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咨询Carrier Free
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.
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.
1544-IR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
1544-IR/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| 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.
|
Recombinant Human Insulin R/CD220 (aa 28-944) Protein Summary
Product Specifications
His28-Arg750 ( alpha subunit) & Ser751-Lys944 with a C-terminal 10-His tag ( beta subunit)
Analysis
Background: Insulin R/CD220
The Insulin Receptor (gene name INSR, designated CD220) is a type I transmembrane glycoprotein in the Insulin/IGF Receptor family of receptor tyrosine kinases that share structural similarity and overlapping intracellular signaling events (1-3). The 1370 amino acid (aa) human Insulin R preproprotein (A isoform) is processed by proteolysis to remove the signal peptide and produce an extracellular alpha portion (aa 28-750), and an extracellular/transmembrane/cytoplasmic beta subunit (aa 751-1370) (4). The extracellular domain (ECD) contains two homologous globular domains separated by a cysteine-rich domain and followed by three fibronectin type III domains. The intracellular region contains insulin-receptor substrate (IRS) docking sites, the kinase domain, and a phosphotyrosine-containing linker region. The human Insulin R ECD shares 96% aa sequence identity with mouse, rat, equine and canine Insulin R. As a result of alternative splicing, two INSR isoforms that differ by the absence (IR-A) or presence (IR-B) of a 12 aa residue sequence in the carboxyl terminus of the alpha subunit exist (4). IR-A expression is highest in fetal tissues and cancer cells, while IR-B is concentrated in adult differentiated cells (2-5). IR-A and IR-B may homodimerize, or heterodimerize with the IGF-I receptor (1, 3, 4). All receptor combinations bind insulin, IGF-I or IGF-II, but with differing affinities; for example, IR-A has considerably higher affinity for IGF-II as compared to IR-B (2-5). This system allows fine tuning of signaling pathways according to the concentrations of insulin, IGF-I and IGF-II, and expression of receptor subunits on the cell surface (2, 3). Insulin R signaling regulates glucose uptake and metabolism, but also contributes to cell growth, differentiation and apoptosis (2, 3, 5, 6). Mutations in the Insulin R gene have been linked severe insulin resistance (type A and Rabson-Mendenhall syndrome) that may include type II diabetes mellitus and, rarely, leprechaunism (Donohue syndrome) that also includes growth delays and endocrine system abnormalities (1, 7). The R&D Systems human Insulin R consists of the entire ECD of the IR-A isoform.
- Nakae, J. et al. (2001) Endoc. Rev. 22:818.
- Sciacca, L. et al. (2003) Endocrinology 144:2650.
- Belfiore, A. et al. (2009) Endocrine Rev. 30:586.
- Lawrence, M.C. et al. (2007) Curr. Opin. Struct. Biol. 17:699.
- Sacco, A. et al. (2009) Endocrinology 150:3594.
- Kitamura, T. et al. (2004) J. Clin. Invest. 113:209.
- Musso, C. et al. (2004) Medicine (Baltimore) 83:209.
