Recombinant Human Interleukin 1, Alpha, Fc Chimera
| Cat.No. : | IL1A-109H |
| Product Overview : | Recombinant Human interleukin 1, alpha encoding the signal peptide and extracellular domain of human IL-1 Receptor I (IL-1RI) (aa 1-333) , was expressed in modifiedhuman 293 cells. It was fused to the Fc region of human IgG1 (aa 93-330). |
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| Cat. No. : | IL1A -109H |
| Description : | Interleukin 1, alpha Fc Chimera is an 80kDa type I transmembrane glycoprotein expressed on T cells and fibroblasts. Structurally the extracellular domain (ECD) of IL-1R1 contains 3 Immunoglobulin like domains. Glycosylation of IL-1R1has been shown to be necessary for optimal binding of IL-1, as blocking of glycosylation sites reduces binding to IL-1. |
| Source : | Human 293 cells. |
| Amino Acid Sequence : | LEADKCK EREEKIIL VS SANEIDVR PCP LNPNEHK GTITWYK DDSKTP VSTEQA SRIHQ HKEKLWF VPAKVED SGHYY CVVR NSSY CLRIK ISAK FVE NEP NL CY NAQAIFKQK LPVAGDGGLVC PYMEFFK NENN EL PK LQ W YK DCKPLLLDNI HFSG VKDRLIVM NVAEKH RGNYTCH ASYTYLG KQYPITRVIE FIT LEE NKPT RPVIVSP ANETMEVDLG SQIQLICNVTGQL SDIAYWKWNGSVIDE DDPVLGE DYYSVE NPANKR RSTLI TVLNIS EIESRFYK HPFTCFAKN THGIDAAYIQ LIYPVTNRSS NTKV DKK VEPKS CDKTH TCPPCP AP ELLGGPSV FL FPP KPK DTLMISRTPEVTCVVVDVSHEDPE VKFNWY VDGVEV HNAKTK PREEQY NSTY RVVSVL TVLHQD WLNGK EYKCR VSNKALP APIEKTISKAKGQ PREPQ YTL PPSRDE LTKNQVSLTCL VKGFYPSDIAV EWESNGQPEN NYKTTPPVLDSD GSF FLYSKL TVDKS RWQQGNV FSCSVM HEALH NHYTQKSLSLSPGK. |
| Molecular Mass : | Interleukin 1, alpha Fc Chimera migrates as a broad band between 65 and 100 kDa in SDS-PAGE due to post-translation modifications, in particular glycosylation. This compares with unmodified IL-1RI-Fc that has a predicted molecular mass of 63.6 kDa. |
| pI : | Interleukin 1, alpha Fc Chimera separates into a number of isoforms with a pI between 5 and 8 in 2D PAGE due to post-translational modifications, in particular glycosylation. This compares with the unmodified IL-1RI-Fc that has a predicted pI of 7. |
| % Carbohydrate : | Purified Interleukin 1, alpha Fc Chimera consists of 0-36% carbohydrate by weight. |
| Glycosylation : | Interleukin 1, alpha Fc Chimera has N-linked and may have O-linked oligosaccharides. |
| Purity : | >95%, as determined by SDS-PAGE and visualized by silver stain. |
| Formulation : | When reconstituted in 0.5 ml sterile phosphate-buffered saline, the solution will contain 1% human serum albumin (HSA) and 10% trehalose. |
| Reconstitution : | It is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. |
| Storage : | Lyophilized products should be stored at 2 to 8°C. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. Repeated freeze thawing is not recommended. |
| Gene Name : | IL1A interleukin 1, alpha [ Homo sapiens ] |
| Synonyms : | IL1A; interleukin 1, alpha; IL1; IL-1A; IL1F1; IL1-ALPHA; preinterleukin 1 alpha; hematopoietin-1; pro-interleukin-1-alpha; Interleukin-1 alpha;IL-1 alpha; Hematopoietin-1; IL1A (IL1F1) |
| Gene ID : | 3552 |
| mRNA Refseq : | NM_000573 |
| Protein Refseq : | NP_000566 |
| MIM : | 147760 |
| UniProt ID : | P01583 |
| Chromosome Location : | 2q14 |
| Pathway : | Apoptosis; Cytokine-cytokine receptor interaction; Graft-versus-host disease; Hematopoietic cell lineage; MAPK signaling pathway; Prion diseases; Type I diabetes mellitus |
| Function : | cytokine activity; interleukin-1 receptor binding; protein binding |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionCross-talk between IL-1α's and other cytokines is dissected through methods such as co-immunoprecipitation, ELISA, and cytokine profiling arrays.
IL-1α's paradoxical roles are dissected using conditional knockout mice, 3D culture systems, and molecular analyses to delineate context-specific effects.
Single-cell RNA sequencing uncovers heterogeneity in IL-1α-responsive cell populations and their roles, revealing distinct molecular profiles and functions.
IL-1α's intricate pro-inflammatory signaling pathways are decoded using advanced techniques like mass spectrometry, phosphoproteomics, and bioinformatics.
Genetic editing tools like CRISPR-Cas9 unveil IL-1α's contributions to diseases by generating knockout models and studying resulting phenotypic changes.
In vitro co-culture systems are manipulated to study IL-1α-mediated responses, elucidating immune-stromal cell interactions via cytokine-specific neutralization.
Specific cellular receptors and effectors influenced by IL-1α are identified through techniques like co-immunoprecipitation, ChIP-seq, and siRNA knockdown.
Live-cell microscopy captures real-time IL-1α release dynamics and its impact on neighboring cells, facilitated by fluorescent tagging and high-resolution imaging.
Longitudinal studies and statistical modeling establish the quantitative relationship between IL-1α levels and disease progression, offering predictive insights.
Multi-omics analyses provide a holistic view of IL-1α signaling's impact, integrating transcriptomics, proteomics, and metabolomics data for comprehensive insights.
Customer Reviews (3)
Write a reviewHigh solubility. -
Good for intracellular staining. -
Effective in apoptosis assays. -
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