Recombinant Prealbumin/Transthyretin Monoclonal Antibody (AN302048L)
For research use only.
| Verified Samples |
Verified Samples in WB: Human plasma, Human plasma Verified Samples in IHC: Human kidney |
| Dilution | WB 1:1000, IHC 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | Prealbumin/Transthyretin |
| Synonyms | HEL, HsT, TTR, CTS, CTS1, HEL111, HsT2651, PALB, TBPA, ATTR, Prealbumin, Transthyretin, Amyloid polyneuropathy, Amyloidosis I, Carpal tunnel syndrome 1, Dysprealbuminemic euthyroidal hyperthyroxinemia, Dystransthyretinemic hyperthyroxinemia, Epididymis luminal protein 111, Prealbumin amyloidosis type I, Prealbumin Thyroxine-binding, Senile systemic amyloidosis, Thyroxine binding prealbumin, Transthyretin, TTR, TTHY, TTR protein |
| Swissprot | |
| Calculated MW | 16 kDa |
| Observed MW |
35 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Secreted, Cytoplasm |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Neuroscience, Cardiovascular |
| Clone No. | A768 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Transthyretin (TTR) is a highly conserved homotetremric protein that is synthesized in the liver and choroid plexus of the brain. TTR wasoriginally discovered as a protein found in human plasma and cerebrospinal fluid (CSF). TTR transports thyroid hormones (TH) and retinol bybinding to retinol-binding protein. Although TTR is synthesized in the liver and choroid plexus, TTR is detected in blood plasma andcerebrospinal fluid migrating as monomers, dimers, and tetramers. Beyond its function as a carrier protein of TH and retinol in plasma andCSF, several additional TTR functions have been described, including proteolytic cleavage of specific substrates like apolipoprotein,neuropeptide Y (NPY), and APP. These neuronal substrates suggest a functional role for TTR in the central nervous system. Consistent witha CNS function, TTR null mice exhibit memory impairments and altered sensorimotor behavior). TTR may also be linked to neurodegenerativedisease: TTR levels in Alzheimer’s disease (AD) patients are negatively correlated with disease progression, and a protective role for TTR, atleast in AD mouse models, has been described. TTR itself may play a more direct role in disease as gain-of-function mutations in TTR causethe protein to misfold and aggregate into amyloid fibrils, contributing to autosomal dominant hereditary amyloidosis in diseases such as familialamyloid polyneuropathy, familial amyloid cardiomyopathy, and familial leptomeningeal amyloidosis. |
Other Clones
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Unconjugated
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