Recombinant Mouse IL-1a Protein

Name: Recombinant Mouse IL-1a Protein
Brand: Beta LifeScience
SKU: BL-1710NP
Availability: InStock

BL-1710NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Cytokines, Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Interleukin-1 Alpha is produced by our E.coli expression system and the target gene encoding Ser115-Ser270 is expressed.
Accession	P01582
Synonym	Interleukin-1 Alpha; IL-1 Alpha; Il1a
Gene Background	Mouse Interleukin-1 (IL-1) designates two proteins, IL-1α and IL-1β, which are the products of distinct genes, but recognize the same cell surface receptors. IL-1α and IL-1β are structurally related polypeptides that show approximately 25% homology at the amino acid level. Both proteins are produced by a wide variety of cells in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins. The proteins are synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17.5 kDa.
Molecular Mass	18 KDa
Apmol Mass	16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 50mM Tris-HCl, 200mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Subcellular Location	Cytoplasm. Secreted.
Protein Families	IL-1 family
Database References	KEGG: mmu:16175 STRING: 10090.ENSMUSP00000028882 UniGene: Mm.15534

Gene Functions References

Infection with Mycobacterium bovis results in increase in interleukin-1alpha, TGF-beta1, and MMP1 in multinucleated macrophages. PMID: 29504104
Together, these data suggest that caspase-11/IL-1alpha pathway plays an important role in defending against Klebsiella pneumoniae by recruiting neutrophils in the early stage of infection. PMID: 28939441
These data highlight an important interdependency between the potent pro-inflammatory cytokine IL1A and Fshr expression. PMID: 28337831
Since neither IL-1alpha nor IL-1beta depletions completely rescued the phenotype, we believe that IL-1alpha and IL-1beta have a similar and probably complementary role in FHF progression PMID: 28953903
These results suggested that Streptococcus pneuomoniae PLY induces the influx of calcium in Streptococcus pneumoniae-infected macrophages, followed by calpain activation and subsequent IL-1alpha maturation and secretion. PMID: 28630064
In response to chemically induced colitis, this microbial landscape promoted the release of IL-1alpha, which acted as a critical driver of colitis and colitis-associated cancer. PMID: 27775548
our results suggest that mature IL-1alpha induced by hS100A7 is via RAGE-p38 MAPK and calpain-1 pathway in keratinocyte and this mechanism may play an important role during psoriasis. PMID: 28060905
Il-1 signaling pathway has a key role in abdominal aortic aneurysm formation in mouse model of Kawasaki disease. PMID: 26941015
endothelial cells were identified as the primary cellular source of G-CSF during OPC, which responded to IL-1alpha that was released from keratinocytes in the infected tissue. PMID: 27632536
Key aspects of IL-1alpha biology and regulation especially with regard to inflammation are reviewed. Review. PMID: 27434011
data suggested that pINSd needs IL-1R1 for inflammatory cytokine induction. Mouse embryo fibroblast cells of IL-1R1-deficient mice further confirmed that pINSd promotes immune responses through IL-1R1 PMID: 27226621
IL-1alpha signaling and DNA damage is important for triggering a sterile inflammatory cascade . PMID: 26439902
As a dual function cytokine, IL-1alpha may contribute to the induction of CHOP intracellularly, while IL-1alpha released from necrotic cells accelerates steatohepatitis via induction of inflammatory cytokines by neighboring cells. PMID: 26022690
These data demonstrate that DC and macrophages display distinct patterns of cytokine regulation, particularly with respect to IL-1, as a consequence of cell-type specific differences in the physicochemical properties of the P2X(7)R PMID: 26068648
Data suggest the role of stromal cell IL-1alpha and IL-1beta in Kawasaki disease vasculitis model. PMID: 26515418
IL-1alpha and IL-36alpha form a self-amplifying inflammatory loop in vivo that in patients with insufficient counter regulatory mechanisms may become hyper-engaged and/or chronic PMID: 26203636
IL-1alpha-positive cells were identified in the epithelium in dextran sulfate sodium (DSS)-induced colitis. IL-1alpha was detected in the stool of colitic mice before IL-1beta. PMID: 25864926
IL-1alpha acts as an alarmin essential for leukocyte recruitment and protective immunity against HSV-1 PMID: 25323745
The aim of this study was to characterize the role of IL-1 in cellular responses of carbon nanotubes in cells from IL-1alpha/beta wild type (IL1-WT) mice. PMID: 25748835
These findings do not support the previously suggested role of nuclear IL-1alpha in gene regulation of IL-1beta. PMID: 25748836
the underlying mechanism by which AR influences AAA development is through IL-1alpha and transforming growth factor-beta1, and provides a potential new therapy to suppress/prevent AAA by targeting AR with ASC-J9. PMID: 26324502
inhibition of this potentially important source of chronic inflammation in atherosclerosis requires blockade of interleukin-1alpha and not interleukin-1beta. PMID: 26139463
The frustrated host response to Legionella pneumophila is bypassed by MyD88-dependent translation of pro-inflammatory cytokines. PMID: 25058342
data suggest that central inhibition of IL-1alpha or Tox3 overexpression during the acute phase of a CNS insult may be an effective means for preventing the loss of neurological function PMID: 26224856
Data (including date from studies in knockout mice) suggest that neutralization/deletion of Il1a reduces Il1b production and neutrophil infiltration in lung after inhalation exposure to silica nanoparticles. PMID: 25497724
The controlled release of IL-1alpha could be a critical regulator during acute liver inflammation PMID: 25870999
it appears the balance between TPO and IL-1alpha determines the MK cellular programming for thrombopoiesis in response to acute and chronic platelet needs. PMID: 25963822
In acute lung injury, lipopolysaccharide induced alveolar macrophage necrosis via CD14 and the P2X7 receptor leading to interleukin-1alpha release. PMID: 25862090
IL-1alpha induced the proliferation of CD11b(low) alveolar macrophages and differentiated these cells into CD11b(high) macrophages which perform critical phagocytic functions and organize granuloma. PMID: 25421226
Data indicate that interleukin-1 cytokines IL-1alpha and IL-1beta are regulated by polyubiquitination and proteasomal degradation. PMID: 25371210
IL-1 is a key mediator driving an innate immune response to inflammatory challenge in the mouse brain but is dispensable in extracerebral tissues including the lung and peritoneum. PMID: 25367678
findings identify IL-1alpha as a crucial early danger signal triggering post-MI inflammation. PMID: 25505286
Immune complexes inhibit IL-1 secretion and inflammasome activation. PMID: 25320279
Selective deficiency of IL-1alpha in Kupffer cells reduces liver inflammation and expression of inflammatory cytokines, which may implicate Kupffer cell-derived IL-1alpha in steatohepatitis development. PMID: 24582082
cigarette smoke-induced neutrophilia was dependent on IL-1alpha produced by alveolar macrophages and alveolar macrophages isolated from smoke-exposed mice were primed for excessive IL-1alpha production in response to bacterial ligands. PMID: 25092891
tested the possible role of the proinflammatory cytokine IL-1 in the age-related exhaustion of ovarian reserve using IL-1alpha and IL-1beta-KO mice PMID: 25114230
This study documents distinct roles for IL-1alpha and IL-1beta in the response to Pseudomonas aeruginosa infection as a function of the type 3 secretion system effectors produced by the infecting strain. PMID: 25069982
necroptosis caused the processing and release of IL-1alpha, and this was independent of IL-1beta processing and release PMID: 24790078
IL-1 induces systemic inflammation and augments Streptococcal pneumoniae infection, atherosclerosis, and ischemic brain injury via platelet activation and microvascular coagulation. PMID: 24644058
IL-1alpha was not released upon inflammasome activation unless significant cell damage occurred. PMID: 23684408
haematopoietic-derived IL-1 is a key driver of ischaemic brain injury. PMID: 23519030
In severe S. aureus bacteraemia in mice, TNF-alpha, IL-1alpha, and KC are biomarkers predicting fatal outcome of infection. PMID: 23520553
Our results establish IL-1alpha as a critical initiator of the inflammatory response to L. pneumophila PMID: 23686480
discovery of a novel inflammatory circuit in which RIP1-mediated IL-1alpha secretion in response to deregulated SHP-1 activity triggers an inflammatory destructive disease that proceeds independently of inflammasomes and programmed necrosis PMID: 23708968
Results suggest importance of IL-1R1/IL-1alpha to the recruitment and activation of dendritic cells in response to cigarette smoke exposure. PMID: 22992200
ERalpha-regulated repression of TNFalpha and IL1alpha is important for lumen formation and maintenance. PMID: 22328525
Allergic sensitization to HDM was abolished in vivo when IL-1alpha, GM-CSF, or IL-33 was neutralized. PMID: 22802353
Autophagy has a potentially pivotal role to play in the induction and regulation of inflammatory responses by innate immune cells, largely driven by IL-1 and its consequential effects on IL-23 secretion. PMID: 22972933
Vascular wall resident cells are the main targets for the pro-atherogenic effects of bone marrow-derived IL-1 through IL-1R1, partly by induction of adhesion and chemotactic molecules in endothelial cells. PMID: 22236482
This study demonstrated here in in vivo experiments that IL-1 exacerbates the effects of SCI by accentuating the impact of the inflammatory responses. PMID: 22483094

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.