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Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF

Name: Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF
Brand: R&D Systems
SKU: 8335D-GMP
Price: 310 USD
Availability: InStock

R&D Systems | Catalog # 8335D-GMP

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Product Documents

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Product Specifications
Scientific Data
Preparation & Storage
Calculators
Background
Product Documents
Manufacturing Specifications
Specific Notices
Research Areas

Key Product Details

Source

E. coli

Accession Number

P05019.1

Applications

Bioactivity

View all IGF-I/IGF-1 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human IGF-I/IGF-1 protein

MFPAMPLSSLFVN	Human LR3 IGF-I/IGF-1 (Gly49-Ala118 (Glu51Arg)) Accession # P05019.1
N-terminus		C-terminus

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. The result of the major peak from mass spectrometry analysis is 9111 Da, which corresponds to the calculated molecular mass of 9118 Da.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met-Phe-Pro-Ala-Met-Pro-Leu-Ser-Ser-Leu

Predicted Molecular Mass

9 kDa

SDS-PAGE

8 kDa, reducing conditions

Activity

Measured in a serum-free cell proliferation assay using MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083.
The ED₅₀ for this effect is 0.3-1.5 ng/mL. IGFBP-3 does not inhibit its activity.

Host Cell Protein

<0.1 ng per µg of protein when tested by ELISA.

Mycoplasma

Negative for Mycoplasma.

Host Cell DNA

<0.0015 ng per µg of protein when tested by PCR.

Scientific Data Images for Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF

Recombinant Human LR3 IGF-I/IGF-1 GMP Protein Bioactivity

GMP-grade Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335D‑GMP) stimulates cell proliferation in a serum-free assay using the MCF‑7 human breast cancer cell line. The ED₅₀ for this effect is 0.3‑1.5 ng/mL.

Recombinant Human LR3 IGF-I/IGF-1 GMP Protein SDS-PAGE

2 μg/lane of GMP-grade Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335D-GMP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing R and NR bands at 8 kDa.

Formulation, Preparation, and Storage

8335D-GMP

Formulation	Lyophilized from a 0.2 μm filtered solution in Acetic Acid.
Reconstitution	Reconstitute at 100-200 μg/mL in sterile 100 mM Acetic Acid
Shipping	The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, ≤ -20 °C under sterile conditions after reconstitution.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

Volume (to add to vial)

Mass (in vial)

Desired Reconstitution Concentration

Background: IGF-I/IGF-1

Insulin-like Growth Factor 1 (IGF-1 or IGF-I), also known as Somatomedin C, is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. Human IGF-1 is synthesized as two precursor isoforms with N- and alternative C‑terminal propeptides (1). These isoforms are differentially expressed by various tissues (1). The 7.6 kDa mature IGF‑1 is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-1 shares 94% and 96% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively (2). GH stimulates the production of IGF-1 in most tissues (3). Hepatocytes produce circulating IGF-1, while local IGF-1 is produced by many other tissues in which it has paracrine effects (1). IGF-1 induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally (4, 5). IGF-1 regulates glucose, fatty acid, and protein metabolism, steroid hormone activity, and cartilage and bone metabolism (6-11). It plays an important role in muscle regeneration and tumor progression (1, 12, 13). IGF-1 binds IGF1R, IGF2R, and the Insulin Receptor, although its effects are mediated primarily by IGF1R (14). IGF-1 also binds with strong affinity to IGF binding proteins (IGFBPs), which regulate the availability and biological activities of IGF-1 (15, 16).

Long R3 IGF-1 (LR3 IGF-1) is a 9.2 kDa synthetic analog of IGF-1 that is generated by modifying the aa sequence for mature human IGF-1. These modifications include the substitution of an Arg for Glu at position 3 of the mature IGF-1 sequence and the addition of a thirteen aa N-terminal extension, which is derived from methionyl porcine Growth Hormone (17). These aa changes generate a protein that is still capable of binding to IGF-1 and Insulin receptors, but shows considerably lower affinity binding to IGFBPs compared to wild-type IGF-1 (17, 18). As a result, LR3 IGF-1 has an increased half-life and displays increased biological potency compared to IGF-1 (17-22).

References

Philippou, A. et al. (2007) In Vivo 21:45.
Sandberg-Nordqvist, A.C. et al. (1992) Brain Res. Mol. Brain Res. 12:275.
Berryman, D.E. et al. (2013) Nat. Rev. Endocrinol. 9:346.
Guvakova, M.A. (2007) Int. J. Biochem. Cell Biol. 39:890.
Sadagurski, M. and M.F. White (2013) Endocrinol. Metab. Clin. North Am. 42:127.
Clemmons, D.R. (2006) Curr. Opin. Pharmacol. 6:620.
Bluher, S. et al. (2005) Best Pract. Res. Clin. Endocrinol. Metab. 19:577.
Garcia-Segura, L.M. et al. (2006) Neuroendocrinology 84:275.
Malemud, C.J. (2007) Clin. Chim. Acta 375:10.
Ling, P.R. et al. (1995) Am. J. Clin. Nutr. 61:116.
Sheng, M.H. et al. (2014) J. Bone Metab. 21:41.
Samani, A.A. et al. (2007) Endocrine Rev. 28:20.
Gallagher, E.J. et al. (2010) Endocr. Pract. 16:864.
LeRoith, D. and S. Yakar (2007) Nat. Clin. Pract. Endocrinol. Metab. 3:302.
Denley, A. et al. (2005) Cytokine Growth Factor Rev. 16:421.
Duan, C. and Q. Xu (2005) Gen. Comp. Endocrinol. 142:44.
Francis, G.L. et al. (1992) J. Mol. Endocrinol. 8:213.
Voorhamme, D. and C.A. Yandell (2006) Mol. Biotechnol. 34:201.
Tomas, F.M. et al. (1993) Biochem. J. 291:781.
Tomas, F.M. et al. (1996) J. Endocrinol. 150:77.
Tomas, F.M. et al. (1997) J. Endocrinol. 155:377.
von der Thüsen, J.H. et al. (2011) Am. J. Pathol. 178:924.

Long Name

Insulin-like Growth Factor I/Insulin-like Growth Factor 1

Alternate Names

IGF-1, IGF1, IGFI, Somatomedin A, Somatomedin C

Entrez Gene IDs

3479 (Human); 16000 (Mouse); 24482 (Rat)

Gene Symbol

IGF1

UniProt

P05019.1

Additional IGF-I/IGF-1 Products

Product Documents for Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF

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Certificate of Analysis

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Manufacturing Specifications

GMP Proteins
R&D Systems, a Bio-Techne Brand's GMP proteins are produced according to relevant sections of the following documents: USP Chapter 1043, Ancillary Materials for Cell, Gene and Tissue-Engineered Products and Eu. Ph. 5.2.12, Raw Materials of Biological Origin for the Production of Cell-based and Gene Therapy Medicinal Products.

R&D Systems' quality focus includes:

Designed, manufactured and tested under an ISO 9001:2015 and ISO 13485:2016 certified quality system
Documented and controlled manufacturing process
Control of documentation and process changes by QA
Personnel training programs
Raw material inspection and vendor qualification/monitoring program
Validated equipment, processes and test methods
Equipment calibration and maintenance schedules using a Regulatory Asset Manager
Facility/Utilities maintenance, contamination controls, safety and pest control programs
Material review process for variances
Robust product stability program following relevant ICH guidelines

R&D Systems strives to provide our customers with the analytical characteristics of each product so that customers may determine whether our products are appropriate for their application. Each product is provided with a lot-specific Certificate of Analysis that contains the product's specifications and test results. Quality control testing may include, but is not limited to:

N-terminal amino acid analysis
SDS-PAGE purity analysis
Molecular weight analysis via mass spectrometry
Endotoxin assessment per USP <85> and Ph. Eur. 2.6.14 guidelines
Bioassay analysis
Microbial testing per USP <71> and Ph. Eur. 2.6.1 guidelines
Host cell protein assessment
Host cell DNA assessment
Mycoplasma assessment

Additional testing and documentation requested by the customer can be arranged at an additional cost.

Production records and facilities are available for examination by appropriate personnel on-site at R&D Systems in Minneapolis and St. Paul, Minnesota USA.

R&D Systems sells GMP grade products for preclinical or clinical ex vivo use. They are not for in vivo use. Please read the following End User Terms prior to using this product.

Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.

Production