Reacts with recombinant Human H1.1, not with other Human H1 isoforms or core histones.
Does not react with histone H1 acid extracted from cell-lines such as breast cancer cell line T47D, because H1.1 is not expressed in this cell line. H1.1 is not expressed in many cell lines, as has been previously reported (Meergans et al, 1997)
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Detects a band of approximately 30 kDa (predicted molecular weight: 21.7 kDa). Human H1.1 is not present in many human cell lines. Cross reacts with a band of approx. 52kDa and 40kDa in nuclear extracts of T47D cell line.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. The C-terminal region also shows the most differences in aa sequence between the H1 histone variants H1.0/1/2/3/4/5.
Johann DJ et al. Approaching solid tumor heterogeneity on a cellular basis by tissue proteomics using laser capture microdissection and biological mass spectrometry. J Proteome Res8:2310-8 (2009).
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Happel N et al. H1 histone subtype constitution and phosphorylation state of the ageing cell system of human peripheral blood lymphocytes. Exp Gerontol43:184-99 (2008).
Read more (PubMed: 18234461) »