描述：
Human interleukin-36 alpha [IL-36α; previously IL-1F6 and also FIL-1ε (epsilon) ]
is a member of the IL-1 family of proteins. IL-1 family members include IL-1β, IL-1α,
IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9
and IL-1F10. All family members show a 12 β-strand, β-trefoil configuration,
and all family members are believed to have arisen from a common ancestral
gene that has undergone multiple duplications. IL-36α/IL-1F6 is synthesized as
a 158 amino acid (aa) protein that contains no signal sequence, no prosegment
and no potential N-linked glycosylation site(s). It appears to be actively secreted.
When found in cell lysate, it presents as an 18 kDa monomer. Human to mouse, full
length IL-1F6 has 54% aa identity. Within the family, IL-1F6 is 30% aa identical to
IL-1ra, and 27%, 31%, 36%, 46%, 57% and 28% aa identical to IL-1β, IL-36Ra/IL-1F5,
IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9 andIL-1F10, respectively.
Cells reported to express IL-36α/IL-1F6 include monocytes, B cells and T cells.
Notably, IL-36α/IL-1F6 is the only novel IL-1 family member found to be expressed
on T cells. The receptor for IL-36α/IL-1F6 is reported to be a combination of IL-1
Rrp2 and IL-1 RAcP.RecombinantIL-36α/IL-1F6, along with IL-36β/IL-1F8 and IL-36γ/IL-1F9,
has been shown to act as an agonist by activating the pathway involving NF-κB and MAPK
in an IL-1 Rrp2 dependent manner. This suggests that IL-36α/IL-1F6 may signal
in a similar fashion to IL-1 and IL-18 in having a binding receptor which upon ligation,
recruits a second receptor as a signaling component, forming an active heterodimeric
receptor complex.
原厂资料：
Human interleukin-36 alpha [IL-36α; previously IL-1F6 and also FIL-1ε (epsilon) ]
is a member of the IL-1 family of proteins. IL-1 family members include IL-1β, IL-1α,
IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9
and IL-1F10. All family members show a 12 β-strand, β-trefoil configuration,
and all family members are believed to have arisen from a common ancestral
gene that has undergone multiple duplications. IL-36α/IL-1F6 is synthesized as
a 158 amino acid (aa) protein that contains no signal sequence, no prosegment
and no potential N-linked glycosylation site(s). It appears to be actively secreted.
When found in cell lysate, it presents as an 18 kDa monomer. Human to mouse, full
length IL-1F6 has 54% aa identity. Within the family, IL-1F6 is 30% aa identical to
IL-1ra, and 27%, 31%, 36%, 46%, 57% and 28% aa identical to IL-1β, IL-36Ra/IL-1F5,
IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9 andIL-1F10, respectively.
Cells reported to express IL-36α/IL-1F6 include monocytes, B cells and T cells.
Notably, IL-36α/IL-1F6 is the only novel IL-1 family member found to be expressed
on T cells. The receptor for IL-36α/IL-1F6 is reported to be a combination of IL-1
Rrp2 and IL-1 RAcP.RecombinantIL-36α/IL-1F6, along with IL-36β/IL-1F8 and IL-36γ/IL-1F9,
has been shown to act as an agonist by activating the pathway involving NF-κB and MAPK
in an IL-1 Rrp2 dependent manner. This suggests that IL-36α/IL-1F6 may signal
in a similar fashion to IL-1 and IL-18 in having a binding receptor which upon ligation,
recruits a second receptor as a signaling component, forming an active heterodimeric
receptor complex.
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