GCLM Human

Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

Recombinant human GCLM, produced in E. coli, is a single polypeptide chain consisting of 298 amino acids (residues 1-274) with a molecular weight of 33.3kDa. This protein includes a 24 amino acid His-tag fused to the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4779
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

HERC5 Human

HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant

Recombinantly produced in E. coli, HERC5 Human is a single, non-glycosylated polypeptide chain consisting of 367 amino acids (specifically, residues 681-1024). Its molecular weight is 43kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of the HERC5 protein.
Shipped with Ice Packs
Cat. No.
BT4906
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.

SIAH1 Human

Siah E3 Ubiquitin Protein Ligase 1 Human Recombinant

Recombinant SIAH1 protein for human use is produced in E. coli. It is a single polypeptide chain with a molecular weight of 24.1 kDa, comprised of 216 amino acids (residues 90-282). This SIAH1 protein is fused to a 23 amino acid His-tag located at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5011
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

T4 DNA

T4 DNA Ligase Recombinant

T4 DNA Ligase is an enzyme that facilitates the creation of a phosphodiester bond between the 5' phosphate and 3' hydroxyl termini of adjacent DNA or RNA strands. It can join both blunt and cohesive ends, and repair single-strand nicks in duplex DNA, RNA, or DNA/RNA hybrids.
Shipped with Ice Packs
Cat. No.
BT5080
Source
Escherichia Colilambda lysogen NM 989.
Appearance
A liquid solution, sterilized by filtration, with a concentration of 167,000 units per milliliter.
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:

  • EC 6.1: Ligases forming carbon-oxygen bonds
  • EC 6.2: Ligases forming carbon-sulfur bonds
  • EC 6.3: Ligases forming carbon-nitrogen bonds
  • EC 6.4: Ligases forming carbon-carbon bonds
  • EC 6.5: Ligases forming phosphoric ester bonds
  • EC 6.6: Ligases forming nitrogen-metal bonds .
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 .
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