ID2 Human

Inhibitor of DNA Binding 2 Human Recombinant
Cat. No.
BT24305
Source
E.coli.
Synonyms
DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% 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.
Shipped with Ice Packs
In Stock

Description

ID2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17kDa. ID2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Inhibitor of DNA Binding 2 (ID2) is a member of the inhibitor of DNA binding family. These transcriptional regulators possess a helix-loop-helix (HLH) domain but lack a basic domain. ID family members utilize their HLH domains to suppress the heterodimerization of basic helix-loop-helix transcription factors, thereby negatively regulating their functions. ID2 plays a role in inhibiting cell differentiation and may suppress tissue-specific gene expression.
Description
Recombinant human ID2, expressed in E. coli, is a non-glycosylated polypeptide chain containing 154 amino acids (residues 1-134). The 17 kDa protein consists of ID2 with an N-terminal 20 amino acid His-tag. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The ID2 protein solution is provided at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined to be greater than 85% via SDS-PAGE analysis.
Synonyms
DNA-binding protein inhibitor ID-2, bHLHb26, GIG8, ID2A, ID2H, MGC26389, Class B basic helix-loop-helix protein 26, Inhibitor of DNA binding 2.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKAFSPVRSV RKNSLSDHSL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVS KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQNQASR TPLTTLNTDI SILSLQASEF PSELMSNDSK ALCG.

Product Science Overview

Structure and Function

Id2, like other ID proteins, lacks a DNA-binding domain but contains a helix-loop-helix (HLH) domain. This domain allows Id2 to form heterodimers with bHLH transcription factors, preventing them from binding to DNA and thus inhibiting their function . This mechanism is crucial in various biological processes, including cell cycle regulation, differentiation, and development.

Role in Cancer

Id2 has been implicated in the regulation of cancer stem cells (CSCs) in head and neck squamous cell carcinomas (HNSCCs). Research has shown that Id2 expression is higher in HNSCC cells with stemness characteristics compared to differentiated cells . Overexpression of Id2 enhances proliferation, self-renewal, and expression of stemness markers like CD44 in HNSCC cells. Conversely, silencing Id2 reduces these stemness traits, indicating its potential as a therapeutic target for cancer treatment .

Therapeutic Potential

Given its role in maintaining the stemness of cancer cells, Id2 is considered a promising target for cancer therapy. Targeting Id2 could potentially reduce the proliferation and chemoresistance of CSCs, improving treatment outcomes for patients with HNSCC .

Research and Applications

The study of Id2 extends beyond cancer research. Its role in negatively regulating cell differentiation makes it a significant protein in developmental biology and regenerative medicine. Researchers are exploring various methods to modulate Id2 activity, including the use of small-molecule inhibitors to disrupt its interaction with bHLH transcription factors .

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