IL-1-beta Interleukin-1 beta Human Recombinant Protein, HEK
CAT:
519-PROTP01584-01
Size:
2 µg
Price:
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- Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
- Dry Ice Shipment: No


IL-1-beta Interleukin-1 beta Human Recombinant Protein, HEK
Description:
Interleukin-1 beta Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 18-25kDa due to glycosylation. The IL-1 beta is purified by proprietary chromatographic techniques.Synonyms:
Catabolin; Lymphocyte-activating factor (LAF) ; Endogenous Pyrogen (EP) ; Leukocyte Endogenous Mediator (LEM) ; Mononuclear Cell Factor (MCF) ; IL1F2; IL-1 betaGene Name:
IL1BUniProt:
P01584Reactivity:
HumanSource:
HEKSequence:
[object Object]Purification:
Greater than 95% as obsereved by SDS-PAGE.Bioactivity:
The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.Form:
Sterile Filtered White lyophilized (freeze-dried) powder.Reconstitution:
It is recommended to reconstitute the lyophilized IL-1b in sterile PBS containing 0.1% endotoxin-free recombinant HSA.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.Shipping Conditions:
AvailableStorage Conditions:
Lyophilized IL-1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) . Please prevent freeze-thaw cycles.Other Gene Names:
Interleukin-1 betaSubcellular Location:
Secreted. The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.
