PKCθ/PRKCQ Antibody [L3H13]

Catalog No.: F4807

Application: Reactivity: Human

Lane 1: Jurkat, Lane 2: MOLT4

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

文献中Selleckの製品使用例(1)

使用情報

Dilution
WB1:1000 IHC1:2000 FCM1:50

Application
WB, IHC, FCM

Source
Rabbit Monoclonal Antibody

Reactivity
Human

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
82 kDa 40 kDa,75 kDa
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

Specificity
PKCθ/PRKCQ Antibody [L3H13] detects endogenous levels of total PKCθ/PRKCQ protein.

Clone
L3H13

Synonym(s)
PRKCT; PRKCQ; Protein kinase C theta type; nPKC‑theta

Background
PKCθ (PRKCQ), a novel serine/threonine kinase of the protein kinase C family, predominantly localizes to the immune synapse of T lymphocytes, where it orchestrates signal transduction from T cell receptor (TCR) and CD28 engagement to drive activation, differentiation, and effector functions. It features a C1 domain for diacylglycerol binding and a kinase domain that undergoes conformational activation upon TCR-induced translocation to the central supramolecular activation complex (cSMAC). Upon antigen stimulation, PKCθ complexes with CARMA1, BCL10, and MALT1 to activate the CBM signalosome, catalyzing IKKβ phosphorylation through oligomerization and K63-linked polyubiquitination of NEMO, which liberates NF-κB dimers (p65/p50) for nuclear translocation and transcription of IL-2, IFN-γ, and survival genes; concurrently, PKCθ phosphorylates CARD11 to amplify AP-1 (c-Jun/Fos) via JNK and ERK cascades while cooperating with calcineurin to dephosphorylate NFAT for optimal cytokine synergy. This positions PKCθ at the crux of the TCR-CD28-NF-κB/AP-1-NFAT axis, selectively required for Th1/Th2/Th17 differentiation and regulatory T cell suppressive function, while dispensable for thymocyte development. It governs immune homeostasis, allograft tolerance, and antiviral responses, making it a prime target for researchers dissecting T cell polarity in live-cell imaging or profiling pathway dominance via kinase-dead mutants in Jurkat models. Genetic ablation reveals profound defects in Th2-mediated immunity and experimental autoimmune encephalomyelitis.

Background

PKCθ (PRKCQ), a novel serine/threonine kinase of the protein kinase C family, predominantly localizes to the immune synapse of T lymphocytes, where it orchestrates signal transduction from T cell receptor (TCR) and CD28 engagement to drive activation, differentiation, and effector functions. It features a C1 domain for diacylglycerol binding and a kinase domain that undergoes conformational activation upon TCR-induced translocation to the central supramolecular activation complex (cSMAC). Upon antigen stimulation, PKCθ complexes with CARMA1, BCL10, and MALT1 to activate the CBM signalosome, catalyzing IKKβ phosphorylation through oligomerization and K63-linked polyubiquitination of NEMO, which liberates NF-κB dimers (p65/p50) for nuclear translocation and transcription of IL-2, IFN-γ, and survival genes; concurrently, PKCθ phosphorylates CARD11 to amplify AP-1 (c-Jun/Fos) via JNK and ERK cascades while cooperating with calcineurin to dephosphorylate NFAT for optimal cytokine synergy. This positions PKCθ at the crux of the TCR-CD28-NF-κB/AP-1-NFAT axis, selectively required for Th1/Th2/Th17 differentiation and regulatory T cell suppressive function, while dispensable for thymocyte development. It governs immune homeostasis, allograft tolerance, and antiviral responses, making it a prime target for researchers dissecting T cell polarity in live-cell imaging or profiling pathway dominance via kinase-dead mutants in Jurkat models. Genetic ablation reveals profound defects in Th2-mediated immunity and experimental autoimmune encephalomyelitis.

References
[1] Hayashi K, et al. Pharmacol Res. 2007 Jun;55(6):537-44. [2] Kwon MJ, et al. Endocr Metab Immune Disord Drug Targets. 2010 Dec;10(4):367-72.

PVDFメンブレン孔径参考表

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%