c-Rel Antibody [B22C17] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: Raji, Lane 2: U973, Lane 3: A20, Lane 4: Neuro-2a

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse, Rat

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
68-78 kDa

Datasheet & SDS

Biological Description

Specificity
c-Rel Antibody [B22C17] detects endogenous levels of total c-Rel protein.

Clone
B22C17

Synonym(s)
Proto-oncogene c-Rel; REL

Background
c-Rel belongs to the Rel/NF-κB family of transcription factors characterized by a Rel homology domain that mediates DNA binding, dimerization, and nuclear localization. The protein contains an N-terminal Rel homology domain encompassing DNA-binding and dimerization regions, along with C-terminal transactivation domains unique to RelA, c-Rel, and RelB members. In resting hematopoietic cells where c-Rel expression predominates, IκBα and IκBβ sequester c-Rel dimers in the cytoplasm through binding to the nuclear localization signal within the Rel homology domain. Proinflammatory stimuli trigger the IKK complex to phosphorylate IκBα at N-terminal serines, leading to its K48-linked ubiquitination and proteasomal degradation, which unmasks the c-Rel nuclear localization signal and enables nuclear translocation as p50/c-Rel or RelA/c-Rel heterodimers. These dimers bind κB sites in promoters of target genes encoding cytokines, anti-apoptotic factors, and cell cycle regulators via the Rel homology domain's DNA-binding region. Distinct domains of IκBα mediate cytoplasmic retention through N-terminal and central ankyrin repeats that mask the nuclear localization signal, while central ankyrin and C-terminal acidic residues suffice for nuclear inhibition by competing for DNA-binding sites or corepressors. c-Rel forms stable p65/c-Rel heterodimers with IκBβ in unstimulated states, where hyperphosphorylated IκBβ acts as an inhibitor until stimulus-induced slow phosphorylation triggers its partial degradation, selectively releasing p65/c-Rel for TNFα promoter activation. Nuclear IκBα colocalizes with constitutively nuclear c-Rel variants to suppress transactivation. In T cell differentiation, c-Rel induces RORγt and IL-21 expression critical for Th17 and Tfh lineages, while supporting Foxp3 in regulatory T cells. Elevated c-Rel activity drives lymphoid malignancies and chronic inflammation through persistent target gene expression.

Background

c-Rel belongs to the Rel/NF-κB family of transcription factors characterized by a Rel homology domain that mediates DNA binding, dimerization, and nuclear localization. The protein contains an N-terminal Rel homology domain encompassing DNA-binding and dimerization regions, along with C-terminal transactivation domains unique to RelA, c-Rel, and RelB members. In resting hematopoietic cells where c-Rel expression predominates, IκBα and IκBβ sequester c-Rel dimers in the cytoplasm through binding to the nuclear localization signal within the Rel homology domain. Proinflammatory stimuli trigger the IKK complex to phosphorylate IκBα at N-terminal serines, leading to its K48-linked ubiquitination and proteasomal degradation, which unmasks the c-Rel nuclear localization signal and enables nuclear translocation as p50/c-Rel or RelA/c-Rel heterodimers. These dimers bind κB sites in promoters of target genes encoding cytokines, anti-apoptotic factors, and cell cycle regulators via the Rel homology domain's DNA-binding region. Distinct domains of IκBα mediate cytoplasmic retention through N-terminal and central ankyrin repeats that mask the nuclear localization signal, while central ankyrin and C-terminal acidic residues suffice for nuclear inhibition by competing for DNA-binding sites or corepressors. c-Rel forms stable p65/c-Rel heterodimers with IκBβ in unstimulated states, where hyperphosphorylated IκBβ acts as an inhibitor until stimulus-induced slow phosphorylation triggers its partial degradation, selectively releasing p65/c-Rel for TNFα promoter activation. Nuclear IκBα colocalizes with constitutively nuclear c-Rel variants to suppress transactivation. In T cell differentiation, c-Rel induces RORγt and IL-21 expression critical for Th17 and Tfh lineages, while supporting Foxp3 in regulatory T cells. Elevated c-Rel activity drives lymphoid malignancies and chronic inflammation through persistent target gene expression.

References
https://pubmed.ncbi.nlm.nih.gov/9488436/ https://pubmed.ncbi.nlm.nih.gov/22207895/

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%