Analytical Data
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Gene name
EFHA2
- Application
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Alternative Names
MICU3; EFHA2; Calcium uptake protein 3. mitochondrial; EF-hand domain-containing family member A2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86XE3
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Expression Region
1-530aa
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AA Sequence
MAALRRLLWPPPRVSPPLCAHQPLLGPWGRPAVTTLGLPGRPFSSREDEERAVAEAAWRRRRRWGELSVAAAAGGGLVGLVCYQLYGDPRAGSPATGRPSKSAATEPEDPPRGRGMLPIPVAAAKETVAIGRTDIEDLDLYATSRERRFRLFASIECEGQLFMTPYDFILAVTTDEPKVAKTWKSLSKQELNQMLAETPPVWKGSSKLFRNLKEKGVISYTEYLFLLCILTKPHAGFRIAFNMFDTDGNEMVDKKEFLVLQEIFRKKNEKREIKGDEEKRAMLRLQLYGYHSPTNSVLKTDAEELVSRSYWDTLRRNTSQALFSDLAERADDITSLVTDTTLLVHFFGKKGKAELNFEDFYRFMDNLQTEVLEIEFLSYSNGMNTISEEDFAHILLRYTNVENTSVFLENVRYSIPEEKGITFDEFRSFFQFLNNLEDFAIALNMYNFASRSIGQDEFKRAVYVATGLKFSPHLVNTVFKIFDVDKDDQLSYKEFIGIMKDRLHRGFRGYKTVQKYPTFKSCLKKELHSR
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Molecular Weight
87.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
EFHA2, or EGF-containing fibulin-like extracellular matrix protein 2, has garnered attention in recent years due to its potential roles in various biological processes and disease pathologies. As a member of the fibulin family, EFHA2 is implicated in cell adhesion, migration, and tissue remodeling, making it a significant player in developmental biology and cancer progression. Research has suggested that EFHA2 may facilitate the binding of cells to the extracellular matrix, thereby influencing tumor microenvironments and metastatic behavior in cancer cells. Studies have shown altered EFHA2 expression levels in several tumors, including breast, ovarian, and colorectal cancers, indicating its potential as a biomarker for disease prognosis and therapeutic targets. Furthermore, its interaction with other cellular proteins and signaling pathways suggests a multifaceted role in maintaining tissue homeostasis and responding to pathological conditions. Given this context, the generation and characterization of recombinant EFHA2 protein have become crucial for elucidating its biological functions and mechanisms of action. Understanding EFHA2’s structure and interactions at a molecular level can provide insights into its contributions to cellular behavior and its potential involvement in therapeutic interventions in cancer and other diseases. As a result, advancing research on EFHA2 presents a promising avenue for developing novel strategies aimed at manipulating its function for therapeutic benefits.
