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

Name: Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF
Brand: rnd
SKU: 8335D-GMP

Catalog # 8335D-GMP

Datasheet / COA / SDS

Animal-Free

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Key Product Details

Source:	E. coli
Accession #:	P05019
Applications:	Bioactivity

View Full Technical Details for Recombinant Human LR3 IGF-I/IGF-1 GMP Protein, CF

Product Specifications

Source

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

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

Produced using non-animal reagents in an animal-free laboratory. Manufactured and tested under cGMP guidelines.

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.

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

	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 ED₅₀for this effect is 0.3‑1.5 ng/mL.
	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

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

8335D-GMP

Carrier Free

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.

Reconstitution Calculator

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.

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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).

Item	Value
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
Entrez Gene IDs	3479 (Human); 16000 (Mouse); 24482 (Rat)
Alternate Names	IBP1, IGF-1, IGF-I, IGF-IA, IGF-IB, IGF1, IGF1A, IGFI, MGF, Mechano growth factor, Somatomedin A, Somatomedin C, insulin-like growth factor 1, insulin-like growth factor 1 (somatomedin C), insulin-like growth factor I, insulin-like growth factor IA, insulin-like growth factor IB, somatomedin-C

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

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Key Product Details

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Product Specifications

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

Formulation, Preparation and Storage

Carrier Free

Carrier Free

Reconstitution Calculator

Background: IGF-I/IGF-1

Citations

Product Datasheets

Product Datasheets

COA

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SDS

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