Recombinant Human Epigen
(rHuEPG)
Catalog Number: C22-105-06
Source: Escherichia coli.
Molecular Weight: Approximately 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the
EGF homologous portion of the Epigen precursor.
Quantity: 5μg/25μg/1000μg
AA Sequence: AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG
ERCEHLTLTS YA
Purity: >98% by SDS-PAGE and HPLC analyses.
Biological Activity: Fully biologically active when compared to standard. The ED50 determined by a cell proliferation
assay using murine Balb/c 3T3 cells is less than 300 ng/ml, corresponding to a specific activity of> 3.3 × 103 IU/mg.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Endotoxin: Less than 1EU/μg of rHuEPG as determined by LAL method.
Reconstitution: 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.
Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage,
preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For
maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to
-70°C. Avoid repeated freeze/thaw cycles.
Usage: This material is offered by Shanghai Corning Bio-Tech for research, laboratory or further
evaluation purposes. NOT FOR HUMAN USE.
Human Epigen
Epigen (EPG) is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several
tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human
Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic
cleavage to produce a mature soluble sequence.