Analysis Note
ControlHuman cortex tissue lysate
Application
Research Sub CategoryNeurodegenerative Diseases
Research CategoryNeuroscience
Anti-TMEM106B, clone TME-N 6F2 detects levels of TMEM106B proteins & has been published & validated for use in WB & IF.
Immunofluorescence Analysis: A 1:50 dilution from a representative lot detected TMEM106B in rat cerebellum tissue.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Transmembrane protein 106B (TMEM106B) is a single-pass type II membrane protein present in endosomal and lysosomal membranes, and is highly expressed in the frontal cortex. Increased TMEM106B expression in the brain may be linked to mechanisms of disease in frontotemporal lobar degeneration with TAR DNA-binding protein (TDP-43) inclusions (FTLD-TDP). Frontotemporal lobar degeneration (FTLD) is the second most common cause of presenile dementia.
Immunogen
Recombinant protein corresponding to the N-terminus of human TMEM106B.
Epitope: N-terminus
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Protein G Purified
Purified rat monoclonal IgG2c in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Format: Purified
Quality
Evaluated by Western Blot in human cortex tissue lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected TMEM106B in 10 µg of human cortex tissue lysate.
Specificity
This antibody recognizes the N-terminus of TMEM106B.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Target description
~30 kDa observed (At higher antibody concentrations, this protein may be observed at ~45 kDa). This protein may be observed at ~50 kDa due to glycosylation (Lang, C. M., et al. (2012). J Biol Chem. 287(23):19355-19365.).
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