Rabbit Polyclonal GAPDH antibody. Suitable for ELISA, I-ELISA, ICC/IF and reacts with Enterobacteria phage M13 samples. Cited in 10 publications.
IgG
Rabbit
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 0.0268% PBS
Liquid
Polyclonal
| ELISA | I-ELISA | ICC/IF | |
|---|---|---|---|
| Enterobacteria phage M13 | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Enterobacteria phage M13 | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Enterobacteria phage M13 | Dilution info - | Notes At least 1/1000 for 5 x107 phage/mlat least 1/8000 for 5 x 1010 phage/ml. |
| Species | Dilution info | Notes |
|---|---|---|
Species Enterobacteria phage M13 | Dilution info Use at an assay dependent concentration. | Notes - |
Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.
VI, VII, IX, Capsid protein G8P
Attachment protein G3P, Gene 3 protein, Minor coat protein, G3P, III
Rabbit Polyclonal GAPDH antibody. Suitable for ELISA, I-ELISA, ICC/IF and reacts with Enterobacteria phage M13 samples. Cited in 10 publications.
IgG
Rabbit
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 0.0268% PBS
Liquid
Polyclonal
IgG fraction
Blue Ice
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Concentration: 5.5 mg/ml- 7.5 mg/ml
Can be used as a capture antibody when coated directly on microtiter plates, or as a primary detection antibody for specifically captured M13 or fd phage. May be useful in rapidly sorting large phage display libraries (antibody, peptide etc.) with the expressed proteins fused to either the gene III or gene VIII protein of the filamentous phage.
May be used as a reagent in "phage ELISA" offering sensitive and specific activity for detection of recombinant phages.
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This supplementary information is collated from multiple sources and compiled automatically.
The M13 bacteriophage coat proteins also known as the phage display proteins play an important role in the structure and functionality of the M13 phage. Commonly referred to as filamentous bacteriophage proteins these coat proteins include pVIII the major coat protein along with pIII pVI pVII and pIX which are minor coat proteins. The mass of pVIII is approximately 5kDa. These coat proteins are expressed on the surface of the M13 bacteriophage primarily after infection of host bacteria like Escherichia coli facilitating the assembly and stability of the phage particle.
M13 phage coat proteins are essential in the assembly and secretion process of the bacteriophage. These proteins form a cylindrical structure encasing the single-stranded DNA core critical for the infection cycle of the virus. During M13 phage display technique scientists exploit these coat proteins to present foreign proteins or peptides on the surface. This capability allows these phage particles to function as tools for molecular library screening and antibody engineering. Although not part of a traditional multiprotein complex they work coordinately to maintain phage integrity and facilitate propagation.
M13 phage coat proteins are integral to the phage assembly and secretion pathways. These pathways occur in the bacterial host and ensure the correct encapsulation of the single-stranded DNA genome. Related proteins in these processes include bacterial proteins that participate in host cell machinery like the Tol and Pal system which interact with coat proteins like pIII during the phage infection cycle. These interactions are fundamental for the phage's continued life cycle and its use in biotechnological applications like phage ELISA.
M13 phage coat proteins have potential implications in cancer and infectious disease research. The M13 bacteriophage due to these coat proteins' adaptability has been used to create phage display libraries aiding in the discovery of biomarkers and target molecules. These coat proteins have been linked with tumor-targeting peptides improving cancer diagnostic and therapeutic strategies. Furthermore researchers have explored their connection with other proteins in immunology for vaccine development against pathogens. This connection highlights their significance in experimental therapeutics.
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