Recombinant Mouse IGF-II (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Insulin-like growth factor II, somatomedin A
Ave. Rating
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Product Citations
publications
IGF-II_Mouse_Recombinant_Protein_BA_070113
MCF-7 cell proliferation induced by mouse IGF-II.
  • IGF-II_Mouse_Recombinant_Protein_BA_070113
    MCF-7 cell proliferation induced by mouse IGF-II.
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588204 25 µg 118€
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Description

IGF-II is a member of the IGF family that is comprised of three members (IGF-I, IGF-II, and insulin). IGF-I and IGF-II share approximately 50% similarity with insulin at the amino acid level. IGF-II is synthesized as a 180 amino acid in the pro-IGF-II form; pro-IGF-II is processed to the mature, active protein with the help of glucose regulating protein 94 (GRP94) that possesses chaperone activity towards IGF-II. GRP94 and IGF-II play a key role in muscle differentiation. Seven binding proteins have been described (IGFBP-1 to -7). IGFBPs extend the half life and regulate the availability of the IGFI and IGFII. It has been described that IGFBP3 is the main circulating binding protein for IGFs; in serum approximately 75% of circulating IGF-I and IGF-II bind to IGFBP3 and the co-carrier acid labile subunit (ALS). IGF-II binds to three receptors, and the binding to IGFIR promotes cell proliferation, survival, differentiation, and migration as well as metabolic function of IGF-II. Embryonic stem cell differentiation into endothelial cells is promoted by the binding of IGF-II to IGFR1. IGF-II binding to IGF-IIR induces internalization and clearing of IGF-II. Osteogenic differentiation and bone formation is enhanced by IGF-II through bone morphogenetic protein-9 (BMP-9). Polymorphisms of IGF-II are associated with obesity, cardiovascular risk factors, and hypertension.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Mouse IGF-II, amino acids (Ala25-Glu91) (Accession# NM_001122736.1) was expressed in E. coli.
Molecular Mass
The 67 amino acid recombinant protein has a predicted molecular mass of approximately 7.4 kD. The DTT-reduced and non-reduced protein migrate at approximately 9 kD by SDS-PAGE. The N-terminal amino acid is Ala.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in 5 mM citric acid, 5 mM NaH2PO4, 0.15 M NaCl, pH 3.0.
Endotoxin Level
Less than 1.0 EU per µg cytokine as determined by the LAL method.
Concentration
25 µg size is bottled at 100 µg/ml.
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
ED50 = 10 - 30 ng/ml, corresponding to a specific activity of 0.3 - 1 x 105 units/mg, as determined by the dose dependent stimulation of MCF-7 cell proliferation.
Application

Bioassay

Application Notes

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 tech@biolegend.com.

Product Citations
  1. Emmrich S, et al. 2022. EMBO J. 41:e109694. PubMed
  2. Ruiz-Rosado Jde D, et al. 2016. Mediators Inflamm. 9101762:2016. PubMed
  3. Hunt L, et al. 2015. Genes Dev. 29: 2475 - 2489. PubMed

Antigen Details

Distribution

Astrocytes, podocytes, hepatocytes, microglia, osteoblast, myoblast

Function
IGF-II induces mitogenesis, proliferation, growth, differentiation, and angiogenesis. IGF-II is a mediator of GH action. IGF-II is involved in neuronal, muscle differentiation, and organ development. TGFb1 diminish IGF-II gene expression and secretion in myoblasts.
Interaction
Neuronal cells, osteoblast, myoblast, and podocytes
Ligand/Receptor
IGF-I receptor, Insulin receptor isoform A, and IGF-II receptor (M-6-P-R)
Cell Type
Embryonic Stem Cells, Hematopoietic stem and progenitors, Mesenchymal Stem Cells, Neural Stem Cells
Biology Area
Cell Biology, Signal Transduction, Stem Cells
Molecular Family
Cytokines/Chemokines, Growth Factors
Antigen References

1. Bell GI, et al. 1984. Nature 310:775.
2. Chen L, et al. 2010. J. Bone Min. Res. 25:2447.
3. Obstrvsky O, et al. 2010. Biochim. Biophys. Acta. 1803:333.
4. Gardner S, et al. 2011. Mol. Endocrinol. 25:128.
5. Piecewicz SM, et al. 2012. Plos One 7(2):e32191.
6. Church DN, et al. 2012. Oncogene 31:3635.
7. Hale LJ, et al. 2013. J. Pathol. 230:95.
8. Zhen-Kun L, et al. 2013. Plos One 7(9):e45224.

Gene ID
16002 View all products for this Gene ID
UniProt
View information about IGF-II on UniProt.org

Related FAQs

Why choose BioLegend recombinant proteins?

     • 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?

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?

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?

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?

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?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 3    Revision Date: 03.28.2024

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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