| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF. |
| Biological Activity | |
| Expression System | |
| Form | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Formulation | |
| Product Type | |
| Protein Length | |
| Protein Size | |
| Purity | |
| Solubility | It is recommended to reconstitute the lyophilized IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. |
| Source | Escherichia Coli. |
| Species | |
| Storage | |
| Target |
Recombinant Human Insulin Like Growth Factor-1 is supplied as a recombinant protein for in vitro research use.
Background
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of: ● Two cell-surface receptors (IGF1R and IGF2R) ● Two ligands (IGF-1 and IGF-2) ● A family of six high-affinity IGF-binding proteins. ● Proteases. The Effect IGF Has On The Body Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body. Diseases And IGF Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies. It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS. How Was IGF Discovered? Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor. What’s The Difference Between IGF-1 And IGF-2? The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells. The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.
Product format
Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.
What is the purity of Recombinant Human Insulin Like Growth Factor-1 (Human)?
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
How should Recombinant Human Insulin Like Growth Factor-1 (Human) be stored?
What expression system was used to produce this protein?
Is this protein biologically active?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
