biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
FB343, monoclonal
form
buffered aqueous solution
mol wt
antigen ~60 kDa
species reactivity
rat, human, mouse
packaging
antibody small pack of 25 μL
concentration
~2 mg/mL
technique(s)
immunocytochemistry: 10-20 μg/mL using human A431 cells, indirect ELISA: suitable, western blot: 5-10 μg/mL using human A431 cell extracts
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... FBXW7(55294)
mouse ... Fbxw7(50754)
General description
FBXW7 is a F-box protein that facilitates as a substrate recognition component of the ubiquitin ligase complex SCF (Skp-Cullin-F-box). FBXW7 exist in three isoforms α, β and γ. It is composed of a conserved F-box domain at their N terminus, which interacts with Skp1. C terminus consist of one or several highly variable protein-protein interaction domains such as Leu-rich repeat (LRR), kelch repeat, tetratricopeptide repeat (TPR), and WD40 repeat.
Immunogen
synthetic peptide corresponding to amino-acids 13-27 of human hFBXW7γ isoform.
Application
Monoclonal Anti-hFBXW7γ antibody is suitable for:-
- Immunocytochemistry at a concentration of 10-20μg/mL using human A431 cells.
- Western blot at a concentration of 5-10μg/mL using human A431 cell extracts.
- Indirect ELISA.
Biochem/physiol Actions
FBXW7 protein is highly involved in the ubiquitination of cyclin E , Notch , c-Jun and c-Myc. It acts as a key component of phosphoepitope-specific substrate recognition complex of SCF ubiquitin ligases to facilitate the recognition of phosphorylated targets such as cyclin E, myc, c-Jun, and Notch. The SV40 large T antigen binds FBXW7 without detectible effects on its stability to acts as an inhibitor of FBXW7 activity.It has been reported that FBXW7 controls c-Myc′s growth-promoting activity followed by cell size, which is an important event of Fbw7 loss in cancers.
Physical form
0.01M 磷酸缓冲盐溶液,pH 7.4,含 15mM 叠氮化钠。
Disclaimer
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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存储类别
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Mukesh Jain et al.
Plant physiology, 143(4), 1467-1483 (2007-02-13)
F-box proteins constitute a large family in eukaryotes and are characterized by a conserved F-box motif (approximately 40 amino acids). As components of the Skp1p-cullin-F-box complex, F-box proteins are critical for the controlled degradation of cellular proteins. We have identified
Nicole E Willmarth et al.
Breast cancer research : BCR, 6(5), R531-R539 (2004-08-21)
Cyclin E, a G1 cyclin essential for G1-S phase transition, is known to have a profound effect on tumorigenesis. Elevated levels of cyclin E have been associated with breast cancer, and chromosomal instability observed in breast cancer is suggested to
Harith Rajagopalan et al.
Nature, 428(6978), 77-81 (2004-03-06)
Aneuploidy, an abnormal chromosome number, has been recognized as a hallmark of human cancer for nearly a century; however, the mechanisms responsible for this abnormality have remained elusive. Here we report the identification of mutations in hCDC4 (also known as
Markus Welcker et al.
Current biology : CB, 14(20), 1852-1857 (2004-10-23)
The human tumor suppressor Fbw7/hCdc4 functions as a phosphoepitope-specific substrate recognition component of SCF ubiquitin ligases that catalyzes the ubiquitination of cyclin E , Notch , c-Jun and c-Myc . Fbw7 loss in cancer may thus have profound effects on
Masayoshi Yada et al.
The EMBO journal, 23(10), 2116-2125 (2004-04-23)
The F-box protein Skp2 mediates c-Myc ubiquitylation by binding to the MB2 domain. However, the turnover of c-Myc is largely dependent on phosphorylation of threonine-58 and serine-62 in MB1, residues that are often mutated in cancer. We now show that
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