Recombinant Human Histone H1.3(HIST1H1D) CSB-EP010379HUd8
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(Histone H1c)(Histone H1s-2)
Species: (Organism)
Homo sapiens (Human)
Gene Names:
HIST1H1D
Tag info:
N-terminal MBP-tagged and C-terminal 6xHis-tagged
Target Protein AA Sequence:
SETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK
Expression Region:
2-221aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
66.0 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Epigenetics and Nuclear Signaling
Function:
Involvement in disease:
Relevance:
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d." Ohe Y., Hayashi H., Iwai K. J. Biochem. 106:844-857(1989)
