| H4

Histone H4 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H4 is involved with the structure of the nucleosome of the 'beads on a string' organization. Histone proteins are highly post-translationally modified. Covalently bonded modifications include acetylation and methylation of the N-terminal tails. These modifications may alter expression of genes located on DNA associated with its parent histone octamer.[1][2] Histone H4 is an important protein in the structure and function of chromatin, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.
 

| Typical data

As the OD values of the standard curve may vary according to the conditions of the actual assay performance (e.g. operator, pipetting technique, wash technique or temperature effects), the operator should establish a standard curve for each test. Typical standard curve and data are provided below for reference only.

 

Concentration (ng/mL)	10	5	2.5	1.25	0.625	0.312	0.156	0
OD	2.33	1.41	0.78	0.49	0.32	0.25	0.2	0.09
Corrected OD	2.24	1.32	0.69	0.4	0.23	0.16	0.11	-

 

| Repeatability

Intra-assay Precision (Precision within an assay)：CV% < 10%; Inter-assay Precision (Precision between assays)：CV% < 10%
 

| Recovery

The recovery of Mouse H4 spiked at three different levels in samples throughout the range of the assay was evaluated in various matrices.

 

Sample Type	Range(%)	Average Recovery(%)
Tissue Homogenates(n=8)	84-101	96
Cell Lysates(n=8)	92-104	101
Cell Culture Supernates(n=8)	96-108	105

 

| Linearity

Samples were spiked with high concentrations of Mouse H4 and diluted with Universal Diluent to produce samples with values within the range of the assay.

 

		Tissue Homogenates(n=4)	Cell Lysates(n=4)	Cell Culture Supernates(n=4)
1 : 2	Range (%)	84-95	87-96	90-111
	Average (%)	91	92	96
1 : 4	Range (%)	89-103	87-108	105-115
	Average (%)	94	98	108