TRAF6BP/TAX1BP1 C-terminal Antibody [J5J4]

Application: Reactivity: Human

Lane 1: HepG2, Lane 2: A549, Lane 3: 293T, Lane 4: U937

Usage Information

Dilution
WB1:1000 - 1:5000 IF1:50 - 1:100

Application
WB, IF

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
91 kDa 95 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	HEK-293T cells; HepG2 cells; A549 cells; 293T cells; U937 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
TRAF6BP/TAX1BP1 C-terminal Antibody [J5J4] detects endogenous levels of C-terminal of total TRAF6BP/TAX1BP1 protein.

Clone
J5J4

Synonym(s)
T6BP; PRO0105; TAX1BP1; Tax1-binding protein 1; TRAF6-binding protein

Background
The C-terminal domain of TRAF6BP/TAX1BP1 (Tax1-binding protein 1) is a selective autophagy receptor and negative regulator of innate immunity. It contains two tandem zinc finger ubiquitin-binding domains with conserved CCHC motifs that coordinate zinc ions, forming hydrophobic pockets that specifically engage K63-linked polyubiquitin chains. These zinc fingers are connected by a flexible linker, enabling cooperative bivalent binding to polyubiquitinated substrates, and the domain includes a caspase-8 cleavage site that renders it vulnerable during apoptosis. The ubiquitin-binding domains are essential for recruiting TAX1BP1 to ubiquitinated cargoes, such as TRAF6 K124-linked chains in TNFR and IL1R signaling, where TAX1BP1 serves as an adaptor for the A20/TNFAIP3 deubiquitinase to hydrolyze ubiquitin from TRAF6 or RIPK1, thereby terminating TAK1-NF-κB/AP-1 activation and limiting excessive cytokine production. In antiviral responses, the domain facilitates TAX1BP1 recruitment to MAVS aggregates on mitochondria, where it brings in the ITCH E3 ligase for K48-linked ubiquitination and degradation, attenuating IFN-β signaling. TAX1BP1 also recognizes bacterial effectors and Mtb clusters, working in concert with LIR/SKICH motifs for LC3 engagement and myosin VI C-terminal binding to mediate autophagosome delivery and xenophagy. Mutations in the zinc finger domains that disrupt ubiquitin binding abolish selective autophagy but do not affect oligomerization, leading to hyperinflammation due to persistent TLR3/4 and RIG-I/MAVS signaling. Overexpression of the C-terminal domain suppresses septic shock and tumor PD-L1 expression via enhanced mitophagy, while caspase-mediated cleavage produces an N-terminal fragment that promotes apoptosis through AIF release.

Background

The C-terminal domain of TRAF6BP/TAX1BP1 (Tax1-binding protein 1) is a selective autophagy receptor and negative regulator of innate immunity. It contains two tandem zinc finger ubiquitin-binding domains with conserved CCHC motifs that coordinate zinc ions, forming hydrophobic pockets that specifically engage K63-linked polyubiquitin chains. These zinc fingers are connected by a flexible linker, enabling cooperative bivalent binding to polyubiquitinated substrates, and the domain includes a caspase-8 cleavage site that renders it vulnerable during apoptosis. The ubiquitin-binding domains are essential for recruiting TAX1BP1 to ubiquitinated cargoes, such as TRAF6 K124-linked chains in TNFR and IL1R signaling, where TAX1BP1 serves as an adaptor for the A20/TNFAIP3 deubiquitinase to hydrolyze ubiquitin from TRAF6 or RIPK1, thereby terminating TAK1-NF-κB/AP-1 activation and limiting excessive cytokine production. In antiviral responses, the domain facilitates TAX1BP1 recruitment to MAVS aggregates on mitochondria, where it brings in the ITCH E3 ligase for K48-linked ubiquitination and degradation, attenuating IFN-β signaling. TAX1BP1 also recognizes bacterial effectors and Mtb clusters, working in concert with LIR/SKICH motifs for LC3 engagement and myosin VI C-terminal binding to mediate autophagosome delivery and xenophagy. Mutations in the zinc finger domains that disrupt ubiquitin binding abolish selective autophagy but do not affect oligomerization, leading to hyperinflammation due to persistent TLR3/4 and RIG-I/MAVS signaling. Overexpression of the C-terminal domain suppresses septic shock and tumor PD-L1 expression via enhanced mitophagy, while caspase-mediated cleavage produces an N-terminal fragment that promotes apoptosis through AIF release.

References
https://pubmed.ncbi.nlm.nih.gov/24239949/ https://pubmed.ncbi.nlm.nih.gov/17304240/

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%