Western Blot: Complement C4b/d Antibody (16D2) [NB200-541] - Western blot analysis of C4 expression in J774.A1 (A) aand mouse PBL (B) whole cell lysates.
WB: non-reduced sample treatment and SDS-PAGE was used. IHC-F: Tissue sections were fixed in ice-cold acetone and blocked with 2% BSA, FCS and PBS. Although not confirmed this antibody may be useful in Immunoassays.
Publications
Read Publications using NB200-541 in the following applications:
Alternate Names for Complement C4b/d Antibody (16D2)
basic C4
Basic complement C4
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3
C4B1
C4B12
C4B2
C4B3
C4FMGC164979
CH
Chido form of C4
CO4C4B5
complement C4-B
complement C4B1a
complement component 4B (Chido blood group)
complement component 4B
CPAMD3FLJ60561
EC 2.1.1.144
EC 2.7.11
Background
In eukaryotic cells, DNA is associated with histones and other proteins to form chromatin. The cell division cycle constitutes a series of processes that have evolved to create two genetically identical daughter cells from a mother cell. One of these processes is the conversion of relatively amorphous, extended interphase chromatin into condensed, highly ordered mitotic chromosomes. Proper mitotic chromosome condensation is essential for the correct segregation of sister chromatids into two daughter cells. The basic unit of chromatin is the nucleosome core particle, which consists of 140 bp DNA wrapped around an octameric core containing two each of the four conserved core histones: H2A, H2B, H3 and H4. A fifth histone, the linker histone H1, interacts with DNA of variable length, linking adjacent nucleosome cores, and further compacting the chromatin. Chromatin changes are initiated during G2 phase of the cell cycle, in preparation for cell division. The most striking morphological change is chromatin condensation, which becomes apparent during prophase and is maximal during the subsequent stages of mitosis. Histone H1 and the N-terminal tail of H3 have key roles in the folding and inter-association of the chromatin fiber. Two currently known phosphorylation sites are present in the N-terminus of H3; serine-10 and serine-28.1,2 Mitogenic stimulation, oncogenic transformation, or induction of oncogenic ras expression are accompanied with increase in serine-10 phosphorylation of the H3 N-terminal domain. Indeed, it has been shown that phosphorylated H3 is associated with c-fos and c-myc genes in stimulated cells. Phosphorylation of H3, at both serine-10 and -28, coincides with the induction of mitotic chromosome condensation. H3 phosphorylation may contribute to proto-oncogene induction by modulating chromatin structure and releasing blocks in elongation. In contrast to H1 hyperphosphorylation, site-specific phosphorylation of core histone H3 at serine-10 and -28 appears to occur exclusively during mitosis in mammalian cells. H3 dephosphorylation occurs quite rapidly after mitosis and serine-10/28 remain unphosphorylated throughout the remainder of interphase. PP1 has been identified as the H3 phosphatase. Monoclonal antibodies reacting specifically with phosphorylated histone H3, are useful tools to study molecular mechanisms associated with the G2 to M transition and chromatin condensation, and for the analysis of protein kinase(s) and phosphatase(s) involved in H3 phosphorylation or dephosphorylation. They may also be used in multiparameter analysis to relate H3 phosphorylation in individual cells to the cell
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Ujic D Neurodevelopmental and Protein Analysis in the Maternal Immune Activation Mouse Model of Neurodevelopmental Disorders Thesis 2023-01-01 (WB, Mouse)
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