Mouse interleukin-36 beta [IL-36 beta ; previously IL-1F8, FIL-1 eta(eta) and IL-1H2] is a member of the IL-1 family of proteins that includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-36 alpha /IL-1F6, IL-37/IL-1F7, IL-36 gamma /IL-1F9 and IL-1F10. All family members show a 12 beta-stranded beta-trefoil configuration, share up to 50% amino acid (aa) sequence identity, and are believed to have arisen from a common ancestral gene. Although two alternatively spliced transcript variants for human IL-36 beta /IL-1F8 have been described, to date, only one mouse IL-36 beta /IL-1F8 isoform is known. Mouse IL-36 beta /IL-1F8 is synthesized as a 183 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site(s). Mouse IL-36 beta /IL-1F8 shares 61% and 74% aa identity with human IL-36 beta isoform 2 and rat IL-36 beta, respectively. IL-36 beta is agonistic, stimulating release of inflammatory mediators such as IL-6 and IL-8, and cytotoxic peptides such as beta-defensins 2 and 3 that aid in defense against microbial pathogens. The receptor for IL-36 proteins is IL-1 Rrp2, with IL-1 RAcP as a coreceptor. Antagonism of IL-36 proteins by IL-36Ra, which also binds IL-1 Rrp2, has been shown by some investigators. Skin keratinocytes express highest levels of IL-36 proteins and their receptors, followed by epithelia in the esophagus, trachea and bronchae. IL-36 beta expression is increased in psoriatic skin and may play a role in pathogenesis of psoriasis. IL-36 beta is also expressed in resting and activated monocytes and B cells, synovial fibroblasts, neurons and glia, and is detectable in plasma and body fluids. IL-36 beta, along with IL-36 alpha and IL-36 gamma, is up-regulated by IL-1 alpha and TNF- alpha in keratinocytes, and has been shown to activate NF- kappa B and MAPK signaling pathways in an IL-1 Rrp2-dependent manner. Full-length recombinant IL-36 proteins appear less active than their endogenous counterparts, but trimming of the N-termini enhances their activity.

 

Product Properties

Synonyms	FIL1 eta, IL-1 eta, IL-1F8, IL-1H2
Accession	Q9D6Z6
GeneID	69677
Source	E.coli-derived Mouse IL-36β, 183aa, Met1-Lys183, with an N-terminal Met.
Molecular Weight	Approximately 20.9 kDa.
AA Sequence	MMAFPPQSCV HVLPPKSIQM WEPNHNTMHG SSQSPRNYRV HDSQQMVWVL TGNTLTAVPA SNNVKPVILS LIACRDTEFQ DVKKGNLVFL GIKNRNLCFC CVEMEGKPTL QLKEVDIMNL YKERKAQKAF LFYHGIEGST SVFQSVLYPG WFIATSSIER QTIILTHQRG KLVNTNFYIE SEK
Tag	None
Physical Appearance	Sterile Filtered White lyophilized (freeze-dried) powder.
Purity	> 95% by SDS-PAGE and HPLC analyses.
Biological Activity	The specific activity determined by its ability in a functional ELISA. Immobilized rMuIL-36β at 1 µg/mL can bind recombinant murine IL-1 Rrp2 with a range of 0.15-5 µg/mL. Fully biologically active when compared to standard.
Endotoxin	< 1.0 EU per 1μg of the protein by the LAL method.
Formulation	Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 300 mM NaCl, pH 8.0, 5 % trehalose.
Reconstitution	We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.

 

Shipping and Storage

 

The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year.

Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.

 

Cautions

1. Avoid repeated freeze-thaw cycles.

2. For your safety and health, please wear lab coats and disposable gloves for operation.

3. For research use only!

 

HB220415