Carbonic Anhydrase 2 Human

Carbonic Anhydrase 2 Human Recombinant
Cat. No.
BT29555
Source
Escherichia Coli.
Synonyms
Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Carbonic anhydrase 2 Human Recombinant protein produced in E.Coli containing 260 amino acids (1-260) and having a molecular mass of 29.2 kDa.
The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Carbonic anhydrase II, also known as carbonate dehydratase (accession number NP_414668), belongs to a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate, carbonic acid, and protons (CO2 + H2O ↔ HCO3- + H+). This reaction occurs slowly in the absence of a catalyst. Most carbonic anhydrases are metalloenzymes, containing a zinc ion in their active site. Carbonic anhydrase plays a crucial role in maintaining acid-base balance in blood and tissues and facilitates carbon dioxide transport. These enzymes are ubiquitous, found in all kingdoms of life. There are three distinct classes of carbonic anhydrases: alpha, beta, and gamma, with minimal sequence or structural similarity but sharing the same function and the requirement for a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class, while plant carbonic anhydrase is dimeric and belongs to the beta class. Methane-producing bacteria, found in hot springs, possess trimeric carbonic anhydrase, forming the gamma class.
Description
Recombinant human Carbonic anhydrase 2, produced in E. coli, encompasses 260 amino acids (1-260) and exhibits a molecular weight of 29.2 kDa. The purification of Carbonic anhydrase 2 is achieved using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The Carbonic Anhydrase 2 protein solution is provided at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 1mM DTT, 50mM NaCl, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product should be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freeze-thaw cycles should be avoided.
Biological Activity
The specific activity, determined by measuring the increase in p-nitrophenol due to esterase activity, ranges from 50 to 70 nmoles/min/µg. Specific activity represents the amount of p-nitrophenol that 1 µg of enzyme can reduce per minute at a temperature of 25°C.
Purity
The purity of the protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.
Source
Escherichia Coli.
Amino Acid Sequence
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL KNRQIKASFK

Product Science Overview

Function and Importance

CA2 catalyzes the reversible hydration of carbon dioxide, converting it into bicarbonate and protons. This reaction is essential for maintaining acid-base balance in blood and other tissues . The enzyme is involved in several physiological processes, including:

  • pH regulation: Helps maintain the acid-base balance in the body.
  • Ion transport: Facilitates the transport of ions across cell membranes.
  • Metabolic processes: Plays a role in various metabolic pathways .
Genetic and Clinical Significance

Mutations in the CA2 gene can lead to CA II deficiency syndrome, an autosomal recessive disorder. This syndrome is characterized by:

  • Osteopetrosis: A condition where bones become overly dense.
  • Renal tubular acidosis: A disorder that affects the kidneys’ ability to maintain acid-base balance.
  • Cerebral calcification: Abnormal calcium deposits in the brain .
Recombinant Human CA2

Recombinant human CA2 is produced using E. coli expression systems. The recombinant protein is typically purified using conventional chromatography techniques . It is available in various formulations, including those with and without carrier proteins like Bovine Serum Albumin (BSA). The carrier-free versions are recommended for applications where the presence of BSA could interfere with experimental results .

Applications

Recombinant human CA2 is widely used in research, particularly in studies related to:

  • Signal transduction: Understanding the pathways and mechanisms of cellular signaling.
  • Drug development: Screening for potential inhibitors or activators of CA2.
  • Physiological studies: Investigating the enzyme’s role in various physiological processes .
Storage and Stability

Recombinant human CA2 is typically stored at -20°C to -70°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity. The protein can be stored for up to six months under these conditions .

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