描述：
Human interleukin-36 beta [IL-36β; previously IL-1F8 and also named FIL-1η (eta)
and IL-1H2] is a member of the IL-1 family of proteins. IL-1 family members
includeIL-1β, IL-1α, IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-36α/IL-1F6, IL-37/IL-1F7,
IL-36γ/IL-1F9 and IL-1F10 (4, 6). All family members show a
12β-stranded β-trefoil configuration, and are believed to have arisen from a
common ancestral gene that has undergone multiple duplications. Two alternatively
spliced transcript variants encode distinct (164 or 157 residues) protein isoforms
that differ in their C-terminal 70 amino acid (aa) residues have been reported.
IL-36β/IL-1F8 isoform 2 is synthesized as a 157 aa protein that contains no signal
sequence and no prosegment. Unlike IL-36β/IL-1F8 isoform 1 which lacks potential
N-linked glycosylation sites, isoform 2 contains one potential N-linked glycosylation
site in its unique C-terminus. IL-36β/IL-1F8 is reported to be actively secreted. Human
IL-36β/IL-1F8 isoform 2 shares 61% aa identity with mouse IL-1 ra, a 183 aa form
of IL-36β/IL-1F8. Within the IL-1 family, IL-36β/IL-1F8 shares 30%, 32%, 37%, 46%,
34%, 45% and 28% aa sequence identity with IL-1 ra, IL-1β, IL-36Ra/IL-1F5, IL-36α/IL-1F6,
IL-37/IL-1F7, IL-36γ/IL-1F9 and IL-1F10, respectively. Cells reported to express
IL-36β/IL-1F8 include resting and activated monocytes and B cells. The receptor
for IL-36β/IL-1F8 is reported to be a combination of IL-1 Rrp2 and IL-1 RAcP. Recombinant
IL-36β/IL-1F8, along with IL-36α/IL-1F6 and IL-36γ/IL-1F9, has been shown to activate the
pathway involving NF-κB and MAPK in an IL-1 Rrp2 dependent manner.
原厂资料：
Human interleukin-36 beta [IL-36β; previously IL-1F8 and also named FIL-1η (eta)
and IL-1H2] is a member of the IL-1 family of proteins. IL-1 family members
includeIL-1β, IL-1α, IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-36α/IL-1F6, IL-37/IL-1F7,
IL-36γ/IL-1F9 and IL-1F10 (4, 6). All family members show a
12β-stranded β-trefoil configuration, and are believed to have arisen from a
common ancestral gene that has undergone multiple duplications. Two alternatively
spliced transcript variants encode distinct (164 or 157 residues) protein isoforms
that differ in their C-terminal 70 amino acid (aa) residues have been reported.
IL-36β/IL-1F8 isoform 2 is synthesized as a 157 aa protein that contains no signal
sequence and no prosegment. Unlike IL-36β/IL-1F8 isoform 1 which lacks potential
N-linked glycosylation sites, isoform 2 contains one potential N-linked glycosylation
site in its unique C-terminus. IL-36β/IL-1F8 is reported to be actively secreted. Human
IL-36β/IL-1F8 isoform 2 shares 61% aa identity with mouse IL-1 ra, a 183 aa form
of IL-36β/IL-1F8. Within the IL-1 family, IL-36β/IL-1F8 shares 30%, 32%, 37%, 46%,
34%, 45% and 28% aa sequence identity with IL-1 ra, IL-1β, IL-36Ra/IL-1F5, IL-36α/IL-1F6,
IL-37/IL-1F7, IL-36γ/IL-1F9 and IL-1F10, respectively. Cells reported to express
IL-36β/IL-1F8 include resting and activated monocytes and B cells. The receptor
for IL-36β/IL-1F8 is reported to be a combination of IL-1 Rrp2 and IL-1 RAcP. Recombinant
IL-36β/IL-1F8, along with IL-36α/IL-1F6 and IL-36γ/IL-1F9, has been shown to activate the
pathway involving NF-κB and MAPK in an IL-1 Rrp2 dependent manner.
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