PKCθ/PRKCQ Antibody [L3H13] | Primary Antibodies

Application: Reactivity: Human

Lane 1: Jurkat, Lane 2: MOLT4

Usage Information

Dilution
WB1:1000 IHC1:2000 FCM1:50

Application
WB, IHC, FCM

Reactivity
Human

Source
Rabbit Monoclonal Antibody

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
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

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
https://pubmed.ncbi.nlm.nih.gov/17544292/ https://pubmed.ncbi.nlm.nih.gov/20923402/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

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%