THYN1 Human

Thymocyte Nuclear Protein 1 Human Recombinant
Cat. No.
BT24253
Source
Escherichia Coli.
Synonyms
MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

THYN1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-225a.a.) and having a molecular mass of 27.8kDa.
THYN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
THYN1 is a highly conserved protein found in vertebrates and plants. It plays a role in apoptosis induction. Studies have shown that THYN1 is primarily localized in the nucleus of cells, including thymocytes and lymphoma cells. This nuclear localization is observed regardless of the cell cycle stage.
Description
This recombinant THYN1 protein is produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 245 amino acids (amino acids 1-225) with a molecular weight of 27.8 kDa. The protein includes a 20 amino acid His-tag at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The THYN1 protein is supplied at a concentration of 0.5 mg/ml in a buffer solution containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 100 mM NaCl, and 20% glycerol.
Purity
The purity of the THYN1 protein is greater than 95% as determined by SDS-PAGE analysis.
Stability
For short-term storage (2-4 weeks), the protein can be stored at 4°C. For long-term storage, it is recommended to store the protein frozen at -20°C. Repeated freeze-thaw cycles should be avoided.
Synonyms
MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS

Product Science Overview

Structure and Expression

THYN1 is a nuclear protein, meaning it is primarily localized within the nucleus of cells. It is expressed in thymocytes, which are immature T cells found in the thymus. The protein is present in the nucleus irrespective of the cell cycle stage, whether the cell is in a resting or active phase .

The recombinant form of THYN1, often used in research, is typically produced in Escherichia coli (E. coli) and purified using conventional chromatography techniques. This recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification and detection .

Function

THYN1 plays a significant role in the regulation of apoptosis, a process of programmed cell death that is crucial for maintaining cellular homeostasis and development. The protein specifically binds to 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of this epigenetic mark .

Clinical Relevance

Mutations or dysregulation of the THYN1 gene have been associated with various diseases. For instance, THYN1 has been linked to optic atrophy 8 and preterm premature rupture of the membranes . Understanding the function and regulation of THYN1 can provide insights into these conditions and potentially lead to the development of therapeutic strategies.

Research Applications

Recombinant THYN1 is widely used in research to study its function and role in apoptosis. It is also used to investigate the mechanisms of thymocyte development and the regulation of gene expression in the thymus. The availability of recombinant THYN1 allows researchers to conduct detailed biochemical and structural analyses, which are essential for understanding its function at a molecular level .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.