Pab to Keratin K14 Cat. No. GP-CK14

PROGEN Biotechnik GmbH  Maaßstraße 30  69123 Heidelberg Germany
Tel.: +49 (0) 6221 8278-0  Fax: +49 (0) 6221 8278-24  Email: [email protected]  Web: www.progen.de
Pab to
Keratin K14
Source
Guinea pig (GP CK 14-2.3)
Form
Stabilized antiserum
Antigen
Peptide against human K14 C-VSTHEQVLRTKN (460-472)
Reactive Polypeptide (Specificity)
Acidic keratin K14 (Mr 50 000; formerly also designated cytokeratin
14), expressed in basal and first suprabasal layers of epidermis
Antigen Recognized in
Species (tested so far)
Human, mouse
Bovine (predicted)
Reactivity on Cultured Cell Lines
(tested so far)
BPH-1 (derived from non-neoplastic prostatic tissue)
Tumors Specifically Detected
The antiserum reacts with keratin K14, expressed in the basal cells of
the larynx, esophagus, trachea, bladder, prostate, cervix, vagina,
breast acini, skin and sweat glands. In several studies the correlation
between the expression of keratin K14 in different types of carcinomas
(putatively derived from basal epithelial cells) and prognosis has been
discussed (see references listed below).
Application
Suitable for
 immunohistochemistry on frozen* & paraffin-embedded** tissue
 cytological material
 immunoblotting*** (Western)
Working Dilution
*
**
***
Incubation Time
1 h at RT; extended with paraffin-embedded material
Storage
At 2-8°C
Volume
100 µl; contains 0.09% sodium azide and 0.5% BSA
1:100 - 1:200 for immunohistochemistry
1:50 for paraffin-embedded tissue
1:5000 - 1:10 000 for Western blotting
For research use only, not for therapeutic or diagnostic use!
References
Demirkesen C, Hoede N, Moll R: Epithelial markers and differentiation in adnexal neoplasms of the skin: an immunohistochemical
study including individual cytokeratins. J Cutan Pathol 22: 518-535 (1995).
Moll R. et al.: Differenzierungsmarker bei gynäkologischen Tumoren: Methodische und diagnostische Aspekte. In: Aktuelle Aspekte der
Tumorimmunologie in der Gynäkologie. W. Zuckschwerdt Verlag (1995).
Hofmann I, Mertens C, Brettel M, Nimmrich V, Schnölzer M, Herrmann H: Interaction of plakophilins with desmoplakin and intermediate
filament proteins: an in vitro analysis. J Cell Science 113, 2471-2483 (2000).
Herrmann T, van der Hoeven F, Groene HJ, Stewart AF, Langbein L, Kaiser I, Liebisch G, Gosch I, Buchkremer F, Drobnik W, Schmitz
G, Stremmel W: Mice with targeted disruption of the fatty acid transport protein 4 (Fatp 4, Slc27a4) gene show features of lethal
restrictive dermopathy. J Cell Biol 161, 1105-1115 (2003).
Langbein L, Pape U-F, Grund C, Kuhn C, Praetzel S, Moll I, Moll R, Franke WW: Tight junction-related structures in the absence of a
lumen: Occludin, claudins and tight junction plaque proteins in densly packed cell formations of stratified epithelia and squamous cell
carcinomas. Eur J Cell Biol 82, 385-400 (2003)
Jennemann R, Sandhoff R, Langbein L, Kaden S, Rothermel U, Gallala H, Sandhoff K, Wiegandt H, Gröne H-J: Integrity and barrier
function of the epidermis critically depend on glycosylceramide synthesis. J Biol Chem 282, 3083-3094 (2007)
Yang C, Fischer-Kešo R, Schlechter T, Ströbel P, Marx A, Hofmann I: Plakophilin 1-deficient cells upregulate SPOCK1: implications for
prostate cancer progression. Tumor Biol. (2015) DOI 10.1007/s13277-015-3628-3
Cat. No.
GP-CK14
GP-CK14/DS-271016