RNF4 Antibody (C-term) #abs102702

abs102702-50ul

In Stock

228

Description

A Rabbit Polyclonal Antibody (Pab) that has been purified based on its affinity for a specific peptide.

Other names

RNF4, also known as E3 ubiquitin-protein ligase RNF4 or Small nuclear ring finger protein (SNURF), is a protein that plays a vital role in controlling the protein degradation process. Its main function is to attach a small protein called ubiquitin to other proteins, marking them for destruction by the cell's proteasome.
The protein RNF4 is a member of the RING finger protein family and has a molecular weight of 632. It is commonly found in human cells and is essential for maintaining proper protein levels within the cell. RNF4 is a potent regulator of transcription and DNA replication, and it also plays a role in the repair of damaged DNA.
In addition to its role in protein degradation, RNF4 has been implicated in numerous cellular processes, including gene expression, cell cycle regulation, and DNA damage response. Interestingly, the protein has been shown to interact with a wide range of cellular components, including other proteins, RNA molecules, and DNA.
Overall, RNF4 is a key player in maintaining the proper functioning of human cells. It is involved in numerous biological processes and is essential for maintaining the stability of important cellular components. Understanding the precise mechanisms by which RNF4 functions will be critical for the development of new therapies for human diseases.

Source

Rabbit

Specificity

The RNF4 antibody being offered is derived from rabbits that were first immunized with a synthetic peptide conjugated with KLH. This peptide spans from amino acids 95-123 within the C-terminal region of the human RNF4 protein. To create content that is highly similar to the original information, rearrange the text accordingly.

Species Reactivity

Human

Application

FC~~1:25
WB~~1:1000

Properties

Clonality

Polyclonal Antibody

Isotype

Rabbit Ig

Stability & Storage

Store at 2-8°C for a maximum of 2 weeks to maintain refrigeration. For extended storage, it is recommended to freeze the samples at -20°C in smaller portions to avoid freeze-thaw cycles.

Storage buffer

This purified polyclonal antibody is provided in phosphate-buffered saline (PBS) containing 0.09% (w/v) sodium azide. The purification process involves passing the antibody through a protein A column, followed by affinity purification using peptides.

Research area

Crown Antibodies

Target

Background

This protein, known as an E3 ubiquitin-protein ligase, is responsible for binding polysumoylated chains that are covalently attached to various proteins. Through this binding, it can facilitate the polyubiquitination of these substrates, leading to their targeting for degradation by the proteasome. One of the proteins regulated by this ligase is PML, as well as the transcriptional activator PEA3.
In addition to these functions, the E3 ligase also plays a role in regulating chromosome alignment and spindle assembly, particularly through its influence on the kinetochore CENPH-CENPI-CENPK complex. By targeting polysumoylated CENPI for proteasomal degradation, the ligase helps to ensure proper function of this complex.
The protein can also regulate cellular responses to hypoxia and heat shock, through its degradation of EPAS1 and PARP1, respectively. There is some evidence to suggest that this E3 ligase may also directly bind DNA or nucleosomes, allowing it to play a more direct role in transcriptional regulation. Overall, this ligase is a critical component of a complex network of cellular processes that help to regulate protein degradation and other important cellular functions.

Celluar localization

Cytoplasm. Nucleus. Nucleus, PML body. Nucleus, nucleoplasm

UniPort

P78317

References

References

Hu, X.V., et al. Proc. Natl. Acad. Sci. U.S.A. 107(34):15087-15092(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Salonen, J., et al. Mol. Cell. Endocrinol. 307 (1-2), 205-210 (2009) :
Percherancier, Y., et al. J. Biol. Chem. 284(24):16595-16608(2009)
Tatham, M.H., et al. Nat. Cell Biol. 10(5):538-546(2008)