Recombinant Human EGF (E. coli)
|Description||Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell growth, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), which is a competitor for EGF receptor sites. EGF receptors are expressed in almost all types of tissues. Parietal endoderm, mature skeletal muscles, and hematopoietic tissues do not express the receptor. The EGF receptor, designated HER1, is a 170 kDa transmembrane glycoprotein with a length of 1186 amino acids. It is identical with a previously described glycoprotein called SA-7 (species antigen 7). The extracellular receptor domain has a length of 621 amino acids, including 11 glycosylated asparagine residues and 51 cysteine residues. This domain contains the EGF binding site and also binds mammalian TGF-alpha.|
|Species||Human (H. sapiens)|
|Molecular Weight||6.5 kDa|
|Endotoxin Level||<1.0 EU/µg of recombinant protein as determined by the LAL method|
|Purity||>95% as determined by SDS-PAGE|
|Formulation||Recombinant Epidermal Growth Factor was lyophilized from a 0.2 μm filtered solution in PBS.|
|Function||The ED50 was determined by a cell proliferation assay using human epithelial cell line and found to be <0.2ng/ml.|
A quick spin of the vial followed by reconstitution in sterile distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
|Storage||The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable lo|
|Usage||For research use only. Not for diagnostic or therapeutic use.|
- Growth Factor eFlyer
- Growth Factor and Cytokine Brochure
- Active Kinases Brochure
- Growth Factors and Cytokines Catalogue
- Growth Factors and Cytokines FAQ
- Role of Growth Factors in Cell Differentiation (Poster)
|How are endotoxin levels measured?|
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970. · Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL). · For recombinant proteins: EU is reported per microgram of protein. · One EU = 0.1-0.2 ng endotoxin/µg of protein. · At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
|With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?|
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
|Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?|
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.
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