OTUB1 Antibody [N21M4] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IP1:30 IF1:250 FCM1:500

Application
WB, IP, IF, FCM

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
31 kDa

Datasheet & SDS

Biological Description

Specificity
OTUB1 Antibody [N21M4] detects endogenous levels of total OTUB1 protein.

Clone
N21M4

Synonym(s)
OTB1, OTU1, HSPC263, OTUB1, Ubiquitin thioesterase OTUB1, Deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Otubain-1, Ubiquitin-specific-processing protease OTUB1, hOTU1

Background
OTUB1 is an OTU family deubiquitinase that regulates protein ubiquitination both by directly cleaving ubiquitin chains and by non‑catalytically blocking ubiquitin transfer, giving it a central role in tuning protein stability and signaling outputs downstream of multiple receptors. The protein contains an OTU catalytic domain with a conserved cysteine–histidine active site that can hydrolyze K48‑ and K63‑linked ubiquitin chains, and flanking N‑ and C‑terminal regions that engage E2 enzymes and ubiquitin‑loaded complexes, allowing OTUB1 to sense ubiquitin linkage type and interaction partners before deciding between catalytic and non‑catalytic modes of action. OTUB1 docks onto ubiquitin‑charged E2 conjugating enzymes such as UBE2N/UBE2D through defined interfaces and, when engaged with a proximal ubiquitin, can allosterically inhibit further ubiquitin transfer without necessarily promoting chain cleavage, so OTUB1 can stabilize substrates by shutting down E2 activity at specific signaling nodes. This non‑canonical inhibition is prominent in pathways controlled by c‑IAP1 and TNF receptor signaling, where OTUB1 limits K63‑ and linear ubiquitination events that would otherwise promote recruitment of TAK1, IKK complexes, and downstream NF‑κB activation, thereby restraining inflammatory and survival signaling and tuning the balance between pro‑ and anti‑apoptotic outputs. OTUB1 also deubiquitinates or protects regulators of the DNA damage response, including factors in the ubiquitin‑dependent ATM/ATR networks, positioning it as a modulator of checkpoint control, repair complex assembly, and recovery from genotoxic stress. OTUB1 as a frequently upregulated deubiquitinase that stabilizes oncogenic or pro‑survival substrates by preventing their proteasomal degradation, supports epithelial–mesenchymal transition and migration through regulation of EMT‑linked transcription factors and cytoskeletal regulators, and contributes to drug resistance by maintaining levels of checkpoint and immune‑evasive proteins such as PD‑L1 in specific tumor contexts. OTUB1 also has amyloidogenic properties and can form ordered aggregates, and its involvement in maintaining proteostasis via control of ubiquitin turnover connects it to pathways that determine neuronal vulnerability to misfolded proteins and stress.

Background

OTUB1 is an OTU family deubiquitinase that regulates protein ubiquitination both by directly cleaving ubiquitin chains and by non‑catalytically blocking ubiquitin transfer, giving it a central role in tuning protein stability and signaling outputs downstream of multiple receptors. The protein contains an OTU catalytic domain with a conserved cysteine–histidine active site that can hydrolyze K48‑ and K63‑linked ubiquitin chains, and flanking N‑ and C‑terminal regions that engage E2 enzymes and ubiquitin‑loaded complexes, allowing OTUB1 to sense ubiquitin linkage type and interaction partners before deciding between catalytic and non‑catalytic modes of action. OTUB1 docks onto ubiquitin‑charged E2 conjugating enzymes such as UBE2N/UBE2D through defined interfaces and, when engaged with a proximal ubiquitin, can allosterically inhibit further ubiquitin transfer without necessarily promoting chain cleavage, so OTUB1 can stabilize substrates by shutting down E2 activity at specific signaling nodes. This non‑canonical inhibition is prominent in pathways controlled by c‑IAP1 and TNF receptor signaling, where OTUB1 limits K63‑ and linear ubiquitination events that would otherwise promote recruitment of TAK1, IKK complexes, and downstream NF‑κB activation, thereby restraining inflammatory and survival signaling and tuning the balance between pro‑ and anti‑apoptotic outputs. OTUB1 also deubiquitinates or protects regulators of the DNA damage response, including factors in the ubiquitin‑dependent ATM/ATR networks, positioning it as a modulator of checkpoint control, repair complex assembly, and recovery from genotoxic stress. OTUB1 as a frequently upregulated deubiquitinase that stabilizes oncogenic or pro‑survival substrates by preventing their proteasomal degradation, supports epithelial–mesenchymal transition and migration through regulation of EMT‑linked transcription factors and cytoskeletal regulators, and contributes to drug resistance by maintaining levels of checkpoint and immune‑evasive proteins such as PD‑L1 in specific tumor contexts. OTUB1 also has amyloidogenic properties and can form ordered aggregates, and its involvement in maintaining proteostasis via control of ubiquitin turnover connects it to pathways that determine neuronal vulnerability to misfolded proteins and stress.

References
https://pubmed.ncbi.nlm.nih.gov/23524849/ https://pubmed.ncbi.nlm.nih.gov/38264570/

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%