This human IL1A kit is a highly sensitive in-vitro chemiluminescent immunoassay for the measurement of trace amounts of analytes in serum, plasma and other biological fluids.
Applications
CLIA
Reactivity
Human
Sensitivity
2.34pg/mL
Detection Limit
3.91~250pg/mL
Note
FOR SCIENTIFIC EDUCATIONAL RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR OTHER MEDICAL APPLICATIONS.
Product Properties
Storage Instruction
If unopened the kit may be stored at 2-8°C for up to 1 month. If the kit will not be used within 1 month, store the components separately, according to the component table in the manual.
This kit recognizes Human IL-1 Alpha in samples. No significant cross-reactivity or interference between Human IL-1 Alpha and analogues was observed.
Sample Type
Serum, plasma and other biological fluids
Additional Info
Post Translational Modifications
Acetylated within its nuclear localization sequence, which impacts subcellular localization. Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A.
Function
Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity.
NucleusCytoplasmSecretedThe 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 ProteinsThe Secretion Is Dependent On Protein Unfolding And Facilitated By The Cargo Receptor Tmed10It Results In Protein Translocation From The Cytoplasm Into The Ergic (Endoplasmic Reticulum-Golgi Intermediate Compartment) Followed By Vesicle Entry And SecretionRecruited To Dna Damage Sites And Secreted After Genotoxic Stress
