HMGCL Human, Sf9

3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant, Sf9

Recombinant human HMGCL, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It consists of 305 amino acids (residues 28-325), resulting in a molecular mass of 32.5 kDa. However, on SDS-PAGE, the apparent molecular size ranges from 28 to 40 kDa. This discrepancy is attributed to glycosylation. The recombinant HMGCL protein is engineered with a 6-amino acid His tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6963
Source

Sf9, Baculovirus cells.

Appearance
Clear, colorless, and sterile-filtered solution.

NANA E.Coli

N-Acetylneuraminate Lyase E.Coli Recombinant

Produced in E. coli, NANA is a single, non-glycosylated polypeptide chain consisting of 317 amino acids, with the first 297 amino acids forming the NANA protein. With a molecular weight of 34.7kDa, it includes a 20 amino acid His-tag fused at the N-terminus. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7205
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

NPL Human

N-acetylneuraminate Pyruvate Lyase Human Recombinant

Produced in E. coli, our NAL is a single, non-glycosylated polypeptide chain consisting of 340 amino acids (specifically, amino acids 1 to 320). With a molecular weight of 37.3 kDa, our NAL is fused to a 20 amino acid His-tag at the N-terminus and undergoes rigorous purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7289
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ADSL Human

Adenylosuccinate Lyase Human Recombinant

Recombinantly produced in E. coli, ADSL Human is a single, non-glycosylated polypeptide chain. It comprises 520 amino acids, with amino acids 1-484 corresponding to the ADSL protein, and has a molecular weight of 59 kDa. A 36 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6515
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ASL Human

Argininosuccinate Lyase Human Recombinant

Recombinant human ASL, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 484 amino acids (amino acids 1-464) with a molecular weight of 53.8 kDa. It includes a 20-amino acid His-tag fused at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6599
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CCBL1 Human

Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant

CCBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-422 a.a) and having a molecular mass of 50.3kDa. CCBL1 is fused to a 23 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6681
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CTH Human

Cystathionase Human Recombinant

Recombinant human CTH, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 425 amino acids (residues 1-405). It has a molecular weight of 46.7 kDa. This CTH protein includes a 20 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6777
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

HMGCL Human

3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant

Recombinant human HMGCL, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 323 amino acids (residues 28-325) with a molecular weight of 34.2 kDa. This protein is expressed with a 25 amino acid His-tag fused at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6856
Source
Escherichia Coli.
Appearance
Sterile, colorless, and filtered solution.

SRR Human

Serine Racemase Human Recombinant

Recombinant human SRR, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 364 amino acids (residues 1-340) with a molecular weight of 39.1 kDa. The protein is fused to a 24-amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7357
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

Lyases are a class of enzymes that catalyze the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure . They are classified under the EC number classification as EC 4 and can be further divided into several subclasses based on the type of bond they cleave:

  • EC 4.1: Carbon-carbon lyases (e.g., decarboxylases)
  • EC 4.2: Carbon-oxygen lyases (e.g., dehydratases)
  • EC 4.3: Carbon-nitrogen lyases
  • EC 4.4: Carbon-sulfur lyases
  • EC 4.5: Carbon-halide lyases
  • EC 4.6: Phosphorus-oxygen lyases (e.g., adenylyl cyclase)
  • EC 4.99: Other lyases .
Biological Properties

Lyases exhibit diverse biological properties, including specific expression patterns and tissue distribution. For instance, alginate lyases are found in various organisms such as algae, marine mollusks, and bacteria . These enzymes play crucial roles in the degradation of alginate, a polysaccharide found in the cell walls of brown algae . The expression of lyases can be tissue-specific, and their activity can be influenced by environmental factors and developmental stages .

Biological Functions

The primary biological functions of lyases include the catalysis of bond cleavage in various biochemical pathways. For example, phenylalanine ammonia lyase (PAL) is involved in the phenylpropanoid pathway, which is essential for the production of secondary metabolites like flavonoids and lignin . Lyases also play roles in immune responses and pathogen recognition. For instance, alginate lyases can degrade the alginate produced by pathogenic bacteria, aiding in the host’s defense mechanisms .

Modes of Action

Lyases operate through mechanisms that involve the breaking of chemical bonds without the addition of water or transfer of electrons. For example, pectate lyases cleave the α-1,4-glycosidic bond of pectin molecules through a β-elimination reaction, producing pectin oligosaccharides . These enzymes often have specific binding partners and can initiate downstream signaling cascades that regulate various cellular processes .

Regulatory Mechanisms

The expression and activity of lyases are tightly regulated through various mechanisms. Transcriptional regulation involves the binding of transcription factors to promoter regions of lyase genes, as seen with phenylalanine ammonia lyase (PAL) in plants . Post-translational modifications, such as phosphorylation, can also modulate the activity of lyases, ensuring their proper function in response to cellular signals .

Applications

Lyases have significant applications in biomedical research, diagnostics, and therapeutic strategies. Alginate lyases, for instance, are used in the production of biofuels and biochemicals from alginate . They also have potential applications in tissue engineering and wound healing due to their ability to degrade alginate-based biofilms . In diagnostics, lyases can be used as biomarkers for certain diseases, and their inhibitors can serve as therapeutic agents .

Role in the Life Cycle

Throughout the life cycle, lyases play essential roles in development, aging, and disease. For example, isocitrate lyase (ICL) is crucial for plant salt tolerance and is highly expressed during stress conditions . In humans, lyases are involved in metabolic pathways that are critical for growth and development. Dysregulation of lyase activity can lead to various diseases, highlighting their importance in maintaining cellular homeostasis .

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