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 |
Products Types
◆ Recombinant Protein | ||
Aequorin-154 | Recombinant Aequorea victoria Aequorin Protein | +Inquiry |
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)
Ask a questionGenetic 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.
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.
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.
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.
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.
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.
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.
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.
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.
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)
Write a reviewDetecting protein-protein interactions in cellular signal transduction pathways.
Exploring protein-protein interactions involved in protein folding and quality control.
Understanding protein-protein interaction networks in synaptic function.
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