List of products by brand PTM Bio

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Reference: PTM-315
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-316
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine, structurally similar to lysine acetylation, is a...
Reference: PTM-317
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysineis a newly identified reversible modification...
Reference: PTM-318
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-319
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-320
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Histones are subjected to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-322
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Histones are subjected to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-323
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-324
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-326
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-327
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Histones are subjected to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-329
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Butyrylation of lysine, structurally similar to lysine acetylation and lysine propionylation, is a newly identified reversible modification controlling protein activity. With integrated proteomic approaches and...
Reference: PTM-331
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Histones are subjected to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-333
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-334RM
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H3 is core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in...
Reference: PTM-335RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-336
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H3 is core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in...
Reference: PTM-337RM
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Butyrylation of lysine, structurally similar to lysine acetylation and lysine propionylation, is a newly identified reversible modification controlling protein activity. With integrated proteomic approaches and...
Reference: PTM-338RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine is a newly identified reversible modification...
Reference: PTM-401
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Succinylation is a post-translational modification that involves the addition of a succinyl group (-CO-CH2-CH2-CO2 h) is added to a lysine residue of a protein molecule. This modification is found in many proteins,...
Reference: PTM-402
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Lysine succinylation is an important reversible modification, and plays significant roles i nmany cellular processes. Systematical screening of lysine succinylated substrates in various cellular pathological and...
Reference: PTM-409
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Histones are subject to a variety of enzyme catalyzed modifications including acetylation, phosphorylation, ubiquitylation etc. Lysine succinylation is a recently identified novel protein post-translational...
Reference: PTM-412
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Succinylation is a post-translational modification where a succinyl group (-CO-CH2-CH2-COOH) is added to a lysine residue in proteins, including histones. This addition of succinyl group changes lysine's charge from...
Reference: PTM-413
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Histones are subject to a variety of enzyme catalyzed modifications including acetylation, phosphorylation, ubiquitylation etc. Lysine succinylation is a recently identified novel protein post-translational...
Reference: PTM-419
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Succinylation is a posttranslational modification where a succinyl group (-CO-CH2-CH2-CO2H) is added to a lysine residue of a protein molecule. This modification is found in many proteins, including histones. The...
Reference: PTM-421
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Histones are subject to a variety of enzyme catalyzed modifications including acetylation, phosphorylation, ubiquitylation etc. Lysine succinylation is a recently identified novel protein post-translational...
Reference: PTM-422
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Histones are subject to a variety of enzyme catalyzed modifications including acetylation, phosphorylation, ubiquitylation etc. Lysine succinylation is a recently identified novel protein post-translational...
Reference: PTM-501
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Lysine crotonylation is a newly-identified histone post-translational modification that has come to light through integrated proteomic approaches and elaborate biochemistry analyses. Lysine crotonylation has been...
Reference: PTM-502
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Lysine crotonylation is a newly-identified histone post-translational modification that has come to light through integrated proteomic approaches and elaborate biochemistry analyses. Lysine crotonylation has been...
Reference: PTM-503
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Lysine crotonylation is a newly-identified histone post-translational modification by integrated proteomic approaches and elaborate biochemistry analyses. It has been shown that lysine crotonylation is an...
Reference: PTM-505
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-508
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-508RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-509
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-512
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-514
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-515RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-516RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-517RM
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Lysine crotonylation is a newly-identified histone post-translational modification that has come to light through integrated proteomic approaches and elaborate biochemistry analyses. Lysine crotonylation has been...
Reference: PTM-519
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-521RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-522RM
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-523
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-524
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-527
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-528
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-530
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Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-533
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-534
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-535
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-535RM
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-536
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-536RM
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Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation,phosphorylation...
Reference: PTM-537
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-539
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-540
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-541
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-542
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-543
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-544RM
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-545RM
€0.00 (tax incl.)
Lysine crotonylation is a newly-identified histone post-translational modification that has come to light through integrated proteomic approaches and elaborate biochemistry analyses. Lysine crotonylation has been...
Reference: PTM-546RM
€0.00 (tax incl.)
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification...
Reference: PTM-601
€0.00 (tax incl.)
Histone post-translational modifications (PTMs), known as the “histone code”, are key mechanisms of epigenetics that modulate chromatin structures. The PTMs on histone including acetylation, methylation,...
Reference: PTM-602
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-605RM
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Histone post-translational modifications (PTMs) are a key mechanism in epigenetic regulation of chromatin structure and are known as the "histone code." Post-translational modifications on histones include...
Reference: PTM-606
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Histone post-translational modifications (PTMs), known as the “histone code”, are key mechanisms of epigenetics that modulate chromatin structures. The PTMs on histone including acetylation, methylation,...
Reference: PTM-606F
€0.00 (tax incl.)
Histone post-translational modifications (PTMs), known as the “histone code”, are key mechanisms of epigenetics that modulate chromatin structures. The PTMs on histone including acetylation, methylation,...
Reference: PTM-610
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-611
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-611RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-612
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-613
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-614
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-615RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation,phosphorylation...
Reference: PTM-616
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-617
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-617RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-618RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-619
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-619RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-620
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-620RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation,phosphorylation...
Reference: PTM-623
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-623RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-624
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-625
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-625RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-626
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-627
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-627RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-628
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-628RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-629
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-630
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-631
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-631RM
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-632
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...
Reference: PTM-633
€0.00 (tax incl.)
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation...

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