Recombinant Human IGF-1 LR3 (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Insulin-like growth factor I, somatomedin C, Non-suppressible insulin-like activity I (NSILA-I), Insulin-Like Growth Factor IB, IBP1, Long R3 IGF1, Long Arg3 IGF1, Long R3 Insulin-like growth factor I
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Product Citations
publications
a.
Recom_Human-IGF-1-LR3_1_CF_082025
Recombinant human IGF-1 LR3 induces the proliferation of MCF-7 human cells in a dose-dependent manner. The ED50 for this effect is 0.25 – 2.5 ng/mL.
  • a.
Recom_Human-IGF-1-LR3_1_CF_082025
    Recombinant human IGF-1 LR3 induces the proliferation of MCF-7 human cells in a dose-dependent manner. The ED50 for this effect is 0.25 – 2.5 ng/mL.
  • b.
Recom_Human-IGF-1-LR3_2_CF_082025
    Stability Testing for Recombinant Human IGF-1 LR3. Recombinant human IGF-1 LR3 lyophilized was kept at -20°C (Control), and another sampler was reconstituted in PBS, pH7.2 and kept at 4°C for two weeks (2w 4°C). The samples were tested by their property to induce the proliferation of MCF-7 human cells in a dose-dependent manner. The ED50 for this effect is 0.25 – 2.5 ng/mL.
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718856 50 µg 52€
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Description

IGF-I (insulin-like growth factor 1), initially described in 1957, is a hormone that is important in childhood growth and anabolic effects in adults. It 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. Human IGF-I is synthesized as a 191 amino acid prepro-IGF-I. Process of maturation to Pro-IGF- requires glucose regulating protein 94 (GRP94) that possesses chaperone activity towards IGF-I. Deletion of muscle GRP94 impairs muscle and body growth by inhibiting local production of IGF proteins. Seven binding proteins have been described (IGFBP-1 to -7). IGFBPs extend the half-life and regulate the availability of IGF-I and IGF-II. It has been described that IGFBP-3 is the main circulating binding protein for IGFs. In serum approximately 75% of circulating IGF-I and IGF-II bind to IGFBP-3 and the co-carrier acid labile subunit (ALS). IGF-I binds to three receptors, and the binding to IGFIR promotes cell proliferation, survival, differentiation, and migration. IGF-I deficiency is associated with growth hormone insensitivity syndrome (GHIS) also called Laron syndrome, liver cirrhosis, age-related cardiovascular and neurological diseases, and intrauterine growth restriction. IGF-1 LR3 (IGF-1 long R3) is a fusion protein that include in the amino terminus the first 11 amino acids of methionyl porcine growth hormone and the IGF1 sequence, where Glu3 was substituted by Arg. IGF-1 LR3 showed lower affinity to IGF binding proteins and a more potent hypoglycaemic action than IGF-1.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human IGF-1 LR3, amino acids (Gly49 - Ala118 (Glu51Arg)) (Accession# P05019), with N-terminus M-FPAMPLSSLFVN was expressed in E.coli
Molecular Mass
The 83 amino acid recombinant protein has a predicted molecular mass of approximately 6.5 kD. The protein migrates at approximately 8 kD in DTT reducing and non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Met.
Purity
> 95%, as determined by Coomassie stained SDS-PAGE.
Formulation
Lyophilized from 0.22 µm filtered protein solution in PBS, 5% trehalose, pH 7.2
Endotoxin Level
Less than 0.1 EU per µg of cytokine as determined by the LAL method.
Concentration
50 µg size lyophilized
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at - 20°C or colder until the expiration date. Reconstitute lyophilized protein in sterile PBS. Before reconstitution, make sure the PBS and product are at room temperature. Quickly spin the vial or gently tap down on the vial to make sure the lyophilized product is at the bottom of the vial before opening. Use aseptic techniques to add the required volume of reconstitution buffer (PBS) to the vial, to obtain the recommended stock concentration of 250 µg/mL. Close the vial and leave at an ambient temperature for 15-20 minutes. Then gently invert the vial several times or until all the lyophilized product dissolves. Leave the vial at room temperature for another 15 minutes. If small particulates are still observed after 15 minutes, incubate at room temperature for an additional 30 minutes, and leave the vial at 2°C - 8°C overnight. Next day, invert the vial several times or gently pipette the solution up and down before use. If needed, transfer the reconstituted stock solution to a sterile container for additional dilution to no less than 100 µg/mL. Small working aliquots in polypropylene tubes can be made after reconstitution and store the vials at -20°C or lower. Avoid freeze/thaw cycles. Carrier protein such as 0.2 - 1% endotoxin-free BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to two weeks or stored at -20°C or colder for up to 3 months.
Activity
Recombinant human IGF1 LR3 induces the proliferation of MCF-7 human epithelial cells in a dose-dependent manner. The ED50 for this effect is 0.25 – 2.5 ng/mL.
Application

Bioassay

Application Notes

Our lyophilized proteins are validated in-house to maintain activity after shipping at ambient temperature and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

Structure
Monomer
Distribution

Astrocytes, hepatocytes, microglia, intestinal smooth muscle, myoblast, NK cells

Function
IGF-I induces mitogenesis, proliferation, growth, differentiation, and angiogenesis. IGF-I is a mediator of growth hormone action. IGF-I is involved in neuronal myoblast proliferation and differentiation, and organ development. IGF-I promotes NK cell development and cytotoxic activity in NK cells.
Interaction
Neuronal cells, myoblast, T cells, B cells, NK cells
Ligand/Receptor
IGF-I receptor, Insulin receptor isoform A, and IGF-II receptor (M-6-P-R)
Bioactivity
Human LR3 IGF-1 induces the proliferation of MCF-7 human epithelial cells.
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. 310:775-7.
  2. Karey KP and Sirbasku DA. 1988. Cancer Res. 48:4083-92.
  3. Mohan S and Baylink DJ. 2002. J Endocrinol. 175:19-31.
  4. Ostrovsky O, et al. 2010. Biochim Biophys Acta. 1803:333-41.
  5. Barton ER, et al. 2012. FASEB J. 26:3691-702.
  6. Puche JE and Castilla-Cortázar I. 2012. J Transl Med. 10:224.
  7. Ni F, et al. 2013. Nat Commun. 4:1479.
  8. Francis GL, et al. 1992. J Mol Endocrinol. 8:213.
  9. Thomas FM, et al. 1997. J Endocrinol. 155: 337.
Gene ID
3479 View all products for this Gene ID
UniProt
View information about IGF-1 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: 1    Revision Date: 08.20.2025

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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