DescriptionThe high-mobility group (HMG) proteins 14 and 17 are abundant chromosomal proteins that bind to nucleosomes and enhance transcription. HMG-14 and HMG-17 also function as architectural elements, which alter the structure of the chromatin fiber and enhance transcription from chromatin templates. HMG-14/17 proteins modify the nucleosomal organization of the 30 nm chromatin fiber and mediate the unfolding of the higher order chromatin structure thereby facilitating access to the underlying DNA sequence. Clustering of architectural elements, such as HMG proteins and linker histone subtypes into distinct domains, may lead to structural and functional heterogeneity along the chromatin fiber. In addition, HMG-14 and HMG-17 have been identified as constitutive components of mouse oocyte and embryonic chromatin that establish a link between the structure of embryonic chromatin and the normal progression of embryonic development.
|Immunoprecipitation, Western Blot|
|This HMGN1 antibody was raised against a peptide within the C-terminal region of human HMGN1.|
|-20°C, Avoid Freeze/Thaw Cycles|
|70mM tris with 0.07mM EDTA, 105mM NaCl, 30% glycerol, 31mM glycine and 0.035% sodium azide; pH 8|
|BOS_1365; FLJ27265; FLJ31471; high mobility group nucleosomal binding domain 1; high mobility group nucleosome binding domain 1; High mobility group nucleosome-binding domain-containing protein 1; high mobility group protein 14; high-mobility group (nonhistone chromosomal) protein 14; high-mobility group nucleosome binding 1; high-mobility group nucleosome binding domain 1; high-mobility group nucleosome-binding domain-containing protein 1; HMG 14; Hmg14; Hmg-14; HMGN 1; HMGN1; MGC104230; MGC117425; Non-histone chromosomal protein HMG-14; nonhistone chromosomal protein HMG-14|
|Antigen affinity chromatography|
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