KLH-conjugated synthetic peptide encompassing the surrounding amino acids of Tyr 845 in human EGFR.
애플리케이션
Detect phospho-EGFR (Tyr845) using this Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3 validated for use in ELISA, IC, IP & WB.
Research Category Signaling
Research Sub Category Growth Factors & Receptors
품질
Routinely evaluated by immunoblot.
표적 설명
180 kDa
물리적 형태
100 µg of mouse monoclonal IgG1 lyophilized in 2X PBS containing 0.09% sodium azide, PEG, and sucrose
Format: Purified
Subsequent thiophilic adsorption and size exclusion chromatography
저장 및 안정성
2 years at -20°C from date of shipment
분석 메모
Control Includes EGF treated Hep2G cell lysate as a positive control
법적 정보
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
면책조항
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Combinatorial post-translational modifications (PTMs), which can serve as dynamic "molecular barcodes", have been proposed to regulate distinct protein functions. However, studies of combinatorial PTMs on single protein molecules have been hindered by a lack of suitable analytical methods. Here, we
The Journal of biological chemistry, 277(11), 9405-9414 (2002-01-05)
Integrin-mediated cell adhesion cooperates with growth factor receptors in the control of cell proliferation, cell survival, and cell migration. One mechanism to explain these synergistic effects is the ability of integrins to induce phosphorylation of growth factor receptors, for instance
Molecular and cellular biology, 24(16), 7059-7071 (2004-07-30)
When co-overexpressed, the epidermal growth factor receptor (EGFR) and c-Src cooperate to cause synergistic increases in EGF-induced DNA synthesis, soft agar colony growth, and tumor formation in nude mice. This synergy is dependent upon c-Src-mediated phosphorylation of a unique tyrosine
Post-translational modifications (PTMs) of receptor tyrosine kinases (RTKs) at the plasma membrane (PM) determine the signal transduction efficacy alone and in combination. However, current approaches to identify PTMs provide ensemble results, inherently overlooking combinatorial PTMs in a single polypeptide molecule.
The Journal of biological chemistry, 274(12), 8335-8343 (1999-03-13)
Accumulating evidence indicates that interactions between the epidermal growth factor receptor (EGFR) and the nonreceptor tyrosine kinase c-Src may contribute to an aggressive phenotype in multiple human tumors. Previous work from our laboratory demonstrated that murine fibroblasts which overexpress both