Biolegend, 843101, Recombinant Human Tau-412 (1N4R) (Previously Covance catalog# PTN-5278), 25μg

Tau proteins are microtubule-associated protein (MAPs) which are abundant in neurons of the central nervous system, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes and elsewhere. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is active primarily in the distal portions of axons providing microtubule stabilization as well as flexibility. Pathologies and dementias of the nervous system such as Alzheimer's disease feature tau proteins that have become defective and no longer stabilize microtubules properly. As a result, tau forms aggregates with specific structural properties referred to as Paired Helical Filaments (PHFs) that are a characteristic of many different types of dementias, known as tauopathies. Tau has two primary ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in human brain tissue, and they are distinguished by the number of binding domains. Three isoforms have three binding domains and the remaining three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (for binding to the negatively-charged microtubule). Tau isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They also differ in either zero, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-binding regions at the C-terminus. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). Tau is also a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. Phosphorylation has been reported on approximately 30 of these sites in normal tau proteins. Mechanisms that drive tau lesion formation in the highly prevalent sporadic form of AD are not fully understood, but appear to involve abnormal post-translational modifications (PTMs) that influence tau function, stability, and aggregation propensity.
25μg
Verified Reactivity: Human
Purity: >90% by SDS-PAGE
Formulation: 50 mM Tris-HCl, 300 mM NaCl, 10% Glycerol, 0.5 mM TCEP, pH 8.
Concentration: 0.1 mg/mL
Storage & Handling: Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Application: WB - Quality tested
Recommended Usage: The optimal working dilution should be determined for each specific assay condition. • WB: Recommended load amount of 0.2-0.5 μg/lane
Application Notes: This protein has utility in immunoblotting (WB). Uni Prot ID: P10636-7 WB Expected MW: 60 kD Tau-412 MW: 42.9 kD 8X His-tag Tau-412 MW: 45.2 kD WB Positive Control: TAU 5 antibody (Catalog No. 806403)
Biology Area: Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family: Tau
Gene ID: 4137
UniProt: View information about Tau-412 1N4R on UniProt.org
Regulatory Status: RUO
Other Names: Microtubule-Associated Protein Tau, Phf-Tau, Paired Helical Filament-Tau, Neurofibrillary Tangle Protein, Microtubule-Associated Protein Tau, Isoform 4, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1
Previously: Covance Catalog# PTN-5278
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Q: How does the activity of your recombinant proteins compare to competitors?
A: We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
Q: What is the specific activity or ED50 of my recombinant protein?
A: The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
Q: Have your recombinants been tested for stability?
A: Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
Q: Does specific activity of a recombinant protein vary between lots?
A: Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
Q: How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
A: Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)