GenScript

Avi Tag Monoclonal Antibody (1D11D10)

Avi Tag Antibody in Immunocytochemistry (ICC/IF)

FIGURE: 1 / 5

Avi Tag Antibody (A01738-40) in ICC/IF

Immunocytochemistry/Immunofluorescence analysis of Ai tagged protein transfected CHO cells using Ai Tag Antibody, mAb, Mouse (GenScript, A01738) and Mouse IgG Control (GenScript, A01007). The signal was developed with FITC conjugated Goat Anti-Mouse IgG.

Avi Tag Antibody in Flow Cytometry (Flow)

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Product Details

A01738-40

Applications

Tested Dilution

Publications

Western Blot (WB)

0.2-1 µg/mL

Immunocytochemistry (ICC/IF)

1-3 µg/mL

Flow Cytometry (Flow)

1-3 µg 1 x 10^6 cells

ELISA (ELISA)

0.02-0.05 µg/mL

Miscellaneous PubMed (MISC)

View 3 publications 3 publications

Product Specifications

Species Reactivity

Tag

Host/Isotype

Mouse / IgG2a, kappa

Class

Monoclonal

Type

Antibody

Clone

1D11D10

Immunogen

Avi peptide conjugated to KLH

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

Protein A

Storage buffer

PBS, pH 7.4

Contains

0.02% sodium azide

Storage conditions

-20°C or -80°C if preferred

Shipping conditions

Ambient (domestic); Wet ice (international)

Product Specific Information

Reconstitute the lyophilized product with deionized water (or equivalent) to make antibody concentration of 0.5 mg/ml.

Avi tag is a biotin-acceptor peptide, GLNDIFEAQKIEWHE. The 15-residue peptide served as a substrate mimic for biotin ligase (BirA), which usually recognizes the much larger protein domain. Avi Tag Antibody is a useful tool in analysis of Avi fusion proteins.

Target Information

The Avi tag is a biotin-acceptor peptide1, GLNDIFEAQKIEWHE. The 15-residue peptide served as a substrate mimic for biotin ligase (BirA), which usually recognizes the much larger protein domain.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

High-Throughput Mapping of B Cell Receptor Sequences to Antigen Specificity.

Cell

Setliff I,Shiakolas AR,Pilewski KA,Murji AA,Mapengo RE,Janowska K,Richardson S,Oosthuysen C,Raju N,Ronsard L,Kanekiyo M,Qin JS,Kramer KJ,Greenplate AR,McDonnell WJ,Graham BS,Connors M,Lingwood D,Acharya P,Morris L,Georgiev IS

B cell receptor (BCR) sequencing is a powerful tool for interrogating immune responses to infection and vaccination, but it provides limited information about the antigen specificity of the sequenced BCRs. Here, we present LIBRA-seq (linking B cell receptor to antigen specificity through sequencing), a technology for high-throughput mapping of paired heavy- and light-chain BCR sequences to their cognate antigen specificities. B cells are mixed with a panel of DNA-barcoded antigens so that both t

Thu Dec 12 00:00:00 UTC 2019

Human antibody-based chemically induced dimerizers for cell therapeutic applications.

Nature chemical biology

Hill ZB,Martinko AJ,Nguyen DP,Wells JA

Chemically induced dimerizers (CIDs) have emerged as one of the most powerful tools for artificially regulating signaling pathways in cells; however currently available CID systems lack the properties desired for use in regulating cellular therapies. Here we report the development of human antibody-based chemically induced dimerizers (AbCIDs) from known small-molecule-protein complexes by selecting for synthetic antibodies that recognize the chemical epitope created by the bound small molecule.

Thu Feb 01 00:00:00 UTC 2018

Characterization of GPCRs in extracellular vesicle (EV).

Methods in cell biology

Medapati MR,Singh A,Korupally RR,Henderson D,Klonisch T,Manda SV,Chelikani P

Extracellular vesicle (EV) are tiny membranous vesicles usually <500nm in size that recently emerged as a new paradigm in human intercellular signaling. EVs have shown a promising role in development of diagnostic markers in many pathophysiological disorders. The presence of chemosensory and therapeutically relevant G protein-coupled receptors (GPCRs) on EV membranes is poorly characterized. Here, we compare different methods including ultracentrifugation and polymer-charge-based separation to i

Thu May 24 00:00:00 UTC 2018

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