THAP11 Human

THAP Domain Containing, Apoptosis Associated Protein 11 Human Recombinant

Cat. No.

BT11811

Source

Escherichia Coli.

Synonyms

THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 80% as determined by SDS-PAGE.

Usage

THE BioTek's 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.

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Description

THAP11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.8kDa.
THAP11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

THAP Domain Containing, Apoptosis Associated Protein 11 (THAP11), a member of the thanatos-associated protein family, functions as a transcriptional repressor. It interacts with HCF1 via a coiled coil domain. THAP11, found in both the nucleus and cytoplasm, contributes to embryogenesis and embryonic stem cell pluripotency by recruiting epigenetic modifiers.

Description

Recombinant Human THAP11, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 337 amino acids (residues 1-314). It has a molecular weight of 36.8 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.

Physical Appearance

Clear, colorless solution, sterile-filtered.

Formulation

The THAP11 solution is provided at a concentration of 0.5 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.

Stability

For short-term storage (up to 2-4 weeks), store at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.

Purity

Purity is determined to be greater than 80% by SDS-PAGE analysis.

Synonyms

THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMPGFTCC VPGCYNNSHR DKALHFYTFP KDAELRRLWL KNVSRAGVSG CFSTFQPTTG HRLCSVHFQG GRKTYTVRVP TIFPLRGVNE RKVARRPAGA AAARRRQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQSSPSA STAQTAQLQP NLVSASAAVL LTLQATVDSS QAPGSVQPAP ITPTGEDVKP IDLTVQVEFA AAEGAAAAAA ASELQAATAG LEAAECPMGP QLVVVGEEGF PDTGSDHSYS LSSGTTEEEL LRKLNEQRDI LALMEVKMKE MKGSIRHLRL TEAKLREELR EKDRLLAMAV IRKKHGM.

Product Science Overview

Structure and Function

The THAP domain is a putative DNA-binding domain (DBD) that likely also binds a zinc ion. It features a conserved C2CH architecture. The THAP11 protein functions as a transcriptional repressor and plays a crucial role in embryogenesis and the pluripotency of embryonic stem (ES) cells. It acts as a sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers.

Biological Significance

THAP11 is involved in various important cellular processes, including epigenetic regulation, maintenance of pluripotency, and transposition. It has been implicated in several disorders, such as methylmalonic aciduria and homocystinuria, Cblj type, and homocystinuria caused by cystathionine beta-synthase deficiency. Additionally, THAP11 has been linked to various cancers.

Research and Applications

The human THAP protein family consists of twelve members of different lengths, and THAP11, along with THAP7, has been characterized as a transcription factor. The identification of a predicted oligomerization region in the human THAP protein family opens new directions to investigate the members of this protein family.

In research, recombinant THAP11 protein is used to study its role in transcriptional repression and its involvement in various cellular processes and diseases. Understanding the function and regulation of THAP11 can provide insights into its potential as a therapeutic target for diseases associated with its dysfunction.

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THAP11 Human

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