CA10 Human

Carbonic Anhydrase X Human Recombinant

Recombinant human CA10 is a glycosylated polypeptide chain consisting of 317 amino acids (residues 22-328). It has a molecular weight of 36.3 kDa, calculated based on its amino acid sequence. The protein includes a 6-amino acid His-tag at the C-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT28931
Source

HEK293 Cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

CA11 Human

Carbonic Anhydrase XI Human Recombinant

Recombinantly produced in E. coli, CA11 Human is a single, non-glycosylated polypeptide chain comprising 326 amino acids (residues 24-328), resulting in a molecular weight of 36.3 kDa. This protein is engineered with a 21 amino acid His-tag fused at its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29029
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

CA12 Human

Carbonic Anhydrase XII Human Recombinant

Recombinant human CA12, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. This protein consists of 283 amino acids (residues 25-301), resulting in a molecular weight of 31.94 kDa. On SDS-PAGE under reducing conditions, it migrates between 28-40 kDa. The recombinant CA12 protein is designed with a 6-amino acid His-tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29055
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

CA13 Human

Carbonic Anhydrase XIII Human Recombinant

Recombinant CA13 Human, produced in E. coli, is a single, non-glycosylated polypeptide chain. It contains 285 amino acids (1-262a.a), with a molecular mass of 31.8 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.
BT29120
Source
Escherichia Coli.
Appearance
A clear solution, sterilized by filtration.

CA14 Human

Carbonic Anhydrase XIV Human Recombinant

Recombinant human CA14, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 298 amino acids (residues 16-290). It has a molecular weight of 33.2 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29180
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.

CA1 E.Coli

Carbonic Anhydrase-1 E.Coli Recombinant

Recombinant CA1 from E. coli is a single, non-glycosylated polypeptide chain. It consists of 240 amino acids, with amino acids 1-220 representing the CA1 protein, and has a molecular weight of 27.0 kDa. The protein is expressed in E. coli and purified using proprietary chromatographic methods. A 20 amino acid His-Tag is fused to the N-terminus to aid in purification.

Shipped with Ice Packs
Cat. No.
BT28665
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

CA1 Human

Carbonic Anhydrase-1 Human Recombinant

Recombinant Human Carbonic anhydrase 1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 281 amino acids, with 261 amino acids (1-261 a.a) forming the carbonic anhydrase 1 sequence, and has a molecular weight of 31 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification by conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28766
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

CA1 Human, Active

Carbonic Anhydrase-1 Human Recombinant, BioActive

Recombinant human carbonic anhydrase 1 (CA1) was expressed in E. coli. The non-glycosylated polypeptide chain comprises 281 amino acids (residues 1-261), resulting in a molecular weight of 31.0 kDa.

The N-terminus of human CA1 is fused to a 20 amino acid His-Tag. Purification is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT28835
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

CA3 Human

Carbonic Anhydrase III Human Recombinant

Recombinant human CA3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 260 amino acids (1-260 a.a.). With a molecular mass of 29.5 kDa, this protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29241
Source
Escherichia Coli.
Appearance
Sterile Filtered clear and colorless solution.

Carbonic Anhydrase II E.coli

Carbonic Anhydrase II E.coli Recombinant

Carbonic anhydrase II is a recombinant protein derived from E. coli. It consists of 240 amino acids (1-220) and has a molecular weight of 27 kDa. This enzyme is expressed with an amino-terminal hexahistidine tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29656
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Carbonic anhydrase (CA) is a metalloenzyme that catalyzes the reversible hydration of carbon dioxide (CO₂) to bicarbonate (HCO₃⁻) and protons (H⁺) . This enzyme is crucial for maintaining acid-base balance and facilitating CO₂ transport in various organisms. CAs are classified into several distinct families based on their structure and evolutionary origin: α, β, γ, δ, ζ, η, and θ . The α-family is predominant in humans, while other families are found in plants, algae, and bacteria .

Biological Properties

Key Biological Properties: Carbonic anhydrase is characterized by its high catalytic efficiency and the presence of a zinc ion at its active site . This enzyme is involved in rapid interconversion between CO₂ and bicarbonate, which is essential for various physiological processes .

Expression Patterns and Tissue Distribution: CA is ubiquitously expressed in many tissues, including red blood cells, kidneys, lungs, and the gastrointestinal tract . Different isoforms of CA are distributed in specific tissues, reflecting their specialized functions. For example, CA II is abundant in red blood cells, while CA IV is found in the kidneys and lungs .

Biological Functions

Primary Biological Functions: The primary function of CA is to catalyze the reversible hydration of CO₂, which is vital for respiration and pH regulation . In the lungs, CA facilitates the conversion of CO₂ to bicarbonate, aiding in CO₂ transport from tissues to the lungs for exhalation .

Role in Immune Responses and Pathogen Recognition: CA plays a role in maintaining the pH balance in various tissues, which is crucial for immune cell function and pathogen recognition . By regulating the local pH, CA can influence the activity of immune cells and the effectiveness of the immune response .

Modes of Action

Mechanisms with Other Molecules and Cells: CA interacts with various molecules and cells to maintain acid-base homeostasis. It catalyzes the conversion of CO₂ to bicarbonate and protons, which are then transported across cell membranes .

Binding Partners and Downstream Signaling Cascades: CA binds to zinc ions at its active site, which is essential for its catalytic activity . The enzyme’s activity can influence downstream signaling pathways involved in pH regulation and ion transport .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of CA are regulated at multiple levels, including transcriptional regulation and post-translational modifications . Various factors, such as pH, CO₂ levels, and hormonal signals, can influence CA expression .

Transcriptional Regulation and Post-Translational Modifications: Transcription factors and signaling molecules can modulate the expression of CA genes . Post-translational modifications, such as phosphorylation and acetylation, can also affect the enzyme’s activity and stability .

Applications

Biomedical Research: CA is extensively studied in biomedical research due to its role in various physiological processes and diseases . Researchers are exploring CA inhibitors as potential therapeutic agents for conditions like glaucoma, epilepsy, and cancer .

Diagnostic Tools and Therapeutic Strategies: CA inhibitors, such as acetazolamide, are used to treat glaucoma by reducing intraocular pressure . Additionally, CA is being investigated for its potential in cancer therapy, as certain isoforms are overexpressed in tumors .

Role in the Life Cycle

Role Throughout the Life Cycle: CA plays a critical role throughout the life cycle, from development to aging and disease . During development, CA is involved in processes like bone formation and neural development . In aging, changes in CA activity can affect physiological functions and contribute to age-related diseases .

From Development to Aging and Disease: CA’s role in maintaining pH balance and facilitating CO₂ transport is essential for various stages of life . Dysregulation of CA activity can lead to conditions like osteoporosis, neurodegenerative diseases, and metabolic disorders .

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