Data & Images
|Product Name||Anti-EGFR Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Epidermal growth factor receptor(EGFR) detection. Tested with WB in Human;Rat.|
|Cite This Product||Anti-EGFR Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9016)|
|Replacement Item||This antibody may replace the following items: sc-101|sc-31155|sc-53274|sc-80543|sc-365829|sc-31156|sc-31157|sc-373746|sc-120|sc-71032|sc-71033|sc-71035|sc-71034|sc-15827|sc-15828|sc-33746|sc-377073|sc-374607|sc-377229|sc-03|sc-367974|sc-514994|sc-514995 from Santa Cruz Biotechnology.|
|Validated Species||Human, Rat|
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||E.coli-derived human EGFR recombinant protein (Position: L25-K346). Human EGFR shares 89% amino acid (aa) sequence identity with mouse EGFR.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20˚C for one year. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Epidermal growth factor receptor|
|Molecular Weight||134277 MW|
|Protein Function||Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS- RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.|
|Tissue Specificity||Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. .|
|Sequence Similarities||Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.|
|Subcellular Localization||Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome. Endosome membrane. Nucleus. In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF).|
|Alternative Names||Epidermal growth factor receptor;220.127.116.11;Proto-oncogene c-ErbB-1;Receptor tyrosine-protein kinase erbB-1;EGFR;ERBB, ERBB1, HER1;|
|Research Areas|||signal transduction|protein phosphorylation|tyrosine kinases|receptor tyrosine kinases| signal transduction|growth factors/hormones|egf| cancer|oncoproteins/suppressors|oncoproteins|growth factor receptors|tumor biomarkers||
Background for Epidermal growth factor receptor
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-EGFR Picoband™ Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Western blot, 0.1-0.5μg/ml, Human, Rat|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-EGFR Picoband™ Antibody Images
Click the images to enlarge.
All lanes: Anti-EGFR(PB9016) at 0.5ug/ml
Lane 1: HELA Whole Cell Lysate at 40ug
Lane 2: A549 Whole Cell Lysate at 40ug
Lane 3: A431 Whole Cell Lysate at 40ug
Predicted bind size: 134KD
Observed bind size: 200KD
- Review by Elena Deryugina
"I would highly recommend this Boster antibody..."
--Elena Deryugina, CELL AND MOLECULAR BIOLOGY, THE SCRIPPS RESEARCH INSTITUTE, ASSISTANT PROFESSOR
Applications Western Blot Sample Recombinant N-Terminal domain of human EGFR (aa 1-621) tested at 100 ng/lane Detection SuperSignal West Pico Chemiluminescent Substrate
"Rabbit antibody PB9016 from Boster was probed for western blot detection of the recombinant N-terminal domain of human EGFR (100 ng/lane). The antibody nicely detected the protein band with the expected mol.wt. of recombinant protein. The antibody appears to be specific since non-specific bands were not detected in parallel lanes with cell lysates lacking EGFR. I would highly recommend this Boster antibody for detection of EGFR with the intact N-terminal domain."
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,