ID1 Human

Inhibitor of DNA Binding 1 Human Recombinant
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Description

Oncogenic Roles and Clinical Associations

ID1 is overexpressed in >20 cancer types and correlates with advanced disease stages :

Cancer TypeClinical ImpactMechanism
Breast Cancer60% of grade III tumors show strong ID1 expression Promotes metastasis via MT1-MMP upregulation
LeukemiaCritical target of BCR-ABL/FLT3-ITD kinases Sustains proliferation via p27 suppression
GlioblastomaAssociated with radiation resistance COX-2/PGE2 → MAPK/Egr1 → ID1 axis
Hepatocellular CarcinomaDrives chemoresistance Activates pentose phosphate pathway

Therapeutic Targeting Strategies

Recent advances in ID1 modulation demonstrate clinical potential:

ApproachEffectEvidence Source
Antisense oligonucleotidesReduced lung metastases by 67% in breast cancer models PNAS (2003)
Cannabidiol (CBD)Inhibits glioma stem cells via ID1/p-STAT3 axis PMC (2020)
CrizotinibSuppresses ID1 in ALK/MET+ lung cancers PMC (2020)
USP1 inhibitors (Pimozide)Reduces ID1 stability in AML PMC (2020)

Recombinant ID1 Protein Applications

The human recombinant ID1 protein (PRO-1426) enables functional studies :

ParameterSpecification
Expression SystemE. coli
Purity>85% (SDS-PAGE)
Formulation20mM Tris-HCl, 0.15M NaCl, 10% glycerol
Functional UseHLH interaction assays, angiogenesis studies

Controversies and Research Gaps

While ID1 generally promotes tumor progression, paradoxical roles emerge:

  • Enhances docetaxel sensitivity in prostate cancer

  • Predicts better outcomes in adjuvant NSCLC therapy

  • Required for BMP-mediated differentiation in some contexts

These dual functions underscore the need for context-specific therapeutic strategies. Current clinical trials focus on combinatorial approaches targeting ID1 with angiogenesis inhibitors or immune checkpoint modulators .

Product Specs

Introduction
Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein that forms heterodimers with basic helix-loop-helix (bHLH) transcription factors. Lacking DNA binding activity, ID1 inhibits the DNA binding and transcriptional activation of bHLH proteins it interacts with. ID1 plays a role in cell growth, senescence, and differentiation.
Description
Recombinant human ID1, expressed in E. coli, is a single polypeptide chain of 178 amino acids (residues 1-155) with a molecular weight of 18.5 kDa. The protein includes an N-terminal 23-amino acid His-tag and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The ID1 solution is provided at a concentration of 0.5 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze 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 greater than 85% as assessed by SDS-PAGE.
Synonyms
bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKVASGS TATAAAGPSC ALKAGKTASG AGEVVRCLSE QSVAISRCAG GAGARLPALL DEQQVNVLLY DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT PGGRGLPVRA PLSTLNGEIS ALTAEAACVP ADDRILCR.

Product Science Overview

Structure and Function

ID1 is composed of a basic helix-loop-helix (bHLH) domain, which is crucial for its interaction with other proteins. The protein’s primary function is to regulate cell growth, differentiation, and senescence. By inhibiting the DNA binding activity of other HLH proteins, ID1 plays a significant role in controlling gene expression and cellular processes .

Role in Disease and Therapeutic Potential

ID1 has been implicated in various diseases, particularly in cancer and inflammatory conditions. For instance, in rheumatoid arthritis (RA), ID1 is produced by synovial fibroblasts and endothelial cells, contributing to the inflammatory environment. The protein is released from fibroblasts via exosomes and can activate signaling pathways that promote angiogenesis, vasculogenesis, and fibrosis . This makes ID1 a potential target for therapeutic interventions aimed at modulating these processes in diseases like RA .

Recombinant Human ID1

Recombinant human ID1 is produced using techniques that involve the expression of the ID1 gene in bacterial systems such as E. coli. The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification. The purified protein is used in various research applications to study its function and role in different cellular processes .

The recombinant human ID1 protein is typically stored in a buffer containing Tris-HCl, NaCl, glycerol, and DTT to maintain its stability. It is important to avoid freeze-thaw cycles to preserve the protein’s integrity .

Applications in Research

Recombinant human ID1 is widely used in research to understand its role in cell growth, differentiation, and disease. It is utilized in various assays, including enzyme-linked immunosorbent assays (ELISA), Western blotting, and real-time polymerase chain reaction (RT-PCR), to study its expression and function in different cell types and conditions .

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