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ITEM#: 3042-051242S
MFR#: 05-1242-S
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pair
| Product Name | Description | Item# | QTY | |
|---|---|---|---|---|
Anti-trimethyl-Histone H3 (Lys9) Antibody, clone 6F12-H4
|
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pair | 3042-051242 | EA | |
Anti-Trimethyl Histone H3(Lys9) Antibody, clone CMA308
|
Histone H3 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, H3 is involved with the structure of the nucleosomes of the 'beads on a strin | 3042-051250 | EA | |
Anti-Dimethyl Histone H3 (Lys9) Antibody, clone CMA307, Trial Size
|
Histone H3 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, H3 is involved with the structure of the nucleosomes of the 'beads on a strin | 3042-051249S | EA | |
Anti-trimethyl Histone H3 (Lys27) Antibody, clone 18E9.1, Trial Size
|
Histone H3 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, H3 is involved with the structure of the nucleosomes of the 'beads on a strin | 3042-051951S | EA | |
Anti-Trimethyl Histone H3 (Lys4) Antibody, clone CMA304, Trial Size
|
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pair | 3042-051339S | EA |