HDHD1 Human

Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant

Recombinant human HDHD1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This non-glycosylated polypeptide chain contains 248 amino acids (residues 1-228) and has a molecular weight of 27.4 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28371
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

HDHD2 Human

Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 Human Recombinant

When produced in E.Coli, HDHD2 is a single, non-glycosylated polypeptide chain comprised of 279 amino acids (specifically, amino acids 1 through 259). It has a molecular weight of 30.6kDa. This HDHD2 protein is engineered with a 20 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28485
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

HDHD3 Human

Haloacid Dehalogenase-Like Hydrolase Domain Containing 3 Human Recombinant

Recombinant human HDHD3, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 287 amino acids, including a 36 amino acid His tag at the N-terminus (1-251 a.a. of the HDHD3 sequence), and has a molecular weight of 32.2 kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28570
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PAFAH2 Human

Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant

Recombinant human PAFAH2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 415 amino acids (amino acids 1-392). It has a molecular weight of 46.4 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28866
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ABHD10 Human

Abhydrolase Domain Containing 10 Human Recombinant

Recombinant human ABHD10 protein, expressed in E. coli, is a single polypeptide chain with a molecular weight of 30.9 kDa. It encompasses amino acids 53-306 and includes a 25 amino acid His-tag fused to the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26399
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

ABHD14B Human

Abhydrolase Domain Containing 14B Human Recombinant

Recombinant human ABHD14B, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 234 amino acids (residues 1-210) with a molecular weight of 25.0 kDa. It includes an N-terminal 24-amino acid His-tag and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT26461
Source
E.coli.
Appearance
Sterile, colorless solution, free from particulate matter.

ACY1 Human

Aminoacylase-1 Human Recombinant

Recombinant human ACY1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 428 amino acids (specifically, amino acids 1 to 408). With a molecular weight of 48 kDa, it features a 20 amino acid His-Tag fused at its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26540
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

ACY1 Mouse

AminoAcylase-1 Mouse Recombinant

This product consists of the recombinant mouse ACY1 protein, which was expressed in E. coli and purified to a high degree. The protein is a single, non-glycosylated polypeptide chain encompassing amino acids 1 to 408 of the ACY1 sequence. A 25-amino acid His-tag is attached to the N-terminus to facilitate purification. The molecular weight of the recombinant protein is 48.4 kDa.
Shipped with Ice Packs
Cat. No.
BT26638
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

FOLH1 Human

Folate Hydrolase 1 Human Recombinant

This version of FOLH1 is produced in insect cells. It is a single chain of 717 building blocks called amino acids, with a molecular weight of 80.7kDa. It includes a 6 amino acid His tag for purification purposes. The protein has been purified using specialized techniques.

Shipped with Ice Packs
Cat. No.
BT27801
Source

Sf9, Baculovirus cells.

Appearance
A clear and sterile liquid.

FOLH1 Mouse

Folate Hydrolase 1 Mouse Recombinant

Recombinant Mouse FOLH1, produced in Sf9 Baculovirus cells, is a single, non-glycosylated polypeptide chain comprising 717 amino acids (45-752a.a). It has a molecular mass of 80.5 kDa and exhibits a migration pattern of 70-100 kDa on SDS-PAGE under reducing conditions. The protein includes a C-terminal 6-amino acid His-tag and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27878
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

Hydrolases are a class of enzymes that catalyze the hydrolysis of chemical bonds. These enzymes are essential for various biological processes, as they facilitate the breakdown of complex molecules into simpler ones by adding water. Hydrolases are classified based on the type of bond they act upon:

  • Esterases: Hydrolyze ester bonds.
  • Glycosidases: Hydrolyze glycosidic bonds in carbohydrates.
  • Peptidases: Hydrolyze peptide bonds in proteins.
  • Lipases: Hydrolyze lipid molecules.
  • Phosphatases: Hydrolyze phosphate esters.
Biological Properties

Key Biological Properties: Hydrolases exhibit high specificity for their substrates and operate under mild physiological conditions. They are often regulated by factors such as pH, temperature, and the presence of cofactors or inhibitors.

Expression Patterns: The expression of hydrolases varies widely among different organisms and tissues. Some hydrolases are constitutively expressed, while others are inducible in response to specific stimuli.

Tissue Distribution: Hydrolases are distributed throughout various tissues in the body. For example, digestive hydrolases like amylase and lipase are predominantly found in the pancreas and salivary glands, while lysosomal hydrolases are present in almost all cell types.

Biological Functions

Primary Biological Functions: Hydrolases play crucial roles in metabolism, digestion, and cellular maintenance. They are involved in the degradation of macromolecules, recycling of cellular components, and energy production.

Role in Immune Responses: Certain hydrolases, such as lysozyme, are involved in the immune response by breaking down the cell walls of pathogens, thereby aiding in pathogen recognition and destruction.

Pathogen Recognition: Hydrolases can recognize and degrade pathogen-associated molecular patterns (PAMPs), which are essential for the innate immune response.

Modes of Action

Mechanisms with Other Molecules and Cells: Hydrolases interact with various molecules and cells to exert their effects. For instance, digestive hydrolases break down dietary macromolecules into absorbable units.

Binding Partners: Hydrolases often require specific binding partners or cofactors to function effectively. For example, many hydrolases require metal ions like zinc or magnesium for catalytic activity.

Downstream Signaling Cascades: The activity of hydrolases can trigger downstream signaling cascades that regulate various cellular processes. For example, the hydrolysis of phosphoinositides by phospholipase C generates second messengers that modulate cellular signaling pathways.

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of hydrolases are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.

Transcriptional Regulation: The transcription of hydrolase genes can be regulated by various transcription factors in response to environmental cues or cellular signals.

Post-Translational Modifications: Hydrolases can undergo post-translational modifications such as phosphorylation, glycosylation, and ubiquitination, which can alter their activity, stability, and localization.

Applications

Biomedical Research: Hydrolases are widely used in biomedical research to study metabolic pathways, disease mechanisms, and cellular processes.

Diagnostic Tools: Hydrolases serve as biomarkers for various diseases. For example, elevated levels of certain hydrolases in the blood can indicate liver or pancreatic disorders.

Therapeutic Strategies: Hydrolases are employed in therapeutic strategies, such as enzyme replacement therapy for lysosomal storage diseases and the use of proteases in wound debridement.

Role in the Life Cycle

Role Throughout the Life Cycle: Hydrolases play vital roles throughout the life cycle, from development to aging and disease. During development, hydrolases are involved in tissue remodeling and differentiation. In adulthood, they maintain cellular homeostasis and metabolic balance. In aging and disease, dysregulation of hydrolase activity can contribute to pathological conditions such as neurodegeneration and cancer.

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