Specifications
- Assay duration:Multiple steps
- Assay Type (ELISA with LOV):Sandwich
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Human
- Target protein:VIM
- 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 Vimentin (VIM) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:3 h
- Shelf Life:12 Months
- Detection Range:7.8 - 500 ng/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:100 µl
- Sensitivity:3.0 ng/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-SEB040HU
- No. of tests:96 wells
Specifications
About this item
This assay has high sensitivity and excellent specificity for detecting Human VIM (Vimentin). The assay range is from 7.8 to 500 ng/ml (Sandwich kit) with a sensitivity of 3.0 ng/ml. There is no detectable cross-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%
Vimentin is a type III intermediate filament (IF) protein that is expressed in mesenchymal cells. IF proteins are found in all metazoan cells as well as bacteria. IF, along with tubulin-based microtubules and actin-based microfilaments, comprise the cytoskeleton. All IF proteins are expressed in a highly developmentally-regulated fashion; vimentin is the major cytoskeletal component of mesenchymal cells. Because of this, vimentin is often used as a marker of mesenchymally-derived cells or cells undergoing an epithelial-to-mesenchymal transition (EMT) during both normal development and metastatic progression. A vimentin monomer, like all other intermediate filaments, has a central α-helical domain, capped on each end by non-helical amino (head) and carboxyl (tail) domains.