Epiproteomic Histone Modification Panel B

Epiproteomic Histone Modification Panel B

The Epiproteomic Histone Modification Panel (EHMP) provides rapid, low-cost profiling of histone modification states within a sample.  While not providing the depth and localization of ChIPSeq analysis, the EHMP allows researchers to generate hypotheses for future study.  At present, these 95 modification states are assayed.  (More will be added in the near future).

Sample requirements for histone assay:

1.) Cells Requirement: 1 - 5million

2.) Tissue Requirements: 25 - 100mg


H1.4: K25UN H1.4: K25AC H1.4: K25ME1 H1.4: K25ME2 H1.4: K25ME3 H2A: K5UN H2A: K5AC H2A: K9UN H2A: K9AC
H2A: K36UN H2A: K36AC H2A1: K13UN H2A1: K13AC H2A1: K15UN H2A1: K15AC* H2A1: K15UB* H2A3: K13UN H2A3: K13AC
H2A3: K15UN H2A3: K15AC H2A3: K15UB* H3R2UN: K4UN H3R2UN: K4AC H3R2UN: K4ME1 H3R2UN: K4ME2 H3R2UN: K4ME3 H3R2UN: Q5UN
H3R2UN: Q5ME1 H3: K9UN H3: K9AC H3: K9ME1 H3: K9ME2 H3: K9ME3 H3: K14UN H3: K14AC H3: K18UN
H3: K18AC H3: K18ME1 H3: Q19UN H3: Q19ME1 H3: K23UN H3: K23AC H3: K23ME1 H3: R42UN H3: R42ME2*
H3: R49UN H3: R49ME2* H3: Q55UN H3: Q55ME1* H3: K56UN H3: K56AC H3: K64UN H3: K64AC H3: K79UN
H3: K79AC H3: K79ME1 H3: K79ME2 H3: K79ME3 H3: K122UN H3: K122AC H3.1: K27UN H3.1: K27AC H3.1: K27ME1
H3.1: K27ME2 H3.1: K27ME3 H3.1: K36UN H3.1: K36AC H3.1: K36ME1 H3.1: K36ME2 H3.1: K36ME3 H3.3: K27UN H3.3: K27AC
H3.3: K27M* H3.3: K27ME1 H3.3: K27ME2 H3.3: K27ME3 H3.3: K36UN H3.3: K36AC H3.3: K36ME1 H3.3: K36ME2 H3.3: K36ME3
H4: K5UN H4: K5AC H4: K8UN H4: K8AC H4: K12UN H4: K12AC H4: K16UN H4: K16AC H4: K20UN
H4: K20AC H4: K20ME1 H4: K20ME2 H4: K20ME3

* Modification Available upon Request

ac=Acetylated, me=Methylated, ub=Ubiquitylated, number refers to the degree of modification. H3K9me3 indicated the trimethylation of lysine 9 of H3. Unmodified peptides are also included.

Related Publications

LaFave LM, Béguelin W, Koche R, Teater M, Spitzer B, Chramiec A, Papalexi E, Keller MD, Hricik T, Konstantinoff K, Micol JB, Durham B, Knutson SK, Campbell JE, Blum G, Shi X, Doud EH, Krivtsov AV, Chung YR, Khodos I, de Stanchina E, Ouerfelli O, Adusumilli PS, Thomas PM, Kelleher NL, Luo M, Keilhack H, Abdel-Wahab O, Melnick A, Armstrong SA, Levine RL "Loss of BAP1 function leads to EZH2-dependent transformation." Nat Med, 2015, 21(11) p. 1344-9.
Summary | Full Text (PMC) | Full Text (DOI)

Zheng Y, Sweet SM, Popovic R, Martinez-Garcia E, Tipton JD, Thomas PM, Licht JD, Kelleher NL "Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3." Proc Natl Acad Sci U S A, 2012, 109(34) p. 13549-54.
Summary | Full Text (PMC) | Full Text (DOI)

Zheng Y, Thomas PM, Kelleher NL "Measurement of acetylation turnover at distinct lysines in human histones identifies long-lived acetylation sites." Nat Commun, 2013, 4() p. 2203.
Summary | Full Text (PMC) | Full Text (DOI)


  • Northwestern/CBC: $420
    LCC: $378
    External Academic/Nonprofit: $630
    External For-Profit Industry: $1050