JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB130757

Anti-MLV p30 antibody [4B2]

Be the first to review this product! Submit a review

|

(12 Publications)

Anti-MLV p30 antibody [4B2] (ab130757) is a mouse monoclonal antibody detecting MLV p30 in Western Blot.

- Over 10 publications

View Alternative Names

Gag polyprotein, Pr65gag, Core polyprotein, gag

1 Images
Western blot - Anti-MLV p30 antibody [4B2] (AB130757)
  • WB

Unknown

Western blot - Anti-MLV p30 antibody [4B2] (AB130757)

All lanes:

Western blot - Anti-MLV p30 antibody [4B2] (ab130757) at 1/1500 dilution

All lanes:

MLV p30 recombinant protein expressed in E.coli

Predicted band size: 31.56 kDa

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

4B2

Isotype

IgG

Carrier free

No

Applications

WB

applications

Specificity

Species reactivity: Murine Leukemia Virus - MLV Gag, p30

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Recombinant full length protein - Moloney murine leukemia virus": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/1500", "WB-species-notes": "<p></p>" } } }

Product details

What is this antibody validated in?
Anti-MLV p30 antibody [4B2] (ab130757) is a mouse monoclonal antibody and is validated for use in Western Blot (WB). What is the molecular weight of MLV p30?
Anti-MLV p30 [4B2] (ab130757) specifically detects a band for MLV p30 (UniProt: P03332) at a molecular weight of 31.56kDa.

Trusted by the scientific community
Anti-MLV p30 [4B2] (ab130757) was first used in a scientific publication in 2012 and has been cited over 10 times in peer-reviewed journals.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 7.4 Preservative: 0.1% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MLV p30 also known as MLV IgG p30 or MLV full form protein serves as the matrix protein in the murine leukemia virus (MLV). It plays a mechanical role in viral assembly and budding processes. The p30 protein forms a shell beneath the viral envelope aiding in the anchoring of the envelope glycoproteins. With an approximate mass of 30 kDa this protein is predominantly expressed within MLV-infected cells. It facilitates the organization of viral components needed for particle formation.
Biological function summary

The production of MLV p30 orchestrates critical steps in the viral life cycle. The protein is a major part of the matrix structure essential for maintaining virus integrity. Besides giving structure p30 interacts with other proteins to help the virus replicate and spread. It is not part of a larger known multiprotein complex but its interactions support the efficiency of viral replication within the host cells.

Pathways

MLV p30 contributes specifically to the viral assembly pathway. It directly interacts with structural proteins such as Gag which is important for MLV particle maturation and release. The p30 protein also plays a role in the incorporation of the viral envelope proteins into budding virions which is part of the lifecycle pathway of MLV. These interactions ensure the proper formation and release of virus particles.

MLV p30 links strongly to the development of leukemia caused by murine leukemia virus. The protein's role in the stable assembly and release of virions aids in viral propagation within the host organism leading to oncogenesis. This makes p30 an important factor in the study of viral-induced cancers. MLV p30 indirectly associates with other oncogenic proteins through its involvement in viral replication which can influence leukemogenesis.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Gag polyprotein. Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.. Matrix protein p15. Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex.. RNA-binding phosphoprotein p12. Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes.. Capsid protein p30. Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.. Nucleocapsid protein p10-Gag. Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.
See full target information gag

Publications (12)

Recent publications for all applications. Explore the full list and refine your search

Nature 645:235-243 PubMed40634609

2025

Loss of FCoV-23 spike domain 0 enhances fusogenicity and entry kinetics.

Applications

Unspecified application

Species

Unspecified reactive species

M Alejandra Tortorici,Annette Choi,Cecily A Gibson,Jimin Lee,Jack T Brown,Cameron Stewart,Anshu Joshi,Sheri Harari,Isabelle Willoughby,Catherine Treichel,Elizabeth M Leaf,Jesse D Bloom,Neil P King,Christine Tait-Burkard,Gary R Whittaker,David Veesler

mBio 14:e0038723 PubMed37787515

2023

PSGL-1 is an evolutionarily conserved antiviral restriction factor.

Applications

Unspecified application

Species

Unspecified reactive species

Chao Jiang,Miao Mei,Ying Liu,Min Hou,Jun Jiao,Ya Tan,Xu Tan

Journal of virology 97:e0165022 PubMed36790205

2023

Cytoplasmic Tail Truncation Stabilizes S1-S2 Association and Enhances S Protein Incorporation into SARS-CoV-2 Pseudovirions.

Applications

Unspecified application

Species

Unspecified reactive species

Lizhou Zhang,Nancy Hom,Amrita Ojha,Klaus N Lovendahl,Huihui Mou,Kelly K Lee,Hyeryun Choe

mBio 13:e0137622 PubMed35913162

2022

Impact of SARS-CoV-2 Spike Mutations on Its Activation by TMPRSS2 and the Alternative TMPRSS13 Protease.

Applications

Unspecified application

Species

Unspecified reactive species

Annelies Stevaert,Ria Van Berwaer,Cato Mestdagh,Julie Vandeput,Els Vanstreels,Valerie Raeymaekers,Manon Laporte,Lieve Naesens

Cell 185:250-265.e16 PubMed35021064

2022

Engineered virus-like particles for efficient in vivo delivery of therapeutic proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Samagya Banskota,Aditya Raguram,Susie Suh,Samuel W Du,Jessie R Davis,Elliot H Choi,Xiao Wang,Sarah C Nielsen,Gregory A Newby,Peyton B Randolph,Mark J Osborn,Kiran Musunuru,Krzysztof Palczewski,David R Liu

Antimicrobial agents and chemotherapy : PubMed33468464

2021

Inhibition of Arenaviruses by Combinations of Orally Available Approved Drugs.

Applications

Unspecified application

Species

Unspecified reactive species

Shawn Herring,Jessica M Oda,Jessica Wagoner,Delaney Kirchmeier,Aidan O'Connor,Elizabeth A Nelson,Qinfeng Huang,Yuying Liang,Lisa Evans DeWald,Lisa M Johansen,Pamela J Glass,Gene G Olinger,Aleksandr Ianevski,Tero Aittokallio,Mary F Paine,Susan L Fink,Judith M White,Stephen J Polyak

ACS infectious diseases : PubMed33432808

2021

Proteolytic Activation of SARS-CoV-2 Spike at the S1/S2 Boundary: Potential Role of Proteases beyond Furin.

Applications

Unspecified application

Species

Unspecified reactive species

Tiffany Tang,Javier A Jaimes,Miya K Bidon,Marco R Straus,Susan Daniel,Gary R Whittaker

Nature communications 11:6013 PubMed33243994

2020

SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity.

Applications

Unspecified application

Species

Unspecified reactive species

Lizhou Zhang,Cody B Jackson,Huihui Mou,Amrita Ojha,Haiyong Peng,Brian D Quinlan,Erumbi S Rangarajan,Andi Pan,Abigail Vanderheiden,Mehul S Suthar,Wenhui Li,Tina Izard,Christoph Rader,Michael Farzan,Hyeryun Choe

bioRxiv : the preprint server for biology : PubMed32587973

2020

The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity.

Applications

Unspecified application

Species

Unspecified reactive species

Lizhou Zhang,Cody B Jackson,Huihui Mou,Amrita Ojha,Erumbi S Rangarajan,Tina Izard,Michael Farzan,Hyeryun Choe

Retrovirology 15:10 PubMed29357872

2018

Ribosome profiling of the retrovirus murine leukemia virus.

Applications

Unspecified application

Species

Unspecified reactive species

Nerea Irigoyen,Adam M Dinan,Ian Brierley,Andrew E Firth
View all publications

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com