Recombinant Active Human IL1B Protein, His-tagged(C-ter)

• Cat.No.: IL1B-162H
• Product Overview: Recombinant Active Human IL1B Protein with His tag (C-ter) was expressed in E. coli.

Specification

• Description: IL1 beta protein is a member of the interleukin 1 cytokine family. This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. [provided by RefSeq, Jul 2008]
• Source: E. coli
• Species: Human
• Tag: His(C-ter)
• Form: Powder
• Bio-activity: Determined by its ability to induce proliferation in D10.G4.1 cells. The ED50 for this effect is <10 pg/mL. The specific activity of recombinant human IL-1 beta is approximately >1.5 x 10^8 IU/mg. Determined by its ability to induce IL-8 secretion in HT29 cells. The ED50 for this effect is 1.8-5.1 ng/mL.
• AA Sequence: MASAPVRSLNCTLRDSQQKSLVMSG PYELKALHLQGQDMEQQVVFSMSFV QGEESNDKIPVALGLKEKNLYLSCV LKDDKPTLQLESVDPKNYPKKKMEK RFVFNKIEINNKLEFESAQFPNWYI STSQAENMPVFLGGTKGGQDITDFT MQFVSS
• Endotoxin: Endotoxin level is less than 0.1 EU/μg of the protein, as determined by the LAL test.
• Purity: > 98% (by SDS-PAGE)
• Applications: SDS-PAGE
• Notes: For laboratory research only, not for drug, diagnostic or other use.
• Storage: Lyophilized protein should be stored at -20°C. After reconstitution, aliquot and store at -20°C or -80°C for up to one month. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening.
• Storage Buffer: PBS (pH 8.0)
• Reconstitution: It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 100 μg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely.

Gene Information

• Gene Name: IL1B interleukin 1, beta [ Homo sapiens ]
• Official Symbol: IL1B
• Synonyms: IL1B; interleukin 1, beta; interleukin-1 beta; IL 1B; IL1 BETA; IL1F2; IL-1 beta; catabolin; preinterleukin 1 beta; pro-interleukin-1-beta; IL-1; IL1-BETA
• Gene ID: 3553
• mRNA Refseq: NM_000576
• Protein Refseq: NP_000567
• MIM: 147720
• UniProt ID: P01584

Reviews

11/08/2021

Effective in inflammation studies.

04/23/2021

High specificity.

06/30/2020

Suitable for cytokine assays.

Q&As

How does IL-1β initiate inflammasome assembly, and which experimental techniques unravel this intricate process?

Inflammasome assembly initiated by IL-1β is deciphered using techniques like co-immunoprecipitation, proximity ligation assays, and super-resolution microscopy.

What are the specific mechanisms underlying IL-1β's priming of immune cells, and how can flow cytometry and gene expression analyses decipher these molecular pathways?

IL-1β's priming of immune cells is dissected through flow cytometry, RNA sequencing, and chromatin immunoprecipitation, revealing its epigenetic and transcriptional effects.

How do post-translational modifications regulate IL-1β's biological activity, and how can mass spectrometry-based phosphoproteomics provide insights into these modifications?

Mass spectrometry-based phosphoproteomics deciphers IL-1β's post-translational modifications, revealing regulatory sites crucial for its activation and signaling.

How can advanced bioinformatics tools be applied to multi-omics data to comprehensively understand the intricate roles of IL-1β in health and disease?

Bioinformatics tools integrate multi-omics data to provide a comprehensive understanding of IL-1β's roles, revealing its intricate contributions to health and disease.

What is the significance of IL-1β's epigenetic regulation in chronic inflammatory diseases, and how can ChIP-seq and DNA methylation profiling uncover these regulatory elements?

ChIP-seq and DNA methylation profiling uncover IL-1β's epigenetic impact on target genes, shedding light on its role in shaping chronic inflammatory states.

How does IL-1β interact with its downstream effectors to induce the production of pro-inflammatory cytokines, and how can dual-luciferase reporter assays reveal these intricate interactions?

IL-1β's interactions with downstream effectors are unveiled using dual-luciferase reporter assays, surface plasmon resonance, and co-crystallization studies.

What are the complex feedback loops between IL-1β and other cytokines, and how can systems biology approaches like network analysis dissect these dynamic interactions?

Network analysis integrates omics data to unravel IL-1β's intricate cross-talk with other cytokines, mapping out complex regulatory loops in inflammation.

What is the role of IL-1β in modulating the tumor microenvironment, and how can advanced imaging techniques like intravital microscopy elucidate its impact on immune cell dynamics?

IL-1β's impact on the tumor microenvironment is studied using intravital microscopy, 3D culture models, and single-cell RNA sequencing to capture dynamic cell behavior.

What are the mechanisms underlying IL-1β's non-canonical signaling pathways, and how can CRISPR-Cas9 screening identify key mediators of these alternative pathways?

CRISPR-Cas9 screening identifies IL-1β's non-canonical signaling mediators through functional genomics, revealing alternative pathways in cellular responses.

How does IL-1β's signaling adapt to different cellular contexts, and how can single-cell RNA sequencing uncover cell-specific responses to this cytokine?

Single-cell RNA sequencing unveils IL-1β's context-specific responses, exposing cell type-specific signaling and gene expression patterns.