Recombinant Human CEP135 Protein, N-His from ProteoGenix; catalogue ARO-P11400; research use only.
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Recombinant Human CEP135 Protein, also known as centrosomal protein 135, is a highly conserved protein that plays a crucial role in the regulation of cell division and organization of the centrosome. This protein is encoded by the CEP135 gene and is expressed in various tissues, including the brain, heart, and kidney.
Recombinant Human CEP135 Protein is composed of 1183 amino acids and has a molecular weight of approximately 135 kDa. It contains multiple functional domains, including a coiled-coil domain, a leucine zipper domain, and a C-terminal centrosomal targeting domain. These domains are essential for the protein’s interaction with other centrosomal proteins and its localization to the centrosome.
The coiled-coil domain of Recombinant Human CEP135 Protein is responsible for its dimerization, which is necessary for its function. The leucine zipper domain, on the other hand, is involved in protein-protein interactions and plays a role in the assembly of the centrosome. The C-terminal centrosomal targeting domain is responsible for targeting the protein to the centrosome.
Recombinant Human CEP135 Protein is a key regulator of centrosome duplication and maturation. It is involved in the formation of the centrosome, which is the main microtubule organizing center in animal cells. The protein is required for the proper assembly and maintenance of the centrosome, which is crucial for cell division and organization.
During cell division, Recombinant Human CEP135 Protein plays a critical role in the separation of duplicated centrosomes. It facilitates the recruitment of other centrosomal proteins, such as γ-tubulin, to the centrosome, which is necessary for the formation of the mitotic spindle and proper cell division.
In addition to its role in cell division, Recombinant Human CEP135 Protein also plays a role in maintaining the integrity of the centrosome during interphase. It is involved in the regulation of the centrosome’s size and number, ensuring that the cell has the correct number of centrosomes for proper cell division and organization.
Due to its crucial role in centrosome organization and cell division, Recombinant Human CEP135 Protein has been studied extensively in various fields, including cancer research and developmental biology.
Aberrant expression or mutations in the CEP135 gene have been linked to various types of cancer, including breast, lung, and ovarian cancer. Recombinant Human CEP135 Protein has been used as an antigen in studies to understand its role in cancer development and progression. It has also been studied as a potential target for cancer therapy.
In developmental biology, Recombinant Human CEP135 Protein has been used to study the role of the centrosome in embryonic development. It has been shown to be essential for proper cell division and differentiation during early embryogenesis.
Furthermore, Recombinant Human CEP135 Protein has been used in various in vitro studies to investigate its role in cell cycle regulation and centrosome dynamics. It has also been used as a tool to study the function of other centrosomal proteins and their interactions.
Recombinant Human CEP135 Protein is a crucial protein involved in the regulation of centrosome organization and cell division. Its structure and activity make it an important target for research in various fields, including cancer biology and developmental biology. With the advancement of recombinant protein technology, further studies on Recombinant Human CEP135 Protein are expected to provide a better understanding of its role in cellular processes and
ProteoGenix catalogue number ARO-P11400. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 17.14 kDa; Fragment: Asn63-Pro188; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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