Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to
worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting
immunostaining in relation to complex human pathologies.
TCR Screening Services
Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding.
Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".
MBP Tag antibody was raised against the MBP epitope tag recombinant protein.
MBP and is useful in determining its presence in various assays. This polyclonal anti-MBP tag antibody detects over-expressed proteins containing the MBP epitope tag. To date this antibody has reacted with all MBP tagged proteins so far tested. In western blotting of bacterial extracts the antibody does not cross-react with endogenous proteins
Anti-MBP is optimally suited for monitoring the expression of MBP tagged fusion proteins. As such, anti- MBP/MBP can be used to identify fusion proteins containing the MBP epitope. The antibody recognizes the MBP epitope tag fused to the amino- or carboxy- termini of targeted proteins. This antibody has been tested by ELISA and western blotting against MBP containing recombinant proteins. Although not tested, this antibody is likely functional for immunoprecipitation and immunocytochemistry, and other immunodetection techniques. Maltose binding protein is a bacterial protein, which is often used in protein expression studies because it creates a stable fusion product that does not appear to interfere with the bioactivity of the protein of interest. It also allows for its easy purification from bacterial extracts under mild conditions. Anti-MBP is a companion to the pMAL protein expression system and can be used for the detection and purification of MBP-fusion proteins expressed in E. coli. By Western blot, a band is seen at ~42 kD representing MBP.
0.02 M potassium phosphate, 0.15 M sodium chloride, pH 7.2, 0.01% sodium azide.
1 ml deionized water
Long term: -20°C; Short term: +4°C. Avoid repeat freeze-thaw cycles.
Anti-Maltose Binding Protein (MBP) Epitope Tag Antibody - Western Blot. Anti-MBP epitope tag polyclonal antibody detects MBP-tagged recombinant proteins by western blot. Polyclonal rabbit-anti-MBP epitope tag at 0.5-1.0 ug/ml was used to detect 1.0 ug of recombinant protein containing the MBP epitope tag. The apparent molecular weight of this band is 42 kD. A minor band at corresponding to multimers of this protein is also evident. A 4-20% gradient gel was used to separate the protein by SDS-PAGE. The protein was transferred to nitrocellulose using standard methods. After blocking the membrane was probed with the primary antibody for 1 h at room temperature followed by washes and reaction with a 1:2500 dilution of IRDye 800 conjugated Gt-a-Rabbit IgG [H&L] (code for 30 min at room temperature. LICORs Odyssey Infrared Imaging System was used to scan and process the image. Other detection systems will yield similar results.
Rb Anti-Maltose Binding Protein Antibody - Western Blot. Western Blot showing detection of Maltose Binding Protein (MBP) (0.05 ug) in Lane 2. MW markers indicated in Lane 1. Protein was run on a 4-20% gel and transferred to 0.45 micron nitrocellulose. After blocking with 1% BSA-TTBS (MB-013, diluted to 1X) 30 min at 20°C Anti-MBP (RABBIT) antibody (p/n LS-C59538) was used at 1:1000 overnight at 4°C. Anti-Rabbit IgG (GOAT) IRDye800 conjugated antibody (p/n secondary antibody was used at 1:20000 in Blocking Buffer for Fluorescent Western Blot (p/n MB-070) for 30 min at 20°C and imaged on the LiCor Odyssey imaging system. A band is present at the correct molecular weight, ~42 kD, the other bands present are recombinant MBP breakdown.
Requested From: United States
Date Requested: 1/22/2017