Active Recombinant E. coli (strain K12) aqpZ Full Length Transmembrane protein, His-tagged

• Cat.No.: aqpZ-01E
• Product Overview: Active Recombinant E. coli (strain K12) aqpZ protein(P60844)(1-231aa), fused with N-terminal His tag, was expressed in E. coli.

Specification

• Source: In vitro E. coli expression system
• Species: E. coli (strain K12)
• Tag: His
• Form: Tris-based buffer，50% glycerol
• Bio-activity: Measured by its binding ability in a functional ELISA. Immobilized aqpZ at 5 μg/ml can bind E.coli ytfE, the EC50 of E.coli ytfE protein is 197.90-259.70 μg/ml.
• Molecular Mass: 27.7 kDa
• Protein Length: 1-231aa
• AA Sequence: MFRKLAAECFGTFWLVFGGCGSAVL AAGFPELGIGFAGVALAFGLTVLTM AFAVGHISGGHFNPAVTIGLWAGGR FPAKEVVGYVIAQVVGGIVAAALLY LIASGKTGFDAAASGFASNGYGEHS PGGYSMLSALVVELVLSAGFLLVIH GATDKFAPAGFAPIAIGLALTLIHL ISIPVTNTSVNPARSTAVAIFQGGW ALEQLWFFWVVPIVGGIIGGLIYRT LLEKRD
• Purity: Greater than 90% as determined by SDS-PAGE.
• Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
• Reconstitution: Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%.

Reviews

10/07/2021

the protein's high quality ensures accurate and reliable results, enabling precise analysis and interpretation of experimental data.

07/27/2021

Beyond its superb performance in Western blotting, the aqpZ protein has also proven invaluable in protein electron microscopy structure analysis.

06/01/2021

From troubleshooting to optimizing experimental protocols, the manufacturer provides diligent support to ensure the success of the trial.

11/10/2020

Its stability and purity make it an ideal candidate for studying protein structures at a high resolution, providing crucial insights into the organization and function of the aqpZ protein.

08/18/2020

It has consistently demonstrated outstanding results, consistently producing clear and sharp bands, allowing for accurate and reliable protein detection and quantification.

05/29/2020

the manufacturer's commitment to customer satisfaction extends beyond technical support. They offer a comprehensive range of related products and resources to aid researchers in their trials.

09/16/2019

The aqpZ protein offers several advantageous features that make it an ideal choice for researchers conducting trials.

08/29/2019

I highly recommend the aqpZ protein for its exceptional performance in Western blot analysis.

Q&As

Are there any known regulators or factors that influence the expression of AqpZ?

Several factors can influence the expression of AqpZ in bacteria. Osmotic stress, such as changes in salt concentration or water availability, can upregulate AqpZ expression to maintain cellular water balance. Additionally, transcription factors and signaling pathways involved in bacterial responses to environmental changes may also affect AqpZ expression levels. Further research is needed to fully understand the regulatory mechanisms of AqpZ expression.

Are there any pharmaceutical or biotechnological applications of AqpZ?

The study of AqpZ and related aquaporin proteins has led to potential pharmaceutical and biotechnological applications. Researchers are exploring the development of aquaporin-based water filtration systems for desalination and water purification purposes. Furthermore, understanding aquaporin function may contribute to the development of drugs targeting aquaporins in human diseases, such as cancer, edema, or kidney disorders.

Are there any pharmaceutical or biotechnological applications of AqpZ?

The study of AqpZ and related aquaporin proteins has led to potential pharmaceutical and biotechnological applications. Researchers are exploring the development of aquaporin-based water filtration systems for desalination and water purification purposes. Furthermore, understanding aquaporin function may contribute to the development of drugs targeting aquaporins in human diseases, such as cancer, edema, or kidney disorders.

Can AqpZ be targeted for drug development?

While AqpZ itself is primarily studied in bacterial systems, aquaporins in general, including those found in humans, have been identified as potential drug targets. The selective inhibition or modulation of specific aquaporins could be beneficial for various pathological conditions where water transport plays a significant role, such as in the treatment of fluid retention or certain types of tumors.

Can AqpZ be targeted for drug development?

While AqpZ itself is primarily studied in bacterial systems, aquaporins in general, including those found in humans, have been identified as potential drug targets. The selective inhibition or modulation of specific aquaporins could be beneficial for various pathological conditions where water transport plays a significant role, such as in the treatment of fluid retention or certain types of tumors.

Can AqpZ be found in other bacterial species apart from E. coli?

While Aquaporin Z (AqpZ) was initially discovered in E. coli, related homologs have been identified in several other bacterial species. These homologs, known as GlpF, GlpF2, or AqpZ-like proteins, share structural and functional similarities with AqpZ. They also act as water channels in their respective organisms and contribute to osmoregulation and water homeostasis.

Can AqpZ be found in other bacterial species apart from E. coli?

While Aquaporin Z (AqpZ) was initially discovered in E. coli, related homologs have been identified in several other bacterial species. These homologs, known as GlpF, GlpF2, or AqpZ-like proteins, share structural and functional similarities with AqpZ. They also act as water channels in their respective organisms and contribute to osmoregulation and water homeostasis.

How does AqpZ facilitate water transport?

AqpZ forms tetrameric structures in the bacterial cell membrane, creating a channel that allows water molecules to pass through. It utilizes a "hourglass" shape, with a narrow constriction in the middle of the channel that restricts the passage of solutes but allows water molecules to pass through rapidly.

Are there any specific amino acid residues in AqpZ important for its function?

Yes, several amino acid residues within AqpZ are critical for its function. For example, the NPA (Asparagine-Proline-Alanine) motif, located in the helix-loop-helix region, forms part of the water-selective filter of the channel. Other residues, such as Arg195 and Arg225, are involved in regulating the conductance of water and preventing the passage of solutes. These residues play a vital role in maintaining the high water selectivity of AqpZ.

Are there any specific amino acid residues in AqpZ important for its function?

Yes, several amino acid residues within AqpZ are critical for its function. For example, the NPA (Asparagine-Proline-Alanine) motif, located in the helix-loop-helix region, forms part of the water-selective filter of the channel. Other residues, such as Arg195 and Arg225, are involved in regulating the conductance of water and preventing the passage of solutes. These residues play a vital role in maintaining the high water selectivity of AqpZ.

What are the physiological conditions where AqpZ is important?

AqpZ is particularly important for bacteria living in environments with varying osmotic conditions. It helps bacteria adapt to changes in external osmotic pressure by facilitating water entry into or exit from the cell, preventing cellular dehydration or overhydration.

Is AqpZ found only in bacteria, or is it present in other organisms as well?

Aquaporin Z (AqpZ) is primarily found in bacteria, specifically E. coli. However, aquaporin proteins with similar functions are present in various organisms, including plants, animals, and humans. These aquaporins play essential roles in water transport and balance within cells and tissues.

Are there any diseases or disorders associated with AqpZ dysfunction?

As of now, there are no known diseases or disorders directly linked to AqpZ dysfunction in bacteria. However, mutations or altered expression of aquaporin proteins in other organisms have been associated with various diseases, including nephrogenic diabetes insipidus and certain forms of cataracts.

Can AqpZ function as a selective filter for other molecules besides water?

Although AqpZ primarily functions as a selective water channel, some studies have suggested that it may allow the passage of small solutes such as urea or glycerol, but to a much lesser extent compared to water. However, its primary role remains the rapid transport of water across the bacterial cell membrane.

Can AqpZ function as a selective filter for other molecules besides water?

Although AqpZ primarily functions as a selective water channel, some studies have suggested that it may allow the passage of small solutes such as urea or glycerol, but to a much lesser extent compared to water. However, its primary role remains the rapid transport of water across the bacterial cell membrane.