Bcl10 Antibody [J3K14] | Primary Antibodies

Application: Reactivity: Human

Lane 1: Raji, Lane 2: Ramos, Lane 3: HuT-78, Lane 4: Hela

Usage Information

Dilution
WB1:1000 - 1:5000 IP1:20 - 1:50 IHC1:50 IF1:100 - 1:250 FCM1:200

Application
WB, IP, IHC, IF, 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
26 kDa 32 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human lung carcinoma; Human hepatocellular carcinoma; Raji cells; Ramos cells; HuT-78 cells; HeLa cells
Negative Control	A549 cells

Datasheet & SDS

Biological Description

Specificity
Bcl10 Antibody [J3K14] detects endogenous levels of total Bcl10 protein.

Clone
J3K14

Synonym(s)
CIPER; CLAP; BCL10; B-cell lymphoma/leukemia 10; B-cell CLL/lymphoma 10; CARD-containing molecule enhancing NF-kappa-B; CARD-like apoptotic protein; Bcl-10; hCLAP; cCARMEN; c-E10; mE10

Background
Bcl10 (B-cell lymphoma/leukemia 10) is a 233-amino-acid adaptor protein ubiquitously expressed in immune cells and serves as a central scaffold within the CBM (CARD11-Bcl10-MALT1) signalosome, which is essential for antigen receptor-induced NF-κB and JNK activation in adaptive immunity. Initially discovered through t(1;14)(p22;q32) translocations in MALT lymphomas that drive constitutive CBM signaling, Bcl10 consists of an N-terminal caspase recruitment domain (CARD, residues 1–115) forming six α-helices with critical charged residues (Asp80, Glu84) mediating homotypic CARD-CARD interactions to enable helical filament assembly, and a C-terminal serine/threonine-rich unstructured tail (residues 116–233) that is prone to phosphorylation, binds MALT1 immunoglobulin domains, and regulates protein stability. Upon T-cell or B-cell receptor (TCR/BCR) or GPCR stimulation, CARMA1/CARD11 oligomerizes to nucleate Bcl10 CARD filaments, recruiting additional Bcl10 monomers into higher-order hollow helices via basic–acidic patch interfaces. This filament assembly allosterically activates MALT1 protease by conformational release, enabling canonical IKK/NF-κB signaling for lymphocyte survival and proliferation and JNK signaling for effector differentiation; point mutations such as D80A or E84A disrupt polymerization and abrogate downstream signaling. Bcl10 undergoes multi-site phosphorylation by kinases like TBK1/IKKε (Ser218/Thr225) and CK1α to promote filament dynamics and MALT1-mediated cleavage of substrates (e.g., CYLD, RelB), facilitating TRAF6/NEMO ubiquitination, while PKC/TCR-induced degradation provides negative feedback to prevent hyperactivation. Bcl10 deficiency results in severe combined immunodeficiency with defective NF-κB activation, spontaneous exencephaly in mice, and tumor suppression, whereas MALT1 fusions or hyperactive Bcl10 filaments drive lymphomagenesis, inflammatory bowel disease, and psoriasis via unchecked inflammatory signaling.

Background

Bcl10 (B-cell lymphoma/leukemia 10) is a 233-amino-acid adaptor protein ubiquitously expressed in immune cells and serves as a central scaffold within the CBM (CARD11-Bcl10-MALT1) signalosome, which is essential for antigen receptor-induced NF-κB and JNK activation in adaptive immunity. Initially discovered through t(1;14)(p22;q32) translocations in MALT lymphomas that drive constitutive CBM signaling, Bcl10 consists of an N-terminal caspase recruitment domain (CARD, residues 1–115) forming six α-helices with critical charged residues (Asp80, Glu84) mediating homotypic CARD-CARD interactions to enable helical filament assembly, and a C-terminal serine/threonine-rich unstructured tail (residues 116–233) that is prone to phosphorylation, binds MALT1 immunoglobulin domains, and regulates protein stability. Upon T-cell or B-cell receptor (TCR/BCR) or GPCR stimulation, CARMA1/CARD11 oligomerizes to nucleate Bcl10 CARD filaments, recruiting additional Bcl10 monomers into higher-order hollow helices via basic–acidic patch interfaces. This filament assembly allosterically activates MALT1 protease by conformational release, enabling canonical IKK/NF-κB signaling for lymphocyte survival and proliferation and JNK signaling for effector differentiation; point mutations such as D80A or E84A disrupt polymerization and abrogate downstream signaling. Bcl10 undergoes multi-site phosphorylation by kinases like TBK1/IKKε (Ser218/Thr225) and CK1α to promote filament dynamics and MALT1-mediated cleavage of substrates (e.g., CYLD, RelB), facilitating TRAF6/NEMO ubiquitination, while PKC/TCR-induced degradation provides negative feedback to prevent hyperactivation. Bcl10 deficiency results in severe combined immunodeficiency with defective NF-κB activation, spontaneous exencephaly in mice, and tumor suppression, whereas MALT1 fusions or hyperactive Bcl10 filaments drive lymphomagenesis, inflammatory bowel disease, and psoriasis via unchecked inflammatory signaling.

References
https://pubmed.ncbi.nlm.nih.gov/24074955/ https://pubmed.ncbi.nlm.nih.gov/35727133/

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%