Epiproteomic Histone Modification Panel

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 92 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*	H2A3: K13UN	H2A3: K13AC	H2A3: K15UN
H2A3: K15AC	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, UN=Unmodified, and the 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)

Pricing

https://proteomics.northwestern.edu/services/rates/

Instruments Used

Thermo Scientific TSQ Altis Triple Quadrupole Mass Spectrometer