Cat. # | Size | Qty. | Price |
---|---|---|---|
29872S | 100 µl |
|
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 15, 30, 45, 60 |
Source/Isotype | Rabbit IgG |
Product Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
For western blots, incubate membrane with diluted primary antibody in 5% w/v nonfat dry milk, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Loading of prestained molecular weight markers (#59329, 10 µl/lane) to verify electrotransfer and biotinylated protein ladder (#7727, 10 µl/lane) to determine molecular weights are recommended.
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 263
Human
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro106 of human Transthyretin protein.
Transthyretin (TTR) is a highly conserved homotetremric protein that is synthesized in the liver and choroid plexus of the brain. TTR was originally discovered as a protein found in human plasma and cerebrospinal fluid (CSF) (1). TTR transports thyroid hormones (TH) and retinol by binding to retinol-binding protein (2). Although TTR is synthesized in the liver and choroid plexus, TTR is detected in blood plasma and cerebrospinal fluid migrating as monomers, dimers, and tetramers. Beyond its function as a carrier protein of TH and retinol in plasma and CSF, several additional TTR functions have been described, including proteolytic cleavage of specific substrates like apolipoprotein, neuropeptide Y (NPY), and APP (3, 4, 5). These neuronal substrates suggest a functional role for TTR in the central nervous system. Consistent with a CNS function, TTR null mice exhibit memory impairments and altered sensorimotor behavior (6, 7). TTR may also be linked to neurodegenerative disease: TTR levels in Alzheimer’s disease (AD) patients are negatively correlated with disease progression, and a protective role for TTR, at least in AD mouse models, has been described (8, 9). TTR itself may play a more direct role in disease as gain-of-function mutations in TTR cause the protein to misfold and aggregate into amyloid fibrils, contributing to autosomal dominant hereditary amyloidosis in diseases such as familial amyloid polyneuropathy, familial amyloid cardiomyopathy, and familial leptomeningeal amyloidosis (10).
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