EGF Mouse

Epidermal Growth Factor Mouse

Epidermal Growth Factor Mouse, purified from the submaxillary gland, is a single-chain polypeptide with a glycosylation modification. It has a molecular weight of 6.1 kDa. The purification process of EGF involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3264
Source
Mouse Submaxillary Gland.
Appearance
White powder, sterile-filtered, and lyophilized (freeze-dried).

EGF Mouse Protein

Epidermal Growth Factor Mouse Recombinant

Recombinant Mouse Epidermal Growth Factor, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 53 amino acids. It contains 3 intramolecular disulfide bonds and has a molecular weight of 6 kDa. This EGF product is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3344
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder, sterile and filtered.

EGF Mouse, Biotin

Epidermal Growth Factor Mouse Recombinant, Biotin

Recombinant Mouse EGF, Biotinylated, produced in E. coli, is a non-glycosylated polypeptide chain comprising 61 amino acids with a molecular weight of 7.0 kDa. This variant of EGF features an N-terminal leader sequence designed for biotin conjugation, with an average of 0.5 biotins per EGF protein.
Shipped with Ice Packs
Cat. No.
BT3410
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

EGF (1-51), Human

Epidermal Growth Factor (1-51 a.a.)Human Recombinant

This product is a recombinant human Epidermal Growth Factor (EGF) comprising amino acids 1-51. It is produced in yeast and purified as a single, glycosylated polypeptide chain with a molecular weight of 6.0 kDa. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT2934
Source

Saccharomyces cerevisiae

Appearance

Sterile, lyophilized powder with a white color.

EGF (Leu 21) Human

Epidermal Growth Factor (Leu-21) Human Recombinant

EGF 21-Leu Human Recombinant, produced in E. coli, is a single-chain polypeptide that lacks glycosylation. It consists of 53 amino acids, resulting in a molecular mass of 6205 Daltons. The purification process of EGF 21-Leu involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3031
Source
Escherichia Coli.
Appearance
The product appears as a white powder that has been sterilized through filtration and lyophilized (freeze-dried).

EGF Human

Epidermal Growth Factor Human Recombinant

Recombinant Human Epidermal Growth Factor, generated using E.Coli as an expression system, is a single-chain polypeptide that lacks glycosylation. It consists of 53 amino acids, resulting in a molecular weight of 6.2kDa. The purification of EGF is achieved through specialized chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT3108
Source
Escherichia Coli.
Appearance
The product appears as a white powder, sterilized through filtration and lyophilized (freeze-dried).

EGF Human, Pichia

Epidermal Growth Factor Human Recombinant, Pichia

Recombinant Human Epidermal Growth Factor, produced in Pichia Pastoris, is a single, glycosylated polypeptide chain with a molecular weight of 6 kDa, comprising 51 amino acids. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3164
Source
Pichia Pastoris.
Appearance
White, sterile-filtered lyophilized powder.

EGF Long Human

Epidermal Growth Factor Long Human Recombinant

Produced in E.coli cells, Recombinant Human EGF Long is a non-glycosylated polypeptide chain composed of 106 amino acids, with a molecular weight of 12.3kDa. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3222
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

MFGE8 Mouse

Milk Fat Globule-EGF Factor 8 Protein Mouse Recombinant

Recombinant MFGE8 Mouse protein, expressed in Sf9 insect cells using a baculovirus system, is a single-chain polypeptide. It undergoes glycosylation, a process of adding sugar molecules, and consists of 413 amino acids (specifically, amino acids 23 to 426). This protein has a molecular weight of 46 kDa, but on SDS-PAGE analysis, it appears as a band around 40-57 kDa. This discrepancy in size is due to glycosylation. For purification and later applications, a 6 amino acid His-tag is added at the C-terminus of the protein. The purification process utilizes proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT2806
Source
Sf9, Baculovirus cells.
Appearance
A clear and colorless solution that has been sterilized by filtration.

EGF Rat

Epidermal Growth Factor Rat Recombinant

Recombinant Rat Epidermal Growth Factor, produced in E. coli, is a single-chain polypeptide that lacks glycosylation. It comprises 53 amino acids, resulting in a molecular weight of 6151 Daltons. The purification process of Rat EGF involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3957
Source
Escherichia Coli.
Appearance
White, lyophilized powder that has been sterile filtered.
Definition and Classification

Epidermal Growth Factor (EGF) is a protein that stimulates cell growth, proliferation, and differentiation by binding to its receptor, EGFR (Epidermal Growth Factor Receptor). It was first discovered in the submaxillary glands of mice and later found in human urine . EGF is classified as a polypeptide growth factor and is part of a larger family of growth factors that includes Transforming Growth Factor-alpha (TGF-α) and Heparin-binding EGF-like growth factor (HB-EGF) .

Biological Properties

Key Biological Properties: EGF is a small protein composed of 53 amino acids and has a molecular weight of approximately 6 kDa. It contains three intramolecular disulfide bonds that are crucial for its stability and function .

Expression Patterns: EGF is expressed in various tissues, including the submandibular and parotid glands, platelets, urine, saliva, milk, tears, and blood plasma . It is also found in the brain, where it plays a role in neurogenesis .

Tissue Distribution: EGF is widely distributed in the body and can be found in multiple tissues and fluids, including the gastrointestinal tract, liver, kidneys, and skin .

Biological Functions

Primary Biological Functions: EGF primarily stimulates cell growth, proliferation, and differentiation. It plays a crucial role in wound healing by promoting the proliferation of epithelial cells . EGF also influences the development of various tissues and organs, including the lungs, kidneys, and reproductive system .

Role in Immune Responses and Pathogen Recognition: EGF has been shown to modulate immune responses by influencing the activity of various immune cells. It can enhance the proliferation and differentiation of T cells and macrophages, thereby playing a role in pathogen recognition and immune defense .

Modes of Action

Mechanisms with Other Molecules and Cells: EGF exerts its effects by binding to the EGFR on the cell surface. This binding induces dimerization of the receptor, leading to its activation . The activated EGFR then triggers a cascade of downstream signaling pathways, including the MAPK/ERK, PI3K/Akt, and JAK/STAT pathways .

Binding Partners and Downstream Signaling Cascades: EGF interacts with various binding partners, including PLCγ (phospholipase C-γ), PLD (phospholipase D), and STAT (signal transducer and activator of transcription) proteins . These interactions lead to the activation of multiple signaling cascades that regulate cell proliferation, survival, and differentiation .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of EGF are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors that bind to the promoter region of the EGF gene . Post-translational modifications, such as phosphorylation and glycosylation, also play a crucial role in modulating the activity and stability of EGF .

Transcriptional Regulation and Post-Translational Modifications: EGF gene expression is regulated by several transcription factors, including Sp1 and AP-2 . Post-translational modifications, such as phosphorylation by protein kinases, can enhance or inhibit the activity of EGF .

Applications

Biomedical Research: EGF is widely used in biomedical research to study cell growth, differentiation, and signaling pathways. It is also used in tissue engineering and regenerative medicine to promote wound healing and tissue repair .

Diagnostic Tools: EGF and its receptor, EGFR, are used as biomarkers in the diagnosis and prognosis of various cancers, including lung, breast, and colorectal cancers .

Therapeutic Strategies: EGF has therapeutic applications in the treatment of chronic wounds, such as diabetic foot ulcers and pressure ulcers. It is also being explored as a potential treatment for neurodegenerative diseases and certain types of cancer .

Role in the Life Cycle

Role Throughout the Life Cycle: EGF plays a vital role throughout the life cycle, from development to aging and disease. During embryonic development, EGF is essential for the proliferation and differentiation of various cell types . In adults, EGF continues to play a role in tissue maintenance and repair . Dysregulation of EGF signaling has been implicated in aging and the development of age-related diseases, such as cancer and neurodegenerative disorders .

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