Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

DDIT3 Human

DNA Damage Inducible Transcript 3 Human Recombinant

DDIT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids and having a molecular mass of 21 kDa. The DDIT3 protein is fused to a 20 amino acids His tag at N-terminus.
The DDIT3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30613
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

DDIT4 Human

DNA Damage Inducible Transcript 4 Recombinant Human

DDIT4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-232.a.a) and having a molecular mass of 27.5kDa.
DDIT4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30647
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

GADD45A Human

Growth Arrest and DNA-Damage-Inducible Alpha Human Recombinant

GADD45A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-165 a.a.) and having a molecular mass of 19.4kDa. GADD45A is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30676
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GADD45B Human

Growth Arrest and DNA-Damage-Inducible Beta Human Recombinant

GADD45B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 17.8 kDa.
Shipped with Ice Packs
Cat. No.
BT30722
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GADD45G Human

Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant

GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.
Shipped with Ice Packs
Cat. No.
BT30766
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GADD45GIP1 Human

Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.
GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30790
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

PDRG1 Human

p53 and DNA-Damage Regulated 1 Human Recombinant

PDRG1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (1-133 a.a.) and having a molecular mass of 17.6kDa. The PDRG1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30811
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

DNA-damage proteins are a diverse group of proteins involved in the detection, signaling, and repair of DNA damage. These proteins play a crucial role in maintaining genomic integrity by recognizing and repairing various types of DNA damage, such as single-strand breaks, double-strand breaks, and base modifications . They can be classified into several categories based on their functions, including DNA repair proteins, damage sensors, transducers, and effectors .

Biological Properties

Key Biological Properties: DNA-damage proteins exhibit specific properties that enable them to recognize and repair damaged DNA. These properties include DNA-binding domains, enzymatic activities, and the ability to interact with other proteins involved in the DNA damage response .

Expression Patterns: The expression of DNA-damage proteins varies across different tissues and cell types. Some proteins, such as p53, are ubiquitously expressed, while others, like DDB2, show tissue-specific expression patterns .

Tissue Distribution: DNA-damage proteins are distributed throughout the body, with higher expression levels in tissues with high cell turnover rates, such as the skin, gastrointestinal tract, and bone marrow .

Biological Functions

Primary Biological Functions: The primary function of DNA-damage proteins is to detect and repair DNA damage. They achieve this by recognizing damaged DNA, recruiting other repair proteins, and facilitating the repair process .

Role in Immune Responses: DNA-damage proteins also play a role in immune responses by recognizing pathogen-induced DNA damage and activating immune signaling pathways .

Pathogen Recognition: Some DNA-damage proteins, such as the MRN complex, can recognize and respond to DNA damage caused by viral infections, thereby contributing to the host’s defense against pathogens .

Modes of Action

Mechanisms with Other Molecules and Cells: DNA-damage proteins interact with various molecules and cells to coordinate the DNA damage response. For example, the ATM kinase phosphorylates several downstream targets, including p53, to initiate cell cycle arrest and DNA repair .

Binding Partners: DNA-damage proteins often form complexes with other proteins to enhance their function. For instance, the MRN complex (Mre11-Rad50-Nbs1) acts as a sensor for double-strand breaks and recruits other repair proteins to the damage site .

Downstream Signaling Cascades: Upon detecting DNA damage, DNA-damage proteins activate downstream signaling cascades that regulate cell cycle progression, DNA repair, and apoptosis .

Regulatory Mechanisms

Transcriptional Regulation: The expression of DNA-damage proteins is tightly regulated at the transcriptional level by various transcription factors, such as p53 and NF-κB .

Post-Translational Modifications: DNA-damage proteins undergo post-translational modifications, such as phosphorylation, ubiquitination, and sumoylation, which modulate their activity and stability .

Applications

Biomedical Research: DNA-damage proteins are extensively studied in biomedical research to understand the mechanisms of DNA repair and their implications in diseases such as cancer .

Diagnostic Tools: DNA-damage proteins serve as biomarkers for diagnosing and monitoring various diseases, including cancer and neurodegenerative disorders .

Therapeutic Strategies: Targeting DNA-damage proteins has therapeutic potential in treating diseases characterized by defective DNA repair, such as cancer. For example, PARP inhibitors are used to treat BRCA-mutated cancers by exploiting the synthetic lethality between PARP inhibition and BRCA deficiency .

Role in the Life Cycle

Development: DNA-damage proteins are essential for normal development by ensuring the integrity of the genome during cell division and differentiation .

Aging: Accumulation of DNA damage over time contributes to aging and age-related diseases. DNA-damage proteins play a role in mitigating the effects of DNA damage and maintaining cellular function during aging .

Disease: Defects in DNA-damage proteins can lead to various diseases, including cancer, neurodegenerative disorders, and immunodeficiency syndromes .

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