Phospho-HDAC4 (Ser 246) + HDAC5 (Ser 259) + HDAC7 (Ser 155) Rabbit mAb

Catalog No.: F3397

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使用情報

Dilution
WB1:1000 IP1:30

Application
WB, IP

Source
Rabbit

Reactivity
Human, Mouse, Rat

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
124 kDa, 140 kDa 124 kDa, 140 kDa
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

Specificity
Phospho-HDAC4 (Ser 246) + HDAC5 (Ser 259) + HDAC7 (Ser 155) Rabbit mAb recognizes endogenous levels of total HDAC4 phosphorylated at Ser 246, HDAC5 phosphorylated at Ser 259, and HDAC7 phosphorylated at Ser 155.

Clone
J21N6

Background
Phospho-HDAC4 (Ser 246) + HDAC5 (Ser 259) + HDAC7 (Ser 155) are key phosphorylation sites on class IIa histone deacetylases (HDACs), which regulate gene expression by modulating chromatin structure through histone deacetylation. Phosphorylation at these serine residues is a critical mechanism controlling the subcellular localization and activity of these HDACs. Upon phosphorylation, these sites bind to 14-3-3 proteins, sequestering the HDACs in the cytoplasm and preventing their nuclear entry and transcriptional repression activity. HDAC4 phosphorylation at Ser 246, mediated by kinases like CaMKII and PKD, regulates muscle differentiation and neuronal function. Similarly, HDAC5 phosphorylation at Ser 259, also mediated by CaMKII, influences cardiac hypertrophy. HDAC7 phosphorylation at Ser 155, primarily by PKD, affects immune system regulation and vascular biology. These phosphorylation events integrate cellular signalling with epigenetic regulation, ensuring dynamic control of gene expression during development, differentiation, and stress responses. Dysregulation of these processes is linked to diseases such as cancer, neurodegenerative disorders, and cardiovascular conditions.

Background

Phospho-HDAC4 (Ser 246) + HDAC5 (Ser 259) + HDAC7 (Ser 155) are key phosphorylation sites on class IIa histone deacetylases (HDACs), which regulate gene expression by modulating chromatin structure through histone deacetylation. Phosphorylation at these serine residues is a critical mechanism controlling the subcellular localization and activity of these HDACs. Upon phosphorylation, these sites bind to 14-3-3 proteins, sequestering the HDACs in the cytoplasm and preventing their nuclear entry and transcriptional repression activity. HDAC4 phosphorylation at Ser 246, mediated by kinases like CaMKII and PKD, regulates muscle differentiation and neuronal function. Similarly, HDAC5 phosphorylation at Ser 259, also mediated by CaMKII, influences cardiac hypertrophy. HDAC7 phosphorylation at Ser 155, primarily by PKD, affects immune system regulation and vascular biology. These phosphorylation events integrate cellular signalling with epigenetic regulation, ensuring dynamic control of gene expression during development, differentiation, and stress responses. Dysregulation of these processes is linked to diseases such as cancer, neurodegenerative disorders, and cardiovascular conditions.

References
[1] Di Giorgio E, et al. Epigenomics. 2016 Feb;8(2):251-69.

PVDFメンブレン孔径参考表

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%