EGF Polyclonal Antibody (AN007200L)
For research use only.
| Verified Samples | Verified Samples in WB: Rat kidney |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human EGF protein expressed by Mammalian |
| Abbre | EGF |
| Synonyms | HOMG, EGF, HOMG4, URG, Beta urogastrone, beta-urogastrone, Epidermal growth factor, OTTHUMP00000219721, OTTHUMP00000219722, Pro epidermal growth factor, Pro-Epidermal Growth Factor, Urogastrone |
| Swissprot | |
| Calculated MW | 133 kDa |
| Observed MW |
80 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Secreted, Cell membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Research Areas | Signal Transduction, Cell Biology, Cancer, Kits, Lysates, Other |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
| background | Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through -6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intramolecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. These receptors undergo a complex pattern of ligand induced homo- or hetero-dimerization to transduce EGF family signals . EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Dimerization results in autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a variety of signaling molecules. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. |
Other Clones
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Unconjugated
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