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AB108960

重组Anti-SUPT16H抗体[EPR3685]

Anti-SUPT16H antibody [EPR3685]

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(2 Publications)

Rabbit Recombinant Monoclonal SUPT16H antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications.

查看别名

FACT140, FACTP140, SUPT16H, FACT complex subunit SPT16, Chromatin-specific transcription elongation factor 140 kDa subunit, FACT 140 kDa subunit, FACTp140, Facilitates chromatin transcription complex subunit SPT16, hSPT16

1 Images
Western blot - Anti-SUPT16H antibody [EPR3685] (AB108960)
  • WB

Unknown

Western blot - Anti-SUPT16H antibody [EPR3685] (AB108960)

All lanes:

Western blot - Anti-SUPT16H antibody [EPR3685] (ab108960) at 1/1000 dilution

Lane 1:

HeLa cell lysate at 10 µg

Lane 2:

Jurkat cell lysate at 10 µg

Lane 3:

A549 cell lysate at 10 µg

Predicted band size: 120 kDa

false

关键信息

宿主种属

Rabbit

克隆

Monoclonal

克隆号

EPR3685

亚型

IgG

不含载体蛋白

No

反应种属

Human

应用

WB

applications

免疫原

The exact immunogen used to generate this antibody is proprietary information.

反应性数据

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产品详情

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Species reactivity
Rat: We have preliminary internal testing data to indicate this antibody may not react with this species.
Please contact us for more information.

性能和储存信息

形式
Liquid
纯化工艺
Affinity purification Protein A
存储溶液
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.31% Sodium citrate, 0.175% Sodium chloride, 0.05% BSA, 0.0172% EDTA
运输条件
Blue Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
储存信息
Stable for 12 months at -20°C

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

SUPT16H also known as FACT80 is a protein that plays an important mechanical role in chromatin remodeling. It has a molecular mass of approximately 142 kDa. This protein becomes substantially expressed in actively dividing cells particularly in tissues with high rates of cell proliferation such as the bone marrow and epithelial layers. SUPT16H along with SSRP1 forms a heterodimeric structure that functions as the Facilitates Chromatin Transcription (FACT) complex which modulates nucleosome organization during transcription elongation.
Biological function summary

The SUPT16H protein operates by working within the FACT complex to unravel nucleosomes allowing RNA polymerase II to move along DNA more efficiently by transiently modifying chromatin structure. This function is essential during the transcriptional elongation process making it pivotal in gene expression regulation. The protein as part of the FACT complex participates in chromatin destabilization and reassembly proving important in maintaining chromatin integrity during cell cycle progression and other cellular stress responses.

Pathways

SUPT16H plays a role in the transcriptional regulation pathway. It is strongly linked to pathways like the p53 signaling pathway which responds to DNA damage and maintains genomic stability. Within these pathways SUPT16H interacts with proteins such as RNA polymerase II highlighting its role in transcriptional regulation. In direct relation to this function SUPT16H also connects with p53-related proteins modulating their transcriptional activity in response to cellular changes.

The SUPT16H protein has demonstrated involvement in various cancer types due to its role in gene expression regulation. Aberrations in its function can lead to dysregulated transcription contributing to oncogenic transformations. Furthermore SUPT16H ties into neurodegenerative disorders such as Alzheimer's disease where altered chromatin dynamics may impact neuronal survival. In these contexts SUPT16H associates with cancer-related proteins and those involved in neuronal signaling pathways highlighting its importance in disease pathogenesis.

产品实验方案

For this product, it's our understanding that no specific protocols are required. You can visit:

靶点信息

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II).
See full target information SUPT16H

文献 (2)

Recent publications for all applications. Explore the full list and refine your search

Journal of orthopaedic translation 53:187-205 PubMed40678612

2025

PPARγ controls ESCRT-dependent fibroblast-like synoviocyte exosome biogenesis and alleviates chondrocyte osteoarthritis mediated by exosomal ANXA1.

Applications

Unspecified application

Species

Unspecified reactive species

Shuangshuo Jia,Yue Yang,Jiabao Liu,Ziyuan Wang,Lunhao Bai

Cell 185:3232-3247.e18 PubMed35952671

2022

Epigenetic reader SP140 loss of function drives Crohn's disease due to uncontrolled macrophage topoisomerases.

Applications

Unspecified application

Species

Unspecified reactive species

Hajera Amatullah,Isabella Fraschilla,Sreehaas Digumarthi,Julie Huang,Fatemeh Adiliaghdam,Gracia Bonilla,Lai Ping Wong,Marie-Eve Rivard,Claudine Beauchamp,Virginie Mercier,Philippe Goyette,Ruslan I Sadreyev,Robert M Anthony,John D Rioux,Kate L Jeffrey
View all publications

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