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Merck

D2178

Sigma-Aldrich

Monoclonal Anti-Death Associated Protein Kinase antibody produced in mouse

clone DAPK-55, ascites fluid

Synonim(y):

Anti-DAP Kinase

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About This Item

Numer MDL:
Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

mouse

Poziom jakości

białko sprzężone

unconjugated

forma przeciwciała

ascites fluid

rodzaj przeciwciała

primary antibodies

klon

DAPK-55, monoclonal

masa cząsteczkowa

antigen 160 kDa

zawiera

15 mM sodium azide

reaktywność gatunkowa

human, monkey

metody

immunoprecipitation (IP): suitable
microarray: suitable
western blot: 1:250 using COS-7 cell extract

izotyp

IgG1

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... DAP(1611)

Opis ogólny

Monoclonal Anti-Death Associated Protein (DAP) Kinase (mouse IgG1 isotype) is derived from the DAPK-55 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Death-associated protein 1 (DAP1) gene is mapped to human chromosome 9q34.1. It belongs to the DAP family.
The gene is widely expressed in many tissues of embryonic and adult origin and gives rise to a single 6.3 Kb mRNA transcript. The protein consists of 1423 amino acids (160 kDa) and belongs to a family of calmodulin-dependent protein kinases. It contains 8 ankyrin repeats and 2 potential P-loop motifs apart from the kinase domain and the calmodulin regulatory domain.

Immunogen

recombinant human DAP kinase expressed in bacteria.

Zastosowanie

Monoclonal Anti-Death Associated Protein Kinase antibody produced in mouse has been used in immunoblotting and immunoprecipitation.

Działania biochem./fizjol.

DAP-kinase is a novel, structurally unique, human serine/threonine kinase identified as a positive mediator of interferon-γ-induced programmed cell death. It has an intrinsic kinase activity towards itself that is regulated by calmodulin and calcium.
Death-associated protein 1 (DAP1) participates in the regulation of cell growth and death including that of cancer cells. DAP-kinase has an intrinsic kinase activity towards itself that is regulated by calmodulin and calcium.

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

nwg

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Death-associated protein kinase increases glycolytic rate through binding and activation of pyruvate kinase
Mor I, et al.
Oncogene, 31(6), 683-683 (2012)
B Inbal et al.
Nature, 390(6656), 180-184 (1997-11-21)
DAP kinase is a new type of calcium/calmodulin-dependent enzyme that phosphorylates serine/threonine residues on proteins. Its structure contains ankyrin repeats and the 'death' domain, and it is associated with the cell cytoskeleton. The gene encoding DAP kinase was initially isolated
The role of DAPK-BimEL pathway in neuronal death induced by oxygen-glucose deprivation
He C, et al.
Neuroscience, 258(6), 254-262 (2014)
Barbara Geering et al.
Journal of leukocyte biology, 95(2), 293-303 (2013-10-29)
The tight regulation of granulocyte chemotaxis is crucial for initiation and resolution of inflammation. Here, we show that DAPK2, a Ca(2+)/CaM-sensitive serine/threonine kinase known to modulate cell death in various cell types, is a novel regulator of migration in granulocytes.
KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated PML and DAPK ubiquitination
Chen HY, et al.
Oncogene, 34(40), 5141-5141 (2015)

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