Key Specifications Table
|Species Reactivity||Key Applications|
|Vrt||WB, ChIP-seq, ChIP|
|Format||Protein G Purified|
|Presentation||Anti-monomethyl-Histone H3 (Lys9) (mouse monoclonal IgG2aқ, clone CMA306). One vial containing 50 μg of protein G purified antibody in 50 μL PBS containing 0.05% sodium azide. Store at -20°C.
Normal Mouse IgG. Two vials containing 25 μg purified Mouse IgG in 25 μL storage buffer containing 0.1% sodium azide. Store at -20°C.
ChIP Primers GAPDH Coding region. One vial containing 75 μL of 5 μM of each primer specific for a region of the human GAPDH coding region. Store at -20°C.
FOR: GGC TCC CAC CTT TCT CAT CC
REV: GGC CAT CCA CAG TCT TCT GG
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at -20°C from date of receipt. Aliquot upon thawing, avoid freeze thaw cycles.|
|Material Size||25 assays|
|Material Package||25 assays per kit, ~2μg per chromatin immunoprecipitation|
ChIPAb+ Monomethyl-Histone H3 (Lys9) - ChIP Validated Antibody and Primer Set SDS
ChIPAb+ Monomethyl-Histone H3 (Lys9) - ChIP Validated Antibody and Primer Set Certificates of Analysis
|Reference overview||Pub Med ID|
|Prdm16 is required for the maintenance of brown adipocyte identity and function in adult mice.|
Harms, MJ; Ishibashi, J; Wang, W; Lim, HW; Goyama, S; Sato, T; Kurokawa, M; Won, KJ; Seale, P
Cell metabolism 19 593-604 2014
Prdm16 is a transcription factor that regulates the thermogenic gene program in brown and beige adipocytes. However, whether Prdm16 is required for the development or physiological function of brown adipose tissue (BAT) in vivo has been unclear. By analyzing mice that selectively lacked Prdm16 in the brown adipose lineage, we found that Prdm16 was dispensable for embryonic BAT development. However, Prdm16 was required in young mice to suppress the expression of white-fat-selective genes in BAT through recruitment of the histone methyltransferase Ehmt1. Additionally, Prdm16 deficiency caused a severe adult-onset decline in the thermogenic character of interscapular BAT. This resulted in BAT dysfunction and cold sensitivity but did not predispose the animals to obesity. Interestingly, the loss of brown fat identity due to ablation of Prdm16 was accelerated by concurrent deletion of the closely related Prdm3 gene. Together, these results show that Prdm16 and Prdm3 control postnatal BAT identity and function.
|The histone H3 methyltransferase G9A epigenetically activates the serine-glycine synthesis pathway to sustain cancer cell survival and proliferation.|
Ding, J; Li, T; Wang, X; Zhao, E; Choi, JH; Yang, L; Zha, Y; Dong, Z; Huang, S; Asara, JM; Cui, H; Ding, HF
Cell metabolism 18 896-907 2013
Increased activation of the serine-glycine biosynthetic pathway is an integral part of cancer metabolism that drives macromolecule synthesis needed for cell proliferation. Whether this pathway is under epigenetic control is unknown. Here we show that the histone H3 lysine 9 (H3K9) methyltransferase G9A is required for maintaining the pathway enzyme genes in an active state marked by H3K9 monomethylation and for the transcriptional activation of this pathway in response to serine deprivation. G9A inactivation depletes serine and its downstream metabolites, triggering cell death with autophagy in cancer cell lines of different tissue origins. Higher G9A expression, which is observed in various cancers and is associated with greater mortality in cancer patients, increases serine production and enhances the proliferation and tumorigenicity of cancer cells. These findings identify a G9A-dependent epigenetic program in the control of cancer metabolism, providing a rationale for G9A inhibition as a therapeutic strategy for cancer.
|Advance your Epigenetics Research (MilliporeSigma)|