You Searched For: face+shields

Catalog Number: (10252-178)

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.

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Catalog Number: (10276-684)

Supplier: Bioss

Description: Zinc finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger protein 750 is a 723 amino acid member of the Krüppel C2H2-type zinc finger protein family. Localized to the nucleus, ZNF750 contains one conserved C2H2 zinc finger domain and is expressed in the skin, lungs, prostate, placenta and thymus. ZNF750 is also expressed in primary human keratinocytes but not in fibroblasts. Mutations in the gene encoding ZNF750 cause Seborrhea-like dermatitis with psoriasiform, a condition characterized by a chronic and diffuse rash on the face and hyperkeratosis of skin over the elbows, soles, knees and palms.

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Catalog Number: (10251-974)

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.

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Catalog Number: (10252-194)

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.

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Catalog Number: (10251-976)

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.

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Catalog Number: (10103-824)

Supplier: Prosci

Description: PHF6 is a member of the plant homeodomain (PHD)-like finger (PHF) family. PHF6 is a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of its gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS).This gene is a member of the plant homeodomain (PHD)-like finger (PHF) family. It encodes a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of this gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS), a disorder characterized by mental retardation, epilepsy, hypogonadism, hypometabolism, obesity, swelling of subcutaneous tissue of the face, narrow palpebral fissures, and large ears. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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Catalog Number: (10375-474)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (76084-594)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (89416-052)

Supplier: Prosci

Description: Bik Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by the activation of proteolytic enzymes termed caspases. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such protein BIK was recently identified as an endoplasmic reticulum (ER)-residing pro-apoptotic member of the Bcl-2 homology domain-3 (BH3)-only group of the Bcl-2 family that stimulates mitochondrial release of cytochrome c following p53 induction of apoptosis. A significant fraction of BIK is found as an ER transmembrane protein, with most of the protein facing the cytosol. Restricting BIK to the ER membrane by replacing the transmembrane region with that of the ER-selective membrane anchor of cytochrome b resulted in a decreased cytochrome c release from mitochondria and a corresponding drop in cell death. Recent evidence suggests that BIK cooperates with NOXA, another BH3-only protein, to somehow enhance the activation of Bax to stimulate the rapid release of cytochrome c from mitochondria.

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Catalog Number: (10800-366)

Supplier: Rockland Immunochemical

Description: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by the activation of proteolytic enzymes termed caspases. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such protein BIK was recently identified as an endoplasmic reticulum (ER)-residing pro-apoptotic member of the Bcl-2 homology domain-3 (BH3)-only group of the Bcl-2 family that stimulates mitochondrial release of cytochrome c following p53 induction of apoptosis. A significant fraction of BIK is found as an ER transmembrane protein, with most of the protein facing the cytosol. Restricting BIK to the ER membrane by replacing the transmembrane region with that of the ER-selective membrane anchor of cytochrome b resulted in a decreased cytochrome c release from mitochondria and a corresponding drop in cell death. Recent evidence suggests that BIK cooperates with NOXA, another BH3-only protein, to somehow enhance the activation of Bax to stimulate the rapid release of cytochrome c from mitochondria.

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Catalog Number: (10375-470)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (10375-466)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (10371-072)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (76324-122)

Supplier: Safety & Industrial Supplies

Description: FACE SHIELD F10 34-0AP CLR 15 1/2IN CS50

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Catalog Number: (10110-568)

Supplier: Prosci

Description: PHF6 is a member of the plant homeodomain (PHD)-like finger (PHF) family. PHF6 is a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of its gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS).This gene is a member of the plant homeodomain (PHD)-like finger (PHF) family. It encodes a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of this gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS), a disorder characterized by mental retardation, epilepsy, hypogonadism, hypometabolism, obesity, swelling of subcutaneous tissue of the face, narrow palpebral fissures, and large ears. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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Catalog Number: (10375-472)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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