Analytical Data
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Gene name
Galectin-3/LGALS3
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简介
The Galectin-3/LGALS3 protein is a galactose-specific lectin known for its diverse roles in cellular processes. It binds IgE and synergizes with α-3 and β-1 integrins to promote CSPG4-induced endothelial cell migration. Galectin-3/LGALS3 Protein, Human (HEK293, His) is the recombinant human-derived Galectin-3/LGALS3 protein, expressed by HEK293 , with C-6*His labeled tag.
- Application
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Biological Activity
1.Measured by the ability of the immobilized protein to support the adhesion of TF-1 Human blood leukemia cells. The ED50 this effect is ≤6.301 μg/ml, corresponding to a specific activity is ≥158.705 units/mg. 2.Measured by the ability of the immobilized protein to support the adhesion of MOLT-4. The ED50 for this effect is 2.117 μg/mL, corresponding to a specific activity is 472.367 units/mg. 3. Loaded Oloctinebart (HY-P990081) on AHC2 biosensor, can bind Galectin-3/LGALS3 Protein, Human (HEK293, His) with an affinity constant of 5.984E-08 M as determined in BLI assay. Measured by the ability of the immobilized protein to support the adhesion of TF-1 Human blood leukemia cells. The ED50 for this effect is 6.301 μg/ml, corresponding to a specific activity is 158.705 units/mg. Loaded Oloctinebart (HY-P990081) on AHC2 biosensor, can bind Galectin-3/LGALS3 Protein, Human (HEK293, His) with an affinity constant of 5.984E-08 M as determined in BLI assay.
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
AAH53667.1
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Expression Region
A2-I250
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AA Sequence
ADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYHGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSAPGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI
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Protein Length
Full Length of Mature Protein
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Molecular Weight
32-40 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
Ezrin, also known as EZR, is a member of the ERM (ezrin-radixin-moesin) protein family, which plays a crucial role in linking the plasma membrane to the actin cytoskeleton. This protein is essential for various cellular processes, including cell shape maintenance, motility, and signal transduction. Dysregulation or aberrant expression of Ezrin has been implicated in several pathological conditions, such as cancer metastasis, where it facilitates the migration and invasion of tumor cells. The exploration of Ezrin as a recombinant protein has gained traction in recent years, providing insights into its structural and functional properties. Recombinant Ezrin can be produced using various expression systems, enabling detailed studies of its interactions with other proteins and cellular components. Furthermore, understanding the three-dimensional structure of Ezrin can reveal how post-translational modifications, such as phosphorylation, influence its activity and interaction with membrane proteins. This research has significant implications, as targeting Ezrin's function could offer therapeutic avenues in cancer treatment and other diseases characterized by altered cell adhesion and motility. Through the development of Ezrin/EZR recombinant proteins, researchers aim to elucidate the precise mechanisms underlying its role in cellular dynamics and assess its potential as a biomarker or therapeutic target in oncology and other fields.
