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Histones H1 are necessary for the condensation of nucleosome chains into higher order structures.
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Data suggest that Nap1 readily dissociates histone 1 (H1) from DNA and stoichiometrically binds H1 from nucleosomes, supporting a hypothesis whereby histone chaperones contribute to regulation of H1 profile in chromatin.
Thus, our results indicate that linker histone H1 plays an important role in the structure and function of vertebrate chromosomes in mitosis.
H1.X moves more rapidly than other linker histones in vivo Domain swapping between H1.0 and H1.X suggests that the globular domain (GD) and C-terminal domain (CTD) of H1.X independently contribute to the dynamic behavior of H1.X.
this study shows that dynamic epigenetic states defined by the linker histone H1.0 determine which cells within a tumor can sustain the long-term cancer growth.
The N-terminal domain contributes toward the differential chromatin binding affinity, whereas the C-terminal domain contributes toward distinct nucleosomal interface of isotypes H10 and H1c (zeige HIST1H1C Antikörper).
H1(0)histone may be an important factor in normal DC differentiation. Tumor-derived factors may inhibit DC differentiation by affecting H1(0) expression.
Marked reduction in total H1 levels causes significant reduction in both expression and the level of active histone mark H3K4me3 at many Hox (zeige MSH2 Antikörper) genes.
both P-TEFb (zeige CCNT1 Antikörper) activity and H1 phosphorylation are necessary for the full differentiation of C2C12 myoblasts into myotubes.
Histone H1 poly[ADP]-ribosylation of proteins over a specific time course is required for the changes in synaptic plasticity related to memory stabilization in mice.
H1 dephosphorylation and H2A.X (zeige H2AFX Antikörper) hyperphosphorylation are necessary steps on the apoptotic pathway.
Analysis of DNA-induced secondary structure of the carboxyl-terminal domain of histone H1 subtypes H1(0)(C-H1(0)) and H1t (zeige HIST1H1T Antikörper) (C-H1t (zeige HIST1H1T Antikörper)).
H1 isoforms H1.0, H1.1, and H1.2 are non-responsive to hormone whereas prolonged dexamethasone treatment effectively dephosphorylated the H1.3, H1.4, and H1.5 isoforms
Histones H1 are necessary for the condensation of nucleosome chains into higher order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division (By similarity).
, histone H1.0
, histone H5
, H1 histone family, member 0
, Histone H1-0
, histone H1'
, H1.0, H1(0), H1-0
, H1-0 histone
, histone H1(0)-1
, histone H1.0-A
, histone H5B
, H1 histone
, histone H1