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Recombinant Equine IL-1 beta/IL-1F2 Protein

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SDS-Page: Equine IL-1 beta/IL-1F2 Protein [NBP2-34941]

Product Details

Summary
Reactivity EqSpecies Glossary
Applications PAGE, Bioactivity
Format
Carrier-Free
Concentration
LYOPH

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Recombinant Equine IL-1 beta/IL-1F2 Protein Summary

Description
A single non-glycosylated polypeptide chain containing 153 amino acids corresponding to IL-1 beta/IL-1F2 Source: E. coli

Uniprot ID: Q28386

Amino Acid Sequence: AAMHSVNCRL RDIYHKSLVL SGACELQAVH LNGENTNQQV VFCMSFVQGE EETDKIPVAL GLKEKNLYLS CGMKDGKPTL QLETVDPNTY PKRKMEKRFV FNKMEIKGNV EFESAMYPNW YISTSQAEKS PVFLGNTRGG RDITDFIMEI TSA

Details of Functionality
IL1 beta Protein is fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 20 pg/ml, corresponding to a specific activity of > 5.0 x 10^7 IU/mg.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
IL1B
Purity
>95%, by SDS-PAGE and HPLC
Endotoxin Note
Less than 1 EU/ug of IL-1 beta/IL-1F2 as determined by LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
  • SDS-Page
Theoretical MW
17.3 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at -20 to -70C as supplied. After reconstitution, store at 2 to 8C for 1 month and at -20 to -70C for long term storage. Avoid repeated freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in 1 x PBS, pH 7.4, 0.1 % Tween-80.
Preservative
No Preservative
Concentration
LYOPH
Purity
>95%, by SDS-PAGE and HPLC
Reconstitution Instructions
Recommended to centrifuge prior to opening. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Apportion stock solutions into working aliquots and store at <-20C.

Notes

This lyophilized preparation is stable for 12 months from date of receipt at -20 to -70 degrees C, preferably desiccated. Upon reconstitution, the preparation can be stored for 1 month at 2-8 degrees C under sterile conditions, and for 3 months at -20 degrees C to -70 degrees C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Stock solutions should be aliquoted and stored at < -20 degrees C. Further dilutions should be made in appropriate buffered solutions

Alternate Names for Recombinant Equine IL-1 beta/IL-1F2 Protein

  • catabolin
  • IL1 beta
  • IL-1 beta
  • IL-1
  • IL1B
  • IL-1b
  • IL1-BETA
  • IL-1F2
  • IL1F2IL-1 beta
  • interleukin 1, beta
  • interleukin-1 beta
  • preinterleukin 1 beta
  • pro-interleukin-1-beta

Background

Interleukin-1 beta (IL-1 beta), also called IL-1F2, is a proinflammatory cytokine that functions in host defense following injury or inflammation (1-5). IL-1 beta is expressed by cells of the immune system such as monocytes, macrophage, neutrophils, and hepatocytes (1-3). Human IL-1 beta protein is expressed in the cytoplasm in an inactive precursor form (pro-IL-1 beta) which is 269 amino acids in length with a theoretical molecular weight of 31 kDa (1,4,6). Pro-IL-1 beta is cleaved by IL-1 converting enzyme (ICE), also called caspase-1, generating the 18 kDa mature, active protein that is secreted from cells (1,4,6). Pro-IL-1 beta is produced as a cellular response to molecular signals from pathogens and other processes termed pathogen associated molecular patterns (PAMPs) and damage associated molecular patterns (DAMPs) (1,2). PAMPs and DAMPs signal through pattern recognition receptors (PRRs) to induce formation of the inflammasome (1,2). The inflammasome is a multi-protein complex made of a PRR, such as Nod-like receptor family, pyrin domain containing 3(NLRP3), an adaptor, such as apoptosis-associated spec-like protein containing a CARD (ASC), and pro-caspase-1 (1-3,5). Assembly of the inflammasome enables cleavage of pro-caspase-1 into active caspase 1, followed by secretion of activate IL-1 beta (1-3,5).

IL-1 beta binding to its receptor IL-1RI and the downstream signaling contributes to a dual pathophysiological role (3). On one hand, IL-1 beta signaling activates immune cells and drives CD4+ T cell polarization to T helper type 1 (Th1) and Th17 cells, resulting in anti-tumor responses and mediation of acute inflammation (2,3). However, IL-1 beta also supports tumor growth and metastasis driven by multiple mechanisms including chronic inflammation, an immunosuppressive tumor microenvironment (TME), and angiogenesis (3). Additionally, IL-1 beta signaling been implicated in the pathogenesis of neuroinflammatory diseases of the central nervous system (CNS) such as multiple sclerosis (MS), Alzheimer's disease, and diabetic retinopathy (DR) (2). Mouse studies have shown regression of tumors treated with IL-1 as well as protective effects of IL-1 beta in instances of induced colitis and colon carcinoma (3). Conversely, blocking IL-1 beta has also shown promising effect in cancer treatment, especially when combined with chemotherapeutics (2,3). Approved IL-1 beta monoclonal antibody canakinumab has shown significant therapeutic promise in the treatment of DR (2). Given its multifaceted role in disease, IL-1 beta is a promising therapeutic target.

References

1. Lopez-Castejon G, Brough D. Understanding the mechanism of IL-1beta secretion. Cytokine Growth Factor Rev. 2011;22(4):189-195. https://doi.org/10.1016/j.cytogfr.2011.10.001

2. Mendiola AS, Cardona AE. The IL-1beta phenomena in neuroinflammatory diseases. J Neural Transm (Vienna). 2018;125(5):781-795. https://doi.org/10.1007/s00702-017-1732-9

3. Bent R, Moll L, Grabbe S, Bros M. Interleukin-1 Beta-A Friend or Foe in Malignancies?. Int J Mol Sci. 2018;19(8):2155. https://doi.org/doi:10.3390/ijms19082155

4. Krumm B, Xiang Y, Deng J. Structural biology of the IL-1 superfamily: key cytokines in the regulation of immune and inflammatory responses. Protein Sci. 2014;23(5):526-538. https://doi.org/10.1002/pro.2441

5. He Y, Hara H, Nunez G. Mechanism and Regulation of NLRP3 Inflammasome Activation. Trends Biochem Sci. 2016;41(12):1012-1021. https://doi.org/10.1016/j.tibs.2016.09.002

6. Uniprot (P01584)

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol IL1B
Uniprot