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Merck

SAB4300122

Sigma-Aldrich

Anti-phospho-TYK2 (pTyr1054) antibody produced in rabbit

affinity isolated antibody

Synonym(e):

Anti-JTK1 antibody produced in rabbit, Anti-tyrosine kinase 2 antibody produced in rabbit

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

~140 kDa

Speziesreaktivität

human, rat, mouse

Konzentration

1 mg/mL

Methode(n)

western blot: 1:500-1:1000

Isotyp

IgG

Immunogene Sequenz

(H-E-YP-Y-R)

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

phosphorylation (pTyr1054)

Angaben zum Gen

human ... TYK2(7297)

Immunogen

Peptide sequence around phosphorylation site of tyrosine 1054 (H-E-Y(p)-Y-R), according to the protein TYK2.

Leistungsmerkmale und Vorteile

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Zielbeschreibung

TYK2 encodes a member of the tyrosine kinase and, more specifically, the Janus kinases (JAKs) protein families. This protein associates with the cytoplasmic domain of type I and type II cytokine receptors and promulgate cytokine signals by phosphorylating receptor subunits. It is also component of both the type I and type III interferon signaling pathways. As such, it may play a role in anti-viral immunity. A mutation in this gene has been associated with hyperimmunoglobulin E syndrome (HIES) - a primary immunodeficiency characterized by elevated serum immunoglobulin E.

Physikalische Form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Yue Zhu Zhang et al.
Biomedical and environmental sciences : BES, 32(6), 406-418 (2019-07-03)
Previous studies have indicated that the plasticizer di (2-ethylhexyl) phthalate (DEHP) affects lipid accumulation; however, its underlying mechanism remains unclear. We aim to clarify the effect of DEHP on lipid metabolism and the role of TYK2/STAT1 and autophagy. In total
Hui Yuan et al.
Journal of virology, 92(19) (2018-07-13)
Type I interferons (IFNs), as major components of the innate immune system, play a vital role in host resistance to a variety of pathogens. Canonical signaling mediated by type I IFNs activates the Janus kinase-signal transducer and activator of transcription
Xiaoyan Li et al.
Life sciences, 217, 283-292 (2018-12-15)
PMS1 Homolog 2, Mismatch Repair System Component Pseudogene 2 (PMS2L2) has been reported as an up-regulated long non-coding RNA (lncRNA) in osteoarthritis (OA) tissues. The purpose of the present work is to explore whether the differently expressed PMS2L2 is associated
Yoshinori Kitagawa et al.
FEBS letters, 594(5), 864-877 (2019-11-11)
Respirovirus C protein blocks the type I interferon (IFN)-stimulated activation of the JAK-STAT pathway. It has been reported that C protein inhibits IFN-α-stimulated tyrosine phosphorylation of STATs, but the underlying mechanism is poorly understood. Here, we show that the C

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