- Regulatory Status
- RUO
- Other Names
- Notch drosophila homolog of 3, Notch3, Neurogenic locus notch homolog protein 3
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- Product Citations
- publications
![Human_Notch-3_CF_RECOM_1_031519 Human_Notch-3_CF_RECOM_1_031519](https://d1spbj2x7qk4bg.cloudfront.net/Admin/Public/GetImage.ashx?Image=/Files/Images/media_assets/products/product_images/Human_Notch-3_CF_RECOM_1_031519.png&Width=240&Height=300&altFmImage_path=&Compression=90&Crop=5)
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When recombinant human Notch-3-Fc Chimera is immobilized at 5 µg/mL, biotinylated recombinant rat Jagged-1 binds with an EC50 of 0.2 – 0.8 µg/mL in a functional ELISA. HRP Protein A (Cat. No. 689202) was used to detect the binding. -
Stability testing for Human Notch-3. Recombinant human Notch-3-Fc Chimera was aliquoted in PBS, pH 7.2 at 0.2 mg/mL. One aliquot was frozen and thawed four times (4x Freeze/Thaw), and compared to a control kept at 4°C (control). The samples were tested in a binding assay with biotinylated recombinant rat Jagged-1.
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Human Notch-3 is a large type I transmembrane glycoprotein that is involved in cell fate specification, differentiation, and tissue patterning. Notch has two distinct domains, an extracellular domain (NECD) responsible for the interaction with the ligands and an intracellular domain (NICD) responsible for signal transduction. Human NECD (amino acid 19-526) shows 91% amino acid sequence identity with mouse and rat NECD. There are five Notch ligands (DLL1, DLL3, DLL4, Jagged-1 and Jagged-2) and four Notch receptors (Notch-1 to Notch-4) in mammals. Interactions of Notch receptors with membrane bound ligands result in sequential proteolysis by ADAM (disintegrin metalloprotease) and then by presenilin/gamma secretase, resulting in the shedding of NECD and the generation of soluble NICD signaling fragments. The NICD translocates to the nucleus and interacts with transcriptional factors to promote the transcription of target genes. Notch-3 interaction with its ligands regulate a number of biological functions such as differentiation, proliferation, angiogenesis, apoptosis and stem cell renewal. Mutations in Notch-3 in humans is associated with an autosomal dominant condition called CADASIL (cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy), IMF2 (infantile myofibromatosis-2), and LMS (lateral meningocele syndrome).
Product DetailsProduct Details
- Source
- Human Notch-3, amino acid Ala40-Glu467 (Accession # Q9UM47), with a C-terminal human IgG1 (Pro100-Lys330) was expressed in CHO cells.
- Molecular Mass
- The 667 amino acid recombinant protein has a predicted molecular mass of approximately 71.7 kD. The DTT-reduced and non-reduced protein migrates at approximately 70 kD and 140 kD respectively by SDS-PAGE. The predicted N-terminal amino acid is Ala.
- Purity
- >95%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in PBS, pH 7.2
- Endotoxin Level
- Less than 0.1 EU per µg protein as determined by the LAL method.
- Concentration
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Activity
- When recombinant human Notch-3-Fc Chimera is immobilized at 5 µg/mL, biotinylated recombinant rat Jagged-1 binds with an EC50 of 0.2 – 0.8 µg/mL in a functional ELISA.
- Application
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Bioassay
- Application Notes
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BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at [email protected].
Antigen Details
- Structure
- Disulfide-linked homodimer
- Distribution
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Ubiquitously expressed in fetal and adult tissues.
- Function
- Functions as a receptor for membrane-bound ligands Jagged-1, Jagged-2 and Delta-1 to regulate cell-fate determination
- Ligand/Receptor
- Jagged-1, Jagged-2, Delta-1
- Bioactivity
- Measured by its ability to bind biotinylated recombinant rat Jagged-1
- Biology Area
- Immunology, Signal Transduction
- Molecular Family
- Soluble Receptors
- Antigen References
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- Ellisen LW, et al. 1991. Cell. 66: 649-661
- Logeat F, et al. 1998. Proc Nat Acad Sci. 95: 8108-8112
- Chan YM, et al. 1998. Cell. 94: 423-426
- De Strooper B, et al. 1999. Nature. 398: 518-522
- Mumm JS, et al. 2000. Molec Cell. 5: 197-206
- Das I, et al. 2004. J Biol Chem. 279: 30771-30780
- Aguirre A, et al. 2010. Nature. 467: 323-327
- Gene ID
- 4854 View all products for this Gene ID
- UniProt
- View information about Notch-3 on UniProt.org
Related Pages & Pathways
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Related FAQs
- Why choose BioLegend recombinant proteins?
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• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - How does the activity of your recombinant proteins compare to competitors?
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We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
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The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
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Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
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Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
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Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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