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Cow (Bovine) Polyclonal CENPF Primary Antibody for ICC, FACS - ABIN152930
Rattner, Rao, Fritzler, Valencia, Yen: CENP-F is a .ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization. in Cell motility and the cytoskeleton 1994
Show all 45 Pubmed References
Our data show that mutation of the CENP-F gene leads to an unexpected hyperstabilization of the MT network, with a unique loss of dynamic instability. With disruption of MT dynamics, CENP-F-/- cells exhibit dramatic loss of directionally persistent migration, defects in focal adhesion disassembly and lamellipodial formation/retraction, change in cilia frequency, and loss of regulation of cell shape.
FOXM1 (show FOXM1 Antibodies) and CENPF are master regulators of prostate cancer malignancy, and can serve as drug response markers for antineoplastic drugs efficiency.
Loss of CENP-F function in developing myocytes leads to decreased cell division, blunting of trabeculation and an initially smaller, thin-walled heart.
These data demonstrate that CMF1 regulates myocyte differentiation by interaction with Rb family members to induce expression of myogenic regulatory factors.
Data show that the post-anaphase, KEN (show PCNT Antibodies)-box-dependent degradation of Cenp-F requires it to be farnesylated, a post-translational modification usually linked to membrane association.
Results identify Hook2 (show HOOK2 Antibodies), a linker protein (show LAT Antibodies) that is essential for regulation of the microtubule network at the centrosome, as a binding partner of CENP-F.
LEK1 specifically functions during murine development to regulate the activity of Rb proteins during cell division and proliferation.
These data suggest a role for LEK1 in regulating the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing cardiomyocytes.
Results indicate that Raf (show RAF1 Antibodies)-arrested myoblasts may serve as a model system for satellite cell cycle studies and that E2F5 and LEK1 translocation to the nucleus is an important first step during entry into quiescence.
LEK1 plays a prominent role in regulating dendritic cell (DC) function for T cell activation, since knockdown of LEK1 expression results in the rapid maturation of Chlamydia-exposed DCs as measured by analysis of key activation markers.
This is the second case report identifying CENPF mutation as the cause of Stromme syndrome
Authors suggest that CENP-F might act as a transporter of mitochondria and other cellular cargoes by attaching them to dynamic microtubule ends during both polymerization and depolymerization of tubulin (show TUBB Antibodies).
Tumors with higher topoisomerase IIalpha and/or mitosin expression have a higher risk of recurrence after initial treatment, and these patients may benefit from adjuvant treatment and closer radiological follow-up
We show for the first time that Stromme syndrome is an autosomal-recessive disease caused by mutations in CENPF that can result in a wide phenotypic spectrum.
Miro and Cenp-F promote anterograde mitochondrial movement and proper mitochondrial distribution in daughter cells.
Mitosin and pHH3 immunostaining predict poorer survival in astrocytomas WHO grades II and III.
Our data identify CENPF as a new centriolar disease gene implicated in severe human ciliopathy and microcephaly related phenotypes
the increased expression of CENPF plays an important role in the progression of PCa (show FLVCR1 Antibodies).
N-terminal microtubule-binding domain of CENP-F prefers curled oligomers of tubulin (show TUBB Antibodies) relative to microtubule walls by approximately fivefold, suggesting it may contribute to the firm bonds between kinetochores and flared plus ends of dynamic microtubules
FOXM1 (show FOXM1 Antibodies) and CENPF function synergistically to promote tumor growth by coordinated regulation of target gene expression and activation of key signaling pathways associated with prostate cancer malignancy.
This gene encodes a protein that associates with the centromere-kinetochore complex. The protein is a component of the nuclear matrix during the G2 phase of interphase. In late G2 the protein associates with the kinetochore and maintains this association through early anaphase. It localizes to the spindle midzone and the intracellular bridge in late anaphase and telophase, respectively, and is thought to be subsequently degraded. The localization of this protein suggests that it may play a role in chromosome segregation during mitotis. It is thought to form either a homodimer or heterodimer. Autoantibodies against this protein have been found in patients with cancer or graft versus host disease.
centromere protein F
, centromere autoantigen F
, leucine, glutamic acid, lysine family 1 protein
, LEK/centromere protein
, AH antigen
, CENP-F kinetochore protein
, cell-cycle-dependent 350K nuclear protein
, centromere protein F, 350/400kDa (mitosin)
, centromere protein F, 350/400ka (mitosin)
, kinetochore protein CENPF
, cardiac muscle factor 1 CMF1