|Official Full Name
|Recombinant Human Neuregulin 1-beta2 EGF-like domain GMP (rHuNRG1-beta2)
|Amino Acid Sequence
|Neuregulin 1 belongs to a family of structurally related polypeptide growth factors and is produced in numerous isoforms by alternative splicing, which allows it to perform a wide variety of functions. These isoforms include heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). They all have the Ig and EGF-like domain, and can bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding induces ErbB3 and ErbB4 heterodimerization with ErbB2, stimulating intrinsic kinase activity, which leads to tyrosine phosphorylation. NRG1 isoforms have functions of inducing the growth and differentiation of epithelial, neuronal, glial, and other types of cells.
|Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5 ng/ml, corresponding to a specific activity of > 2.0 × 5 U/mg.
|Sterile Filtered White lyophilized (freeze-dried) powder.
|Lyophilized from a 0.2 um filtered solution in PBS, pH 7.4.
|Less than 0.01 EU/ug of rHuNRG1-beta2 GMP as determined by LAL method.
|We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
|Stability and 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 to -70 °C under sterile conditions after reconstitution.
|Safety Data Sheet (SDS) Download
|Click to download
|Technical Data Sheet (TDS) Download
|Click to download