- Assay duration:Multiple steps
- Assay Type (ELISA with LOV):Sandwich
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Rat
- Target protein:IL1a
- Size:1 Kit
- Sample Type:Serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids
- Cross Reactivity:No significant cross-reactivity or interference between Interleukin 1 Alpha (IL1a) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:3 h
- Shelf Life:12 Months
- Detection Range:15.6 - 1000 pg/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:100 µl
- Sensitivity:6.1 pg/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-SEA071RA
- No. of tests:96 wells
This assay has high sensitivity and excellent specificity for detecting Rat IL1a (Interleukin 1 Alpha). The assay range is from 15.6 to 1000 pg/ml (Sandwich kit) with a sensitivity of 6.1 pg/ml. There is no detectable cross to reactivity with other relevant proteins. Activity loss rate and accelerated stability test ect have been conducted to guarantee the best performance of the products after long storage and delivery.
- High sensitivity and specificity
- Perfect reproducibility and consistency across batches
- Quality control with three-level inspections
- Wide range of targets/species available
- Intra-Assay: CV <10%, Inter-Assay: CV <12%
IL-1α is a member of interleukin 1 family. IL-1α and IL-1β recognize the same IL-1 receptor and share a number of similar biological functions. IL-1α is predominantly a cell-associated molecule whereas IL-1β is a secreted molecule. IL-1α is synthesized primarily as a 31 kDa precursor that lacks a signal peptide. Cleavage of the precursor is via the cysteine protease calpain, resulting in a 17.5 kDa mature IL-1 molecule. Being active in the processed form, the IL-1 precursor is also biologically active via specific cell binding. A portion of the precursor is transported to the cell surface and associated with the cell membrane. Precursor IL-1α can be released and cleaved by extracellular proteases when the cells die, and can also be cleaved by activation of the calcium-dependent, membrane-associated calpains.