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D3570

Sigma-Aldrich

Anti-DVL1 antibody produced in rabbit

enhanced validation

~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution, antigen mol wt ~85 kDa

Sinonimo/i:

Anti-Dishevelled-1, Anti-Dsh homolog 1, Anti-Segment polarity protein dishevelled homolog

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen ~85 kDa

Reattività contro le specie

human

Convalida avanzata

recombinant expression
Learn more about Antibody Enhanced Validation

Concentrazione

~1.5 mg/mL

tecniche

western blot: 1-2 μg/mL using HEK-293T cell lysate expressing human DVL1

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... DVL1(1855)

Descrizione generale

The three DVL isoforms display high sequence homology and have conserved DIX, PDZ and DEP domains required for GSK3β inactivation. DVL1 is highly expressed in adult and fetal tissues such as skeletal muscle and pancreas but is also found in the brain and neural tube.

Applicazioni

Anti-DVL1 antibody produced in rabbit has been used in immunoblotting and immunohistochemistry (IHC).

Azioni biochim/fisiol

Dishevelled (Dsh, DVL) proteins are part of a multigene family that mediate wnt signaling pathways that are essential for the regulation of cellular proliferation, differentiation, motility, and morphogenesis. DVL1 regulates the activity of JNK (c-Jun N-terminal kinase) and GSK3β in the wnt signaling pathway. Upon activation of the wnt signaling pathway, DVL1 inactivates GSK3β through complex formation with APC (Antigen-presenting cell), β-catenin and axin proteins, releasing β-catenin from degradation. In neurons, DVL1 is localized to axonal microtubules and stabilizes microtubules by inhibiting the GSK3β mediated phosphorylation of MAP-1B.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Certificati d'analisi (COA)

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Dong Chen et al.
International journal of clinical and experimental pathology, 6(9), 1791-1798 (2013-09-17)
Hirschsprung's disease (HSCR) is a congenital disorder of the enteric nervous system and is characterized by an absence of enteric ganglion cells in terminal regions of the gut during development. Dishevelled (DVL) protein is a cytoplasmic protein which plays pivotal
DVL1 and DVL3 differentially localize to CYP19A1 promoters and regulate aromatase mRNA in breast cancer cells
Castro PI, et al.
Oncotarget, 9(86), 35639-35639 (2018)
ALFY-Controlled DVL3 Autophagy Regulates Wnt Signaling, Determining Human Brain Size
Kadir R, et al.
PLoS Genetics, 12(3), e1005919-e1005919 (2016)
L Li et al.
The Journal of biological chemistry, 274(1), 129-134 (1998-12-29)
Dishevelled (Dsh/Dvl) proteins are known to mediate Wnt signaling by up-regulating beta-catenin levels and stimulating T cell factor (TCF)/LEF-1-dependent transcription. We have identified a new Dvl-mediated signaling pathway in that mouse Dvl proteins, when expressed in COS-7 cells, stimulate c-Jun-dependent
Monica Sharma et al.
Genes & cancer, 12, 77-95 (2021-10-19)
Dishevelled-1 (DVL-1) mediates Wnt signals critical for development and cellular homeostasis. DVL-1 is also linked with tumorigenesis, however its association with specific breast cancer (BC) subtypes and how it contributes to tumorigenicity remains poorly studied. Herein, using bioinformatics and genomics

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