Recombinant Mouse EGF Protein (His Tag)

Name: Recombinant Mouse EGF Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1718
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant epidermal growth factor (egf) proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Mouse
Accession	AAH60741.1
Synonym	AI790464
Background	EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 645-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.
Description	A DNA sequence encoding the mouse Egf (AAH60741.1) (Met1-Arg1029) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Trp 29
AA Sequence	Met1-Arg1029
Molecular Weight	The recombinant mouse Egf consists 1012 a.a. and predicts a molecular mass of 111.3 kDa.
Purity	>90% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	KEGG: mmu:13645 STRING: 10090.ENSMUSP00000029653 UniGene: Mm.252481

Gene Functions References

In mice, both EGF and pimecrolimus groups showed less erythema with significantly reduced inflammation and decreased expression of thymic stromal lymphopoietin. EGF relieved S. aureus-induced inflammation and AD-like skin lesions in Nc/Nga mice. PMID: 29862299
hijacks miR-198/FSTL1 wound-healing switch and steers a two-pronged pathway toward metastasis PMID: 28827448
These results indicate that Kindlin-1 is essential in EGF-induced re-epithelialization in skin wound healing and provide additional rationale for the clinical application of EGF in the treatment of acute wounds. PMID: 28290610
concentration of EGF is critical for the switch between hair follicle growth and inhibition, and EGF promotes DP cell proliferation via Notch signaling pathway PMID: 27109378
EGF promotes FoxM1 expression through the ERK signal pathway PMID: 26022336
Data indicate that Sonic hedgehog (Shh) stimulate branching morphogenesis (BrM) and induced synthesis of mRNAs for Ptch1 protein, epidermal growth factor (EGF) and receptors of the ErbB receptors ErbB1, ErbB2 and ErbB3. PMID: 26930157
Either LIF or EGF is needed during development of pre-implantation embryo. PMID: 27096934
PXR activation stimulates EGF-mediated hepatocyte proliferation in mice, at least in part, through inhibiting FOXO3 from accelerating cell-cycle progression. PMID: 26574435
Data (including data from studies in knockout mice) suggest that Epab (embryonic poly(A)-binding protein), which is oocyte specific, is required for ability of cumulus cells and granulosa cells to exhibit responsiveness to Egf/Egfr signaling. PMID: 26492470
modulation of EGF signaling affects in vitro expansion and differentiation of progenitors from embryonic pancreas of both mice and man. PMID: 25925840
TLR4 blockade prevented TPN-associated intestinal mucosa atrophy by preserving proliferation and preventing apoptosis. This is driven by a reduction in TNF-alpha abundance and increased EGF. PMID: 25782989
EGF is required for cardiac differentiation of P19CL6 cells through interaction with GATA-4 in a time- and dose-dependent manner. PMID: 25504289
These data demonstrate that Mcl-1 is essential for mammopoiesis and identify EGF as a critical trigger of Mcl-1 translation to ensure survival of milk-producing alveolar cells. PMID: 25730472
results indentify EGF signalling as a robust vasculogenic inductive pathway for ATMCs, leading to their transdifferentiation into functional VSMC-like cells. PMID: 24967966
MEKK1 PHD controls p38 and JNK activation during TGF-beta, EGF and microtubule disruption signalling, but does not affect MAPK responses to hyperosmotic stress. PMID: 25260751
VEGFR1-mediated signaling plays a critical role in gastric ulcer healing and angiogenesis through enhanced EGF expression on VEGFR1+CXCR4+ cells PMID: 23982810
The combination of EGF-FGF2 stimulates the proliferation. PMID: 24907656
IL-6 may act as a new potential cumulus expansion-related transcript, which may be involved in the integration of TrkA and EGF signaling in affecting expansion of cumulus oocyte complexes. PMID: 24215827
EGF treatment increases Cx43 phosphorylation up to 4-fold and induces efficient gap junction endocytosis. PMID: 24492000
A previously unrecognized protective role is played by EGF in atopic dermatitis. EGF also has a new role in modulating IL-17 responses in the skin. PMID: 24337738
Insulin treatment resulted in increased vascular leakage apparently mediated by betacellulin and signaling via the epidermal growth factor (EGF) receptor. PMID: 23831329
While EGF activated Gab1 and Shc equally, within the same concentration range, HGF very potently and almost exclusively activated Gab1, having only a minimal effect on Shc PMID: 24126105
These results support the argument that aberrant hyper-signals of EGF have significant impact on mouse behavioral traits and dopamine metabolism. PMID: 23669645
Data indicate that LTB4 receptor type 1 (BLT1)-knockout mice showed delayed liver repair and a 70-80% attenuation in expression of epidermal growth factor (EGF), vascular endothelial growth factor (VEGF), and VEGF receptor 1 (VEGFR1). PMID: 23629862
Data suggest Egf/Egf receptor signaling in cumulus cells (CC) downregulates Npr2 (natriuretic peptide receptor 2), decreases cGMP, elevates calcium, and induces meiotic resumption/oogenesis in cultured CC-oocyte complexes (in induced meiotic arrest). PMID: 23787120
EGF and insulin/IGF prime endometrial epithelial cells to direct the mitogenic effects of estradiol. Furthermore, PTEN deficiency results in enhanced responsiveness to this combination, leading to hyperplasia of endometrial cells. PMID: 23669345
Upregulation of endogenous EGF may act on top of an endocrinous cascade orchestrating the interactions between Sertoli cells and germ cells and may operate as defensive mechanism in response to testicular ischemia/reperfusion stress. PMID: 23241343
study elucidated a previously unknown function of EGF in promoting hematopoietic stem cell regeneration after radiation-induced myelosuppression PMID: 23377280
Suggest that FAK acts as a central coordinator of integrin and growth factor-mediated S-phase entry by regulating Cdk2 in EGF-stimulated hepatocytes. PMID: 23168795
a novel link between EGF receptor stimulation, ILK-containing complexes, and activation of small Rho GTPases necessary for acquisition of front-rear polarity and forward movement PMID: 22160594
The effects of EGF, insulin, and insulin-like growth factor (IGF)-1 correlate with reactive oxyen species (ROS) production in kidney cortical collecting duct cells. PMID: 23135700
nucleobindin-2 regulates EGF-stimulated MAPK kinase/Erk signaling, cell proliferation, and adipocyte differentiation PMID: 22514047
Neurotensin increases EGF expression in skin dendritic cells. PMID: 21767580
It was suggested that, in this in vitro mouse model, EGF signaling during ovulation might protect the cumulus cells from the potential luteinizing effects of LH. PMID: 21293035
Enteric glia promote intestinal mucosal healing via activation of focal adhesion kinase and release of proEGF. PMID: 21350188
Rac1 through NADPH oxidase is part of the signaling pathway constituted by FAK, Rac1, and ERK that regulates focal adhesion disassembly during cell spreading. PMID: 21660950
A switch in autocrine signaling to foster tumor growth that was initially triggered by EGF. PMID: 21464922
The Tgf-beta(3) null mutant mouse palate presents several cellular anomalies that lead to the appearance of cleft palate reveals misexpression of EGF and Msx-1. PMID: 20881363
Proprotein convertase PC7 enhances the activation of the EGF receptor pathway through processing of the EGF precursor. PMID: 21209099
EGF signaling is indispensable for activation of proliferation and inhibition of unexpected cell death in intestinal epithelial cells PMID: 20714325
EGF-induced MAPK signaling inhibits hemidesmosome formation through phosphorylation of the integrin beta 4. PMID: 20870721
EGF/EGR-1 repressed transcriptional activation of the MMP-9 gene by stromal cells. PMID: 20472833
7,3',4'-Trihydroxyisoflavone inhibits epidermal growth factor-induced cell proliferation and transformation by suppressing cyclin-dependent kinases and phosphatidylinositol 3-kinase PMID: 20444693
Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition PMID: 20392696
regulation of beta1-integrin expression/localization is involved in cellular processes, such as proliferation, induced by bFGF and EGF in mouse neuroepithelial cells PMID: 20371608
conclude that neural stem/progenitor cell subpopulations reside in neurospheres that are distinguishable by their responsiveness to fibroblast growth factor-2 and EGF which is differentially regulated by chondroitin sulfate-carbohydrate structures. PMID: 20087964
Palmitoylated EGFR exhibited only low-affinity EGF binding and impaired signal transduction. PMID: 19196031
GH modulates EGF signaling in the liver. PMID: 20032199
EGF is a key regulator of cell growth and development and a sevenfold increase is shown in EGF expression in FVB compared to B10.Q mice. PMID: 20080754
Absence of post-translational aspartyl beta-hydroxylation of domains in mice leads to developmental defects and an increased incidence of intestinal neoplasia PMID: 11773073

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.