Recombinant Proteins

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Product List

ID1 Human

Inhibitor of DNA Binding 1 Human Recombinant

ID1 Human Recombinant produced in E. coli is a single polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 18.5kDa. ID1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24240
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

ID2 Human

Inhibitor of DNA Binding 2 Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT24305
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

Introduction

Definition and Classification

Inhibitor of DNA-binding (ID) proteins are a family of proteins that heterodimerize with basic helix-loop-helix (bHLH) transcription factors to inhibit DNA binding of bHLH proteins . ID proteins contain the HLH-dimerization domain but lack the basic DNA-binding domain, thus regulating bHLH transcription factors when they heterodimerize with them . There are four ID proteins in humans: ID1, ID2, ID3, and ID4 .

Biological Properties

Key Biological Properties: ID proteins are key regulators of development, preventing premature differentiation of stem cells . They promote cell cycle progression, delay senescence, and facilitate cell migration .

Expression Patterns: ID proteins are highly expressed in embryonic stem cells but not in differentiated adult cells . They are overexpressed in many types of cancer, such as pancreatic, breast, and prostate cancers .

Tissue Distribution: ID proteins are found in various tissues, including the brain, heart, and other organs .

Biological Functions

Primary Biological Functions: ID proteins regulate the timing of differentiation of stem cells during development by inhibiting the formation of E-protein dimers that promote differentiation . They also play a role in cell cycle progression and migration .

Role in Immune Responses and Pathogen Recognition: ID proteins are involved in the regulation of immune responses and pathogen recognition by modulating the activity of various transcription factors .

Modes of Action

Mechanisms with Other Molecules and Cells: ID proteins interact with bHLH transcription factors, preventing them from binding to DNA and thus inhibiting transcription . They also interact with other proteins, such as the retinoblastoma protein and paired-box transcription factors .

Binding Partners: ID proteins form heterodimers with bHLH transcription factors, such as E proteins, to inhibit their DNA-binding activity .

Downstream Signaling Cascades: By inhibiting bHLH transcription factors, ID proteins regulate various downstream signaling cascades involved in cell differentiation, proliferation, and migration .

Regulatory Mechanisms

Transcriptional Regulation: The expression of ID proteins is regulated by various transcription factors and signaling pathways .

Post-Translational Modifications: ID proteins undergo post-translational modifications, such as phosphorylation, which can affect their activity and interactions with other proteins .

Applications

Biomedical Research: ID proteins are studied for their role in development, cancer, and other diseases .

Diagnostic Tools: ID proteins can be used as biomarkers for certain types of cancer and other diseases .

Therapeutic Strategies: Targeting ID proteins may provide new therapeutic strategies for cancer and other diseases .

Role in the Life Cycle

Development: ID proteins are essential for normal development, regulating the timing of differentiation of stem cells .

Aging and Disease: Dysregulation of ID proteins can contribute to tumorigenesis and other diseases . They are involved in various stages of the life cycle, from development to aging and disease .

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