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Product List
GCLM Human
Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant
GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.
GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT4779
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
HERC5 Human
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant
HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT4906
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
SIAH1 Human
Siah E3 Ubiquitin Protein Ligase 1 Human Recombinant
SIAH1 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (90-282) and having a molecular mass of 24.1 kDa.
SIAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SIAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
T4 DNA
T4 DNA Ligase Recombinant
T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5' -phosphate and 3' -hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA, RNA or DNA/RNA hybrids.
Shipped with Ice Packs
Cat. No.
BT5080
Source
Escherichia Colilambda lysogen NM 989.
Appearance
Sterile filtered liquid formulation having a concentration of 167,000 U/ml.
Introduction
Definition and Classification
Ligases are a class of enzymes that catalyze the joining of two molecules by forming a new chemical bond, typically with the hydrolysis of a small pendant chemical group on one of the molecules . They are essential in various biological processes, including DNA replication and repair. Ligases are classified under the EC 6 category in the Enzyme Commission number classification and can be further divided into six subclasses based on the type of bond they form:
Biological Properties
Ligases exhibit several key biological properties:
- Expression Patterns: Ligases are expressed in various tissues and cells, with specific types being more prevalent in certain tissues. For example, DNA ligases are ubiquitously expressed due to their critical role in DNA replication and repair .
- Tissue Distribution: The distribution of ligases varies depending on their specific function. DNA ligases are found in all cells, while other ligases, such as ubiquitin ligases, may have more specialized distributions .
Biological Functions
Ligases play crucial roles in numerous biological functions:
- Primary Functions: They are primarily involved in the joining of DNA fragments during replication and repair. DNA ligase, for instance, seals nicks in the DNA backbone by forming phosphodiester bonds .
- Role in Immune Responses and Pathogen Recognition: Certain ligases, such as ubiquitin ligases, are involved in the regulation of immune responses and the recognition of pathogens. They help in tagging proteins for degradation, which is essential for the regulation of immune signaling pathways .
Modes of Action
The mechanisms by which ligases operate involve several steps:
- Binding Partners: Ligases interact with various molecules and cells to perform their functions. For example, DNA ligase binds to the 3’ hydroxyl end of one nucleotide and the 5’ phosphate end of another to form a phosphodiester bond .
- Downstream Signaling Cascades: Ligases can initiate downstream signaling cascades by modifying target proteins. Ubiquitin ligases, for instance, tag proteins with ubiquitin, marking them for degradation by the proteasome .
Regulatory Mechanisms
The expression and activity of ligases are tightly regulated:
- Transcriptional Regulation: The transcription of ligase genes is controlled by various transcription factors that respond to cellular signals .
- Post-Translational Modifications: Ligases themselves can be modified post-translationally, which can affect their activity and stability. For example, phosphorylation can activate or inhibit ligase activity .
Applications
Ligases have several important applications in biomedical research and medicine:
- Biomedical Research: Ligases are used extensively in genetic engineering and molecular biology for cloning and manipulating DNA .
- Diagnostic Tools: Ligase-based assays are used for detecting genetic mutations and variations .
- Therapeutic Strategies: Ligases are targets for drug development, particularly in cancer therapy, where inhibitors of specific ligases can be used to disrupt cancer cell proliferation .
Role in the Life Cycle
Ligases play vital roles throughout the life cycle of an organism:
- Development: During development, ligases are involved in DNA replication and repair, ensuring the integrity of the genome .
- Aging and Disease: As organisms age, the efficiency of ligase activity can decline, leading to an accumulation of DNA damage. This can contribute to aging and the development of age-related diseases .
