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Merck ChIPAb+ Dimethyl-Histone H4 (Arg3) Symmetric - ChIP Validated Antibody and Primer Set
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Merck ChIPAb+ Dimethyl-Histone H4 (Arg3) Symmetric - ChIP Validated Antibody and Primer Set

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ChIP 검증 완료된 항체 및 프라이머 세트로, rabbit 소스의 polyclonal 항체를 사용합니다. Histone H4의 대칭성 이메틸화(Arg3)를 인식하며, mouse, human, rat에서 반응합니다. ChIP, dot blot, western blot에 적합하고 dry ice로 배송됩니다.

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Merck Sigma
판매단위
pk
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마지막 업데이트 2026. 01. 28. 오후 05:39
Merck 17-10250 ChIPAb+ Dimethyl-Histone H4 (Arg3) Symmetric - ChIP Validated Antibody and Primer Set, 25 ASSAYS pk판매 단위 pk ·
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Merck Sigma · Merck ChIPAb+ Dimethyl-Histone H4 (Arg3) Symmetric - ChIP Validated Antibody and Primer Set

ChIPAb+ Dimethyl-Histone H4 (Arg3) Symmetric - ChIP Validated Antibody and Primer Set

생물학적 소스

rabbit

품질 등급

100 (M-Clarity Program)

클론

polyclonal

정제법

affinity chromatography

Species Reactivity

mouse, human, rat

제조사 / 상품명

ChIPAb+
Upstate®

적용 기술

  • ChIP: suitable
  • dot blot: suitable
  • western blot: suitable

NCBI 수납 번호

NP_001029249

UniProt 수납 번호

P62805

배송 상태

dry ice


Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin.
The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each).
Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm.
These modifications—acetylation, phosphorylation, methylation, and ubiquitination—occur predominantly on the N-terminal and C-terminal tails extending beyond the nucleosome core particle.

Arginine modifications of histone proteins are mediated by two classes of protein arginine methyltransferases (PRMTs), class I and II.

  • Class I PRMTs place two methyl groups on one nitrogen atom of the arginine guanidino group, resulting in asymmetric modification.
  • Class II PRMTs place two methyl groups on two nitrogen atoms of the guanidino group, producing symmetric dimethylation.

Although exceptions exist, asymmetric modifications are typically associated with transcription activation, while symmetric modifications are most commonly linked to transcriptional repression.

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