Render Target: STATIC
Render Timestamp: 2024-10-11T09:49:06.022Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:54:51.581
Product last modified at: 2024-09-30T08:01:57.842Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Transthyretin (D8T4Q) Rabbit mAb #29872

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 15, 30, 45, 60
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    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

    Transthyretin (D8T4Q) Rabbit mAb recognizes endogenous levels of total Transthyretin protein in its monomeric, dimeric, trimeric, and tetrameric forms.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro106 of human Transthyretin protein.

    Background

    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). 
    For Research Use Only. Not For Use In Diagnostic Procedures.
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