R-FITC)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (PRSI96-393)

Supplier: ProSci Inc.

Description: High-mobility group protein B1 (HMGB1) is also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a member of the HMGB family consisting of three members, HMGB1, HMGB2 and HMGB3. HMGB1 is a non-histone architectural chromosomal protein ubiquitously present in all vertebrate nuclei and binds double-stranded DNA without sequence specificity. The mechanism of inflammation and damage is binding to TLR4, which mediates HMGB1-dependent activation of macrophage cytokine release. This positions HMGB1 at the intersection of sterile and infectious inflammatory responses. HMGB1 has been studied as a DNA vaccine adjuvant and a target for cancer therapy.

UOM: 1 * 100 µG

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Catalog Number: (BSENC-1698-100)

Supplier: Biosensis

Description: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11333R-CY5)

Supplier: Bioss

Description: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

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Catalog Number: (BOSSBS-11333R-CY3)

Supplier: Bioss

Description: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11241R-CY5)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11241R-A488)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11241R)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11242R-CY3)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12582R)

Supplier: Bioss

Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into Alpha, Beta, and Gamma families, and the Beta- and Gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins constitute the major lens structural proteins, and they associate into dimers, tetramers, and higher order aggregates. The Beta-crystallin subfamily is composed of several gene products, including Beta A1-, Beta A2-, Beta A3-, Beta A4-, Beta B1-, Beta B2- and Beta B3-crystallin. The Beta A1- and Beta A3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and Beta A1-crystallin is generated by use of an alternate translation initiation site.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11241R-CY7)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11242R-CY5)

Supplier: Bioss

Description: Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.

UOM: 1 * 100 µl

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