Recombinant Porcine Interleukin-1 alpha

• Cat.No.: IL1α-81P
• Product Overview: Recombinant Porcine Interleukin-1 produced inE.Coliis single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1 is purified by proprietary chromatographic techniques.

Specification

• Cat. No.: IL1A-81P
• Description: Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
• Source: Escherichia Coli.
• Amino Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
• Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
• Purity: Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
• Formulation: The protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
• Solubility: It is recommended to reconstitute the lyophilized Interleukin-1 alpha in sterile 18 MΩ-cm H₂O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions.
• Specific Activity: The ED₅₀as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.
• Protein Content: Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.669 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.
• Stability: Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18℃. Upon reconstitution IL1 should be stored at 4℃ between 2-7 days and for future use below -18℃. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
• Pathways: Apoptosis; Cytokine-cytokine receptor interaction; Graft-versus-host disease; Hematopoietic cell lineage; Leishmaniasis; MAPK signaling pathway; Prion diseases; Type I diabetes mellitus
• Tag: Non

Gene Information

• Gene Name: IL1A interleukin 1, alpha [ Sus scrofa ]
• Synonyms: IL1A; interleukin 1, alpha; IL-1alpha; interleukin-1 alpha; IL-1 alpha; interleukin 1-alpha
• Gene ID: 397094
• mRNA Refseq: NM_214029
• Protein Refseq: NP_999194
• UniProt ID: P18430
• Chromosome Location: 3q12-q13; 3

Reviews

04/08/2021

High solubility.

07/02/2020

Good for intracellular staining.

03/13/2019

Effective in apoptosis assays.

Q&As

What methods are employed to dissect the intricate cross-talk between IL-1α and other cytokines, shedding light on its role in immune modulation?

Cross-talk between IL-1α's and other cytokines is dissected through methods such as co-immunoprecipitation, ELISA, and cytokine profiling arrays.

What experimental approaches allow researchers to dissect the paradoxical roles of IL-1α as both a pro-inflammatory and tissue repair mediator in distinct contexts?

IL-1α's paradoxical roles are dissected using conditional knockout mice, 3D culture systems, and molecular analyses to delineate context-specific effects.

How are cutting-edge techniques like single-cell RNA sequencing utilized to unravel the heterogeneity in IL-1α-responsive cell populations and their functional implications?

Single-cell RNA sequencing uncovers heterogeneity in IL-1α-responsive cell populations and their roles, revealing distinct molecular profiles and functions.

How is the intricate web of IL-1α's pro-inflammatory signaling pathways decoded using advanced experimental techniques?

IL-1α's intricate pro-inflammatory signaling pathways are decoded using advanced techniques like mass spectrometry, phosphoproteomics, and bioinformatics.

How are state-of-the-art genetic editing tools such as CRISPR-Cas9 applied to unravel IL-1α's precise contributions to inflammatory diseases?

Genetic editing tools like CRISPR-Cas9 unveil IL-1α's contributions to diseases by generating knockout models and studying resulting phenotypic changes.

How do researchers manipulate in vitro co-culture systems to dissect the dynamic interplay between immune cells and stromal cells in IL-1α-mediated responses?

In vitro co-culture systems are manipulated to study IL-1α-mediated responses, elucidating immune-stromal cell interactions via cytokine-specific neutralization.

What experimental strategies enable the identification of specific cellular receptors and downstream effectors responsible for IL-1α's diverse physiological effects?

Specific cellular receptors and effectors influenced by IL-1α are identified through techniques like co-immunoprecipitation, ChIP-seq, and siRNA knockdown.

How are sophisticated imaging techniques like live-cell microscopy harnessed to capture the real-time dynamics of IL-1α release and its impact on neighboring cells?

Live-cell microscopy captures real-time IL-1α release dynamics and its impact on neighboring cells, facilitated by fluorescent tagging and high-resolution imaging.

How is the quantitative relationship between IL-1α levels and disease progression established through longitudinal studies and statistical modeling?

Longitudinal studies and statistical modeling establish the quantitative relationship between IL-1α levels and disease progression, offering predictive insights.

How do multi-omics analyses, including transcriptomics and proteomics, provide a holistic view of the network of molecules influenced by IL-1α signaling?

Multi-omics analyses provide a holistic view of IL-1α signaling's impact, integrating transcriptomics, proteomics, and metabolomics data for comprehensive insights.