Rabbit anti-Human OTULIN Polyclonal Antibody

Uniprot Id

Q96BN8

Target Species

Human

Target Name

OTULIN

Target Full Name

Ubiquitin thioesterase otulin

Target Function

Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex. OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex. Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation. Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling.

Target Involvement

Autoinflammation, panniculitis, and dermatosis syndrome (AIPDS)

Target Subcellular Location

Cytoplasm.

Target Protein Families

Peptidase C65 family, Otulin subfamily

Target Research Area

Epigenetics and Nuclear Signaling

Target Synonyms

AIPDS; Deubiquitinating enzyme otulin; F105B_HUMAN; Fam105b; Family with sequence similarity 105, member B; FLJ34884; GUM; OTU deubiquitinase with linear linkage specificity; OTULIN; Protein FAM105B; Ubiquitin thioesterase Gumby

Target Background

This gene encodes a member of the peptidase C65 family of ubiquitin isopeptidases. Members of this family remove ubiquitin from proteins. The encoded enzyme specifically recognizes and removes M1(Met1)-linked, or linear, ubiquitin chains from protein substrates. Linear ubiquitin chains are known to regulate the NF-kappa B signaling pathway in the context of immunity and inflammation. Mutations in this gene cause a potentially fatal autoinflammatory syndrome in human patients.