R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
EPLIN (D1A7A) Rabbit mAb #50311
Filter:
- WB
- IF
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 85, 110 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
EPLIN (D1A7A) Rabbit mAb recognizes endogenous levels of total EPLIN protein, including EPLIN-α and EPLIN-β isoforms. Based on the absence of signal in NCI-H28 cells, which appear to express low levels of β-Eplin, this antibody may have a preference for α-Eplin by immunofluorescence.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly455 of human EPLIN protein.
Background
Epithelial Protein Lost in Neoplasm (EPLIN) is an actin-binding protein that regulates actin filament dynamics and cross-linking (1). Alpha and beta isoforms are generated from alternate promoters, with the EPLIN-β isoform representing the full-length protein and the EPLIN-α isoform lacking the amino-terminal 160 amino acids (2). Increased expression of EPLIN protein results in more abundant and larger actin stress fibers due to stabilizing of cross-links and inhibition of actin depolymerization. EPLIN protein inhibits Rac1-promoted membrane ruffling and Arp2/3-associated actin filament branching (1).
Research studies demonstrate reduced EPLIN-α expression in tumor tissues, and correlate this reduction with increased invasiveness and poor clinical outcomes (3). The EPLIN protein is an important negative regulator of the epithelial-mesenchymal transition (EMT)(4). While EMT is a critical process during normal embryonic development, dysregulation in transformed cells is a key step in the transition to metastasis (5).
Research studies demonstrate reduced EPLIN-α expression in tumor tissues, and correlate this reduction with increased invasiveness and poor clinical outcomes (3). The EPLIN protein is an important negative regulator of the epithelial-mesenchymal transition (EMT)(4). While EMT is a critical process during normal embryonic development, dysregulation in transformed cells is a key step in the transition to metastasis (5).
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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