Phospho-Histone H1.3 (Thr18) Antibody - #DF2946
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# DF2946, RRID:AB_2840930.
展开/折叠
H1 histone family member 4; H1.4; H14_HUMAN; H1E; H1F4; Hist1h1e; Histone 1 H1e; Histone cluster 1 H1e; Histone H1; Histone H1.4; Histone H1B; MGC116819; H1 histone family member 3; H1.3; H13_HUMAN; H1F3; HIST1 H1D; HIST1H1D; Histone 1 H1d; Histone cluster 1 H1d; Histone H1.3; Histone H1c; MGC138176;
抗原和靶标
A synthesized peptide derived from human Histone H1.3 around the phosphorylation site of T18.
- P10412 H14_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK
- P16402 H13_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK
翻译修饰 - P10412/P16402 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
T4 | Phosphorylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K17 | Ubiquitination | Uniprot | |
T18 | Phosphorylation | P24941 (CDK2) , P06493 (CDK1) | Uniprot |
K21 | Ubiquitination | Uniprot | |
K26 | Acetylation | Uniprot | |
K26 | Methylation | Uniprot | |
S27 | Phosphorylation | Q96GD4 (AURKB) | Uniprot |
K32 | Acetylation | Uniprot | |
K34 | Acetylation | Uniprot | |
K34 | Methylation | Uniprot | |
K34 | Ubiquitination | Uniprot | |
S36 | Phosphorylation | P17612 (PRKACA) | Uniprot |
S41 | Phosphorylation | Uniprot | |
T45 | Phosphorylation | Uniprot | |
K46 | Acetylation | Uniprot | |
K46 | Ubiquitination | Uniprot | |
S51 | Phosphorylation | Uniprot | |
K52 | Acetylation | Uniprot | |
K52 | Ubiquitination | Uniprot | |
R54 | Methylation | Uniprot | |
S55 | Phosphorylation | Uniprot | |
S58 | Phosphorylation | Uniprot | |
K63 | Acetylation | Uniprot | |
K63 | Ubiquitination | Uniprot | |
K64 | Methylation | Uniprot | |
K64 | Sumoylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
Y71 | Phosphorylation | Uniprot | |
K75 | Acetylation | Uniprot | |
K75 | Methylation | Uniprot | |
K75 | Ubiquitination | Uniprot | |
S78 | Phosphorylation | Uniprot | |
K85 | Acetylation | Uniprot | |
K85 | Ubiquitination | Uniprot | |
S86 | Phosphorylation | Uniprot | |
S89 | Phosphorylation | Uniprot | |
K90 | Acetylation | Uniprot | |
K90 | Ubiquitination | Uniprot | |
T92 | Phosphorylation | Uniprot | |
K97 | Methylation | Uniprot | |
K97 | Ubiquitination | Uniprot | |
T99 | Phosphorylation | Uniprot | |
S102 | Phosphorylation | Uniprot | |
S104 | Phosphorylation | Uniprot | |
K106 | Acetylation | Uniprot | |
K106 | Methylation | Uniprot | |
K106 | Ubiquitination | Uniprot | |
K109 | Ubiquitination | Uniprot | |
K110 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
K119 | Methylation | Uniprot | |
K119 | Ubiquitination | Uniprot | |
K121 | Methylation | Uniprot | |
K129 | Acetylation | Uniprot | |
K129 | Methylation | Uniprot | |
K130 | Acetylation | Uniprot | |
K136 | Acetylation | Uniprot | |
K136 | Ubiquitination | Uniprot | |
K137 | Acetylation | Uniprot | |
K137 | Ubiquitination | Uniprot | |
K140 | Ubiquitination | Uniprot | |
T142 | Phosphorylation | Uniprot | |
T146 | Phosphorylation | Uniprot | |
K148 | Acetylation | Uniprot | |
K148 | Methylation | Uniprot | |
K148 | Ubiquitination | Uniprot | |
T154 | Phosphorylation | Uniprot | |
K159 | Methylation | Uniprot | |
K159 | Ubiquitination | Uniprot | |
K160 | Acetylation | Uniprot | |
K160 | Ubiquitination | Uniprot | |
K168 | Acetylation | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K169 | Acetylation | Uniprot | |
K171 | Methylation | Uniprot | |
S172 | Phosphorylation | Uniprot | |
K177 | Methylation | Uniprot | |
S187 | Phosphorylation | Uniprot | |
K192 | Methylation | Uniprot | |
K195 | Ubiquitination | Uniprot | |
K197 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
T4 | Phosphorylation | Uniprot | |
T10 | Phosphorylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K17 | Ubiquitination | Uniprot | |
T18 | Phosphorylation | Uniprot | |
K33 | Acetylation | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Methylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
S42 | Phosphorylation | Uniprot | |
T46 | Phosphorylation | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
S52 | Phosphorylation | Uniprot | |
K53 | Acetylation | Uniprot | |
K53 | Ubiquitination | Uniprot | |
R55 | Methylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S59 | Phosphorylation | Uniprot | |
K64 | Acetylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
K65 | Methylation | Uniprot | |
K65 | Sumoylation | Uniprot | |
K65 | Ubiquitination | Uniprot | |
Y72 | Phosphorylation | Uniprot | |
K76 | Acetylation | Uniprot | |
K76 | Ubiquitination | Uniprot | |
S79 | Phosphorylation | Uniprot | |
K86 | Acetylation | Uniprot | |
K86 | Ubiquitination | Uniprot | |
S87 | Phosphorylation | Uniprot | |
S90 | Phosphorylation | Uniprot | |
K91 | Acetylation | Uniprot | |
K91 | Ubiquitination | Uniprot | |
T93 | Phosphorylation | Uniprot | |
K98 | Methylation | Uniprot | |
K98 | Ubiquitination | Uniprot | |
T100 | Phosphorylation | Uniprot | |
S103 | Phosphorylation | Uniprot | |
S105 | Phosphorylation | Uniprot | |
K107 | Acetylation | Uniprot | |
K107 | Methylation | Uniprot | |
K107 | Ubiquitination | Uniprot | |
K110 | Ubiquitination | Uniprot | |
K111 | Ubiquitination | Uniprot | |
K118 | Ubiquitination | Uniprot | |
K141 | Ubiquitination | Uniprot | |
T147 | Phosphorylation | Uniprot | |
K149 | Ubiquitination | Uniprot | |
S151 | Phosphorylation | Uniprot | |
T155 | Phosphorylation | Uniprot | |
K160 | Ubiquitination | Uniprot | |
K161 | Ubiquitination | Uniprot | |
T164 | Phosphorylation | Uniprot | |
K169 | Acetylation | Uniprot | |
K170 | Acetylation | Uniprot | |
K173 | Acetylation | Uniprot | |
K176 | Acetylation | Uniprot | |
K179 | Ubiquitination | Uniprot | |
T180 | Phosphorylation | Uniprot | |
K188 | Acetylation | Uniprot | |
S189 | Phosphorylation | Uniprot | |
K207 | Acetylation | Uniprot | |
K209 | Acetylation | Uniprot | |
K212 | Acetylation | Uniprot |
研究背景
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
ADP-ribosylated on Ser-150 in response to DNA damage.
Nucleus. Chromosome.
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
The C-terminal domain is required for high-affinity binding to chromatin.
Belongs to the histone H1/H5 family.
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
Nucleus. Chromosome.
Note: According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin.
The C-terminal domain is required for high-affinity binding to chromatin.
Belongs to the histone H1/H5 family.
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