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The centromere is a specialized chromatin domain, present throughout the cell cycle, that acts as a platform on which the transient assembly of the kinetochore occurs during mitosis. All active centromeres are characterized by the presence of long arrays nucleosomes in which CENPA replaces histone H3. CENPM is an additional factor required for centromere assembly.

CENPH is a member of the centromere protein H family. CENPH protein is a component of the CENPA-NAC (nucleosome-associated) complex which has a vital part in assembly of kinetochore proteins. The CENPA-NAC complex utilizes the CENPA-CAD (nucleosome distal) complex and is involved in integration of freshly synthesized CENPA into centromeres.

Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
CENPB is the most important of the centromeric autoantigens: it has a molecular weight of approx. 66 kDa and plays an important role in the formation of the centromeric chromatin. CENPB antibodies are present in the sera of up to 80% of patients with CREST syndrome.

Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
CENPA is another important centromeric autoantigen in addition to CENPB: it has a molecular weight of approx. 20 kDa and is incorporated into centromeric chromatin due to its histone-like properties. CENPA antibodies are an important marker for correct diagnosis of Scleroderma / CREST syndrome in CENPB-autoantibody negative patients.

Centromere protein P (CENPP) is component of the CENPA-CAD (nucleosome distal) complex, which is a complex recruited to centromeres and involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENPP protein is involved in incorporation of newly synthesized CENPA into centromeres by way of its interaction with the CENPA-NAC complex.

Centromere Protein U, also known as CENPU is a specialized chromatin domain, present throughout the cell cycle. CENPU performs as a platform on which the transient assembly of the kinetochore takes place during mitosis. CENPU plays a major role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein is responsible for the first recruitment and maintenance of the kinetochore PLK1 population until its degradation. CENPU is also implicated in transcriptional repression.

CENPQ is a Component of a CENPH-CENPI-associated centromeric complex which targets CENPA to centromeres and is necessary for proper kinetochore function and mitotic progression. CENPQ takes part in incorporation of newly synthesized CENPA into centromeres using its interaction with the CENPA-NAC complex.

Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

BLOC1S2 is a member of the BLOC1S2 family. Biogenesis of lysosome-related organelles complex 1 or BLOC-1 is a universally expressed multisubunit protein complex which is essential for regular biogenesis of specialized organelles of the endosomal-lysosomal system, like melanosomes and platelet dense granules. BLOC1S2 takes part in cell proliferation.

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

Caltractin (CETN2) is a member of a family of calcium-binding proteins and is a structural component of the centrosome. CETN2 has a role in nucleotide excision repair via association with xeroderma pigmentosum group C protein, suggesting possible coupling of cell division and nucleotide excision repair.

CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

Spindle And Kinetochore Associated Complex Subunit 1 (SKA1) is a part of the kinetochore-microtubule interface which associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. SKA1 is necessary for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint.

SMARCA4 belongs to the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Proteins in this family have helicase and ATPase activities and are considered to regulate transcription ofcertain genes by altering the chromatin structure around those genes. SMARCA4 is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is essential for transcriptional activation of genesnormally repressed by chromatin. In addition, SMARCA4 is able to bind BRCA1, as well as regulating the expression ofthe tumorigenic protein CD44. Moreover, mutations in SMARCA4 cause rhabdoid tumor predisposition syndrome type 2.

CBX5 belongs to the heterochromatin protein family. CBX5 is enriched in the heterochromatin and linked with centromeres. CBX5 takes part in the creation of functional kinetochore by interaction with important kinetochore proteins. CBX5 has a pseudogene situated on chromosome 3. Additionaly, The CBX5 proteins reconnect with chromatin at the end of mitosis, as Histone H3 is dephosphorylated.

CBX1 is an enriched heterochromatin which belongs to the heterochromatin protein family. The centromeres related CBX1 identifies and binds histone H3 tails methylated at 'Lys-9', causing epigenetic repression. Collaboration with lamin B receptor (LBR) can impact the relations between the heterochromatin and the inner nuclear membrane. CBX1 has a vital part in the epigenetic control of chromatin structure and gene expression.

CBX3 takes part in transcriptional silencing in heterochromatin-like complexes. CBX3 identifies and binds histone H3 tails methylated at 'Lys-9', thereby create an epigenetic repression. Additionally, CBX3 takes part in the formation of functional kinetochore by interacting with MIS12 complex proteins.

Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.

Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia.