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Recombinant Aequorea victoria Aequorin Protein

Cat.No. : Aequorin-155
Product Overview : Recombinant Aequorea victoria Aequorin was expressed in E. coli.
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  • Gene Information
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Description : Aequorin, a photoprotein originating from the jellyfish Aequorea victoria emits light in the presence of a trace amount of Ca2+ without the requirement of any other cofactor. Aequorin was “charged” with unmodified (native) Coelenterazine and will emit light at 465 nm upon Ca2+ contact.
Source : E. coli
Species : Aequorea victoria
AA Sequence : MTSKQYSVKLTSDFDNPRWIGRHKH MFNFLDVNHNGKISLDEMVYKASDI VINNLGATPEQAKRHKDAVEAFFGG AGMKYGVETDWPAYIEGWKKLATDE LEKYAKNEPTLIRIWGDALFDIVDK DQNGAITLDEWKAYTKAAGIIQSSE DCEETFRVCDIDESGQLDVDEMTRQ HLGFWYTMDPACEKLYGGAVP
Purity : > 95% by SDS-PAGE
Applications : postitive control in Ca2+ assays
Storage : Store at -20 centigrade or below upon arrival.
Reconstitution : with Ca2+ free double distilled water

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (10)

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Are there any genetic variations or mutations in the Aequorin gene that impact the expression or function of Aequorin protein, and how do these variations affect bioluminescence activity? 12/31/2022

Genetic variations or mutations in the Aequorin gene may impact the expression or function of Aequorin protein, potentially affecting its bioluminescence activity and calcium-binding properties.

What is the mechanism of action of Aequorin protein in producing bioluminescence, and how is the light emission measured or quantified in experimental assays? 11/11/2022

Aequorin protein produces bioluminescence through a process called bioluminescence resonance energy transfer (BRET), and the light emission can be measured or quantified using luminescence detection instruments or imaging systems.

How is the expression of Aequorin protein regulated, and what factors influence its expression levels in different cell types or under specific conditions? 03/18/2021

The expression of Aequorin protein is regulated at the transcriptional level by specific promoters and regulatory elements. Factors such as calcium signaling or cellular stress can influence its expression levels.

What are the structural features and domains of Aequorin protein that contribute to its bioluminescent properties? 12/29/2020

The structural features and domains of Aequorin protein, including the EF-hand calcium-binding domain and the luciferin-binding site, contribute to its bioluminescent properties.

What is the optimal pH, temperature, and environmental conditions for the bioluminescence activity of Aequorin protein, and how are these parameters determined experimentally? 09/14/2020

The bioluminescence activity of Aequorin protein is optimal at specific pH, temperature, and environmental conditions, which can be determined experimentally by assessing light emission under different parameters.

Can Aequorin protein be engineered or modified to expand its applications in research, such as developing biosensors or monitoring specific cellular processes? 12/20/2018

Aequorin protein can be engineered or modified to expand its applications in research. For example, fusion with specific targeting sequences or fluorescent proteins can enable its localization to specific cellular compartments or visualization of calcium dynamics.

What experimental techniques or assays have been used to study the functionality of Aequorin protein, such as calcium imaging or bioluminescence resonance energy transfer (BRET)? 07/28/2018

Experimental techniques such as calcium imaging, BRET assays, or luminescence resonance energy transfer (LRET) have been used to study the functionality of Aequorin protein and assess its calcium-binding or bioluminescence properties.

How does Aequorin protein behave in different cellular compartments or organelles, and what is its subcellular localization under normal and experimental conditions? 03/11/2016

Aequorin protein can localize to different cellular compartments or organelles, such as the cytoplasm, endoplasmic reticulum, or mitochondrial matrix, depending on the targeting sequences or specific experimental conditions.

Does Aequorin protein interact with other molecules or participate in protein-protein interactions, and if so, what are the functional implications? 09/03/2015

Aequorin protein can interact with calcium ions and other molecules involved in calcium signaling, as well as potentially participate in protein-protein interactions that modulate its function or localization.

Are there any known post-translational modifications or cofactors required for the proper folding and function of Aequorin protein? 03/19/2015

Post-translational modifications, such as protein glycosylation or phosphorylation, and the presence of cofactors like calcium ions are essential for the proper folding and function of Aequorin protein.

Customer Reviews (3)

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Reviews
10/28/2020

    Detecting protein-protein interactions in cellular signal transduction pathways.

    04/30/2017

      Exploring protein-protein interactions involved in protein folding and quality control.

      03/05/2017

        Understanding protein-protein interaction networks in synaptic function.

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