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Merck
모든 사진(1)

주요 문서

E1780

Sigma-Aldrich

Anti-phospho-Epidermal Growth Factor Receptor (pTyr992) antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

동의어(들):

Anti-phospho-EGFR (pTyr992)

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About This Item

MDL number:
UNSPSC 코드:
51111800
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

양식

buffered aqueous glycerol solution

분자량

antigen ~185 kDa

종 반응성

mouse (predicted), human, rat (predicted), chicken (predicted)

기술

western blot: 1:1,000 using human epidermoid carcinoma A431 cells

UniProt 수납 번호

배송 상태

wet ice

저장 온도

−20°C

유전자 정보

human ... EGFR(1956)
mouse ... Egfr(13649)
rat ... Egfr(24329)

일반 설명

The members of epidermal growth factor receptor (EGF R) or the ErbB receptor family have been identified as useful biomarkers and targets for cancer therapy. The EGFR family includes four receptor tyrosine kinases, EGF R (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. EGF R binds EGF and induces tyrosine phosphorylation leading to proliferation of cells. EGF R is present on many cell types of epithelial and mesenchymal lineages. EGF R is capable of binding transforming growth factor-α and heparin-binding EGF in addition to EGF. There are numerous effector molecule activated by EGF R that result in a variety of biological processes such as morphogenesis, cell motility, apoptosis, differentiation and organ repair and maintenance. Deregulation of EGF R signaling is implicated in progression of a wide variety of tumors, invasion and metastasis. Tyrosine 992 of EGF R is autophosphorylation site and required for increasing the signalling capacity of EGF R
Anti-phospho-EGFR [pTyr992] specifically recognizes human EGFR phosphorylated at tyrosine 992 (~185 kDa). Cross reactivity may be observed with mouse, rat and chicken.

면역원

synthetic phosphopeptide derived from the region of human EGFR that contains tyrosine 992. The sequence is conserved in mouse and rat with 100% homology. Chicken EGFR is 80% homologous.

애플리케이션

Anti-phospho-EGFR [pTyr992] antibody may be used at a working dilution of 1:1000 for immunoblotting using A431 cells.

물리적 형태

Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+) containing 50% glycerol with 1 mg/mL BSA (protease and IgG-free) and 0.05% sodium azide.

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Storage Class Code

10 - Combustible liquids


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문서 라이브러리 방문

Nicole K Nickerson et al.
Oncology research, 20(7), 303-317 (2013-07-25)
Epidermal growth factor receptor (EGFR) expression has been linked to progression of basal breast cancers. Many breast cancer cells harbor the EGFR and produce its family of ligands, suggesting they may participate in autocrine and paracrine signaling with cells of
H Keilhack et al.
The Journal of biological chemistry, 273(38), 24839-24846 (1998-09-12)
The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates the epidermal growth factor receptor (EGFR), and both SH2 domains of SHP-1 are important for this interaction (Tenev, T., Keilhack, H., Tomic, S., Stoyanov, B., Stein-Gerlach, M., Lammers, R., Krivtsov, A. V.
Parthasarathy Seshacharyulu et al.
Expert opinion on therapeutic targets, 16(1), 15-31 (2012-01-14)
Cancer is a devastating disease; however, several therapeutic advances have recently been made, wherein EGFR and its family members have emerged as useful biomarkers and therapeutic targets. EGFR, a transmembrane glycoprotein is a member of the ERBB receptor tyrosine kinase
A Wells
The international journal of biochemistry & cell biology, 31(6), 637-643 (1999-07-15)
The receptor for the epidermal growth factor (EGF) and related ligands (EGFR), the prototypal member of the superfamily of receptors with intrinsic tyrosine kinase activity, is widely expressed on many cell types, including epithelial and mesenchymal lineages. Upon activation by
Rachana Patel et al.
Current pharmaceutical design, 18(19), 2672-2679 (2012-03-07)
Members of epidermal growth factor receptor (EGFR) or ErbB receptor family play a critical role in a wide range of human cancers. In the past decade, there has been a remarkable progress in developing ErbB targeted therapeutics. However, a substantial

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