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Cell Architecture Nuclear Envelope

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gp210 (C-terminal) Antibody- Rabbit Anti-gp210 (C-terminal)
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. GP210 is a membrane-spanning glycoprotein that is a major component of the nuclear pore complex, it is an evolutionarily conserved and has early roles in nuclear pore formation and mediates pore dilation with its tail-binding partners
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gp210 (N-terminal) Antibody- Rabbit Anti-gp210 (N-terminal)
The nuclear pore complex is a massive structure that extends across the nuclear envelope forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells GP210 is a membrane-spanning glycoprotein that is a major component of the nuclear pore complex it is an evolutionarily conserved and has early roles in nuclear pore formation and mediates pore dilation with its tail-binding partners
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Nup53 Antibody- Rabbit Anti-Nup53
Nup53 encodes a recently identified nuclear pore protein. Transport of macromolecules between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complex (NPC), a large macromolecular complex that spans the nuclear envelope. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate. Nup53p forms a complex with two other nucleoporins, Nup170p and Asm4p. The complex is found on both the nuclear and cytoplasmic faces of the NPC, and associates with Pse1p, a member of a protein family implicated in nuclear protein import, via direct interaction between Nup53p and Pse1p. Nup53p is structurally similar to Asm4p, and similar proteins sequences are found in several eukaryotes including human and other multicellular species. Nup53p is not essential; deletion of Nup53 and ASM4 causes slow growth and altered subcellular distribution of Pse1p. In a nup53 pse1 double mutant, NLS-containing proteins are mislocalized to the cytoplasm
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