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 48 modification states are assayed.  (More will be added in the near future).

 

H3K4Un H3K14Un H3.1/2K27me2 H3.3K27me1 H3R42Un H3K122Un H2A.3K13Un H1.4K25ac H4K20me1
H3K4me1 H3K14ac H3.1/2K27me3 H3.3K27me2 H3R42me2 H3K122ac H2A.3K13ac H4K5Un H4K20me2
H3K4me2 H3K18Un H3.1/2K27ac H3.3K27me3 H3K56Un H2AK5Un H2A.3K15Un H4K5ac H4K20me3
H3K4me3 H3K18me1 H3.1/2K36Un H3.3K27ac H3K56me1 H2AK5ac H2A.3K15ub H4K8Un H4K20ac
H3K4ac H3K18ac H3.1/2K36me1 H3.3K27M H3K56ac H2AK9Un H2AK36Un H4K8ac
H3K9Un H3K23Un H3.1/2K36me1 H3.3K36Un H3K79Un H2AK9ac H2AK36ac H4K12Un
H3K9me1 H3K23me1 H3.1/2K36me2 H3.3K36me1 H3K79me1 H2A.1K13Un H1.4K25Un H4K12ac
H3K9me2 H3K23ac H3.1/2K36me3 H3.3K36me2 H3K79me2 H2A.1K13ac H1.4K25me1 H4K16Un
H3K9me3 H3.1/2K27Un H3.1/2K36ac H3.3K36me3 H3K79me3 H2A.1K15Un H1.4K25me2 H4K16ac
H3K9ac H3.1/2K27me1 H3.3K27Un H3.3K36ac H3K79ac H2A.1K15ub H1.4K25me3 H4K20Un

*ac=Acetylated, me=Methylated, ub=Ubiquitylated, number reders 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

  • Northwestern/CBC: $400 (per biological replicate)
    External Academic/Nonprofit: $600
    External For-Profit Industry: $1000

Instruments Used

TSQ Quantum Ultra

Protocols

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