Pan-Keratin (Type I) (E6S1S) & CO-0072-594 SignalStar™ Oligo-Antibody Pair #30754
- IHC
Order Information # 30754
This product is not sold separately. Please see the SignalStar™ Multiplex IHC Panel Builder Tool for ordering information.
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| SignalStar™ Leica Bond | 1:50 - 1:200 |
| SignalStar™ Manual | 1:50 - 1:200 |
Storage
Product Description
SignalStar Oligo-Antibody Pairs are compatible with the SignalStar Multiplex IHC Buffer Kits for use in fluorescent multiplex imaging experiments. This product includes the oligo-conjugated antibodies and complementary oligos required for labeling your target protein on up to 10 slides. SignalStar Multiplex IHC Buffer Kits are required to amplify and image the target signal. Multiple oligo-antibody pairs can be conveniently combined into a multiplex panel using the SignalStar Multiplex IHC Panel Builder. SignalStar Multiplex IHC Kits & Reagents are not compatible with all of Cell Signaling Technology® products and protocols that are recommended for use in immunohistochemical assays.
Protocol
Specificity / Sensitivity
Pan-Keratin (Type I) (E6S1S) Rabbit mAb (SignalStar™ Conjugate 0072) recognizes endogenous levels of total type I keratin protein. The antibody was validated to detect overexpressed keratin 10, 17, and 18. By homology, it is also predicted to detect keratin 13, 14, 15, 16, and 19. It does not detect type II keratins including keratin 1, 5, 6a, 7, and 8. Non-specific staining was observed in Leydig cells of the testis by immunohistochemistry.
Species Reactivity:
Human, Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a mix of synthetic peptides corresponding to residues highly conserved among type I keratins.
Background
Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins K9-K28) and a basic keratin (or type II keratin, keratins K1-K8 and K71-K80) assemble to form filaments. Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research and clinical biomarkers (1,2).
Dysregulation/mutations in keratin genes can lead to a variety of disorders affecting the skin, hair, nails, and other epithelial tissues (3). While expression of keratins can be variable, immunohistochemical staining of keratins is widely used to help in the identification and classification of epithelial tumors, and may also provide prognostic information.
Keratins 8 and 18 (K8/K18) are expressed in simple epithelia of normal tissue, as well as in adenocarcinomas of the breast, lung, ovary, and gastrointestinal tract. Keratin 17 is expressed in basal keratinocytes of stratified epithelia, hair follicles, and sebaceous glands. Onset of keratin 17 expression coincides with the definition of major epithelial lineages during skin development (4). Keratin 14 (K14) is expressed in basal cells of stratified epithelia, and in basal-like subtypes of breast cancer and squamous cell carcinomas. Keratin 19 (K19) is expressed in glandular epithelia, including the liver, gallbladder, and pancreas, as well as in adenocarcinomas of the breast, thyroid, and bile duct. Keratin 20 (K20) is expressed in gastrointestinal epithelium, urothelium, and Merkel cells in the skin, as well as in colorectal carcinomas and some urothelial carcinomas. Keratin 5/6 (K5/6) is expressed in basal cells of stratified epithelia, including the skin, prostate, and breast, as well as in basal-like breast cancers, squamous cell carcinomas, and some lung carcinomas. Keratin 7 (K7) is expressed in glandular epithelia, such as those in the lung, breast, and female reproductive tract, as well as in adenocarcinomas of the lung, breast, and ovary (5,6).
Keratins, particularly K8, K18, and K19, serve as biomarkers for identification of circulating tumor cells (CTCs) (5).
Post-translational modifications, including phosphorylation, acetylation, ubiquitylation, sumoylation, glycosylation, and transamidation, have been shown to affect the functions of keratins in normal and disease states (6). Understanding the molecular mechanisms underlying these PTMs may provide insights into cancer pathogenesis.
- Chang, L. and Goldman, R.D. (2004) Nat Rev Mol Cell Biol 5, 601-13.
- Schweizer, J. et al. (2006) J Cell Biol 174, 169-74.
- Sarma, A. (2022) Int J Biol Macromol 219, 395-413.
- McGowan, K.M. and Coulombe, P.A. (1998) J Cell Biol 143, 469-86.
- Werner, S. et al. (2020) Mol Aspects Med 72, 100817.
- Dmello, C. et al. (2019) J Biosci 44, 33.
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