TIPIN Human

TIMELESS Interacting Protein Human Recombinant
Cat. No.
BT24928
Source
Escherichia Coli.
Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.
TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

The protein TIPIN belongs to the CSM3 family. It plays a crucial role in the progression of the S-phase during cell division and is vital for cell survival when DNA damage or replication stress occurs. TIPIN is particularly important for the ATR-CHEK1 pathway, which is part of the replication checkpoint activated by ultraviolet light.

Description
Recombinant human TIPIN, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 324 amino acids (residues 1-301). It has a molecular weight of 36.9kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The TIPIN solution is provided at a concentration of 0.5mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeatedly freezing and thawing the solution.
Purity
SDS-PAGE analysis indicates a purity greater than 85.0%.
Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

Product Science Overview

Discovery and Structure

The TIMELESS protein was initially identified as a mammalian homologue of the Drosophila circadian clock protein TIM. It was later discovered to be a core component of the replisome, a large protein assembly responsible for DNA replication . The crystal structure of the N-terminal domain of human TIMELESS, spanning amino acids 1–463, revealed a partial binding site for TIPIN .

Function and Mechanism

The TIMELESS-TIPIN complex is essential for maintaining the integrity of the replication fork during DNA synthesis. It helps in stabilizing the replication fork and preventing its collapse under stress conditions . This complex is also involved in the DNA damage checkpoint during the S-phase, ensuring that any damage is repaired before the cell cycle progresses .

Role in Genomic Stability

The TIMELESS-TIPIN complex plays a vital role in preserving genomic integrity. It is recruited to replication origin regions and dissociates as replication proceeds. Depletion of this complex can lead to chromosome fragmentation and defects in damage repair, highlighting its importance in maintaining replication fork stability . Additionally, the complex is required for sister chromatid cohesion, which is crucial for accurate chromosome segregation during cell division .

Clinical Relevance

Defects in the TIMELESS-TIPIN complex can lead to genetic instability, predisposing individuals to various genetic disorders. Understanding the structure and function of this complex can provide insights into potential therapeutic targets for diseases related to genomic instability .

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