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AB63917

Anti-HIV1 p55 + p24 + p17 antibody

4

(2 Reviews)

|

(50 Publications)

Anti-HIV1 p55 + p24 + p17 antibody (ab63917) is a rabbit polyclonal antibody detecting HIV1 p55 + p24 + p17 in Western Blot, ELISA. Suitable for Human immunodeficiency virus.

- Over 30 publications
- Trusted since 2008

View Alternative Names

Gag polyprotein, Pr55Gag, gag

2 Images
Western blot - Anti-HIV1 p55 + p24 + p17 antibody (AB63917)
  • WB

AbReview16868****

Western blot - Anti-HIV1 p55 + p24 + p17 antibody (AB63917)

All lanes:

Western blot - Anti-HIV1 p55 + p24 + p17 antibody (ab63917) at 1/2000 dilution

Lane 1:

HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate transfected with a plasmid expressing HIV1 gag

Lane 2:

Untransfected HeLa whole cell lysate

Secondary

All lanes:

Goat anti-rabbit IgG (whole molecule) HRP polymer at 1/50000 dilution

false

This image is courtesy of an Abreview submitted by David Carpentier.

Western blot - Anti-HIV1 p55 + p24 + p17 antibody (AB63917)
  • WB

Unknown

Western blot - Anti-HIV1 p55 + p24 + p17 antibody (AB63917)

All lanes:

Western blot - Anti-HIV1 p55 + p24 + p17 antibody (ab63917) at 1/2000 dilution

Lane 1:

Extract of MT4 cells

Lane 2:

Extract of MT4 cells infected with HIV1 (LAI strain)

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human immunodeficiency virus

Applications

WB, ELISA

applications

Reactivity data

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Product details

What is this antibody validated in?
Anti-HIV1 p55 + p24 + p17 antibody (ab63917) is a rabbit polyclonal antibody and is validated for use in Western Blot (WB), ELISA in Human immunodeficiency virus samples.

Trusted by the scientific community
Anti-HIV1 p55 + p24 + p17 (ab63917) was first used in a scientific publication in 2008 and has been cited over 30 times in peer-reviewed journals.

Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
pH: 6 - 8.5 Preservative: 0.09% Sodium azide Constituents: Whole serum
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

'HIV1 p55' alternatively known as 'p55 HIV' 'p55 tax form' or 'p55.fun' is a precursor polyprotein composed of the matrix protein p17 the capsid protein p24 and other smaller proteins. This polyprotein with a molecular mass of approximately 55 kDa is expressed in HIV-infected cells. It is integral to the HIV virus structure providing the necessary framework for subsequent protein processing and assembly of viral particles. Researchers commonly use products like anti-HIV antibodies and techniques such as western blot for detection and study of this protein.
Biological function summary

HIV1 p55 serves as an essential component in the assembly and maturation of viral particles. It undergoes cleavage by the viral protease to form the individual proteins including p17 and p24 essential for the structural integrity of the HIV virus. These components play specific roles within the viral life cycle; p24 forms the viral core while p17 is involved in regulating viral RNA packaging. Together they contribute to the membrane budding process completing the virus assembly essential for its replication and infection.

Pathways

HIV1 p55 participates in critical viral infection pathways including the retroviral replication cycle. Protein processing and maturation by the viral protease involve interactions with other viral proteins like the reverse transcriptase and integrase facilitating the integration of viral DNA into the host genome. This process connects HIV1 p55 indirectly to host cellular pathways such as the MAPK signaling pathway influencing viral replication and pathogenesis within the host immune system.

HIV1 p55 is closely related to HIV/AIDS with its proteins playing central roles in disease progression. The HIV infection leading to acquired immunodeficiency syndrome (AIDS) involves the interplay of viral proteins including p17 and p24 with the host's immune response. Detection of p24 in diagnostic assays remains a standard indicator for assessing HIV infection levels in patients. As part of HIV pathogenesis these proteins heavily influence immune system evasion and persistence within the host presenting potential targets for antiretroviral therapy development.

Product protocols

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

Target data

Gag polyprotein. Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).. Matrix protein p17. Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).. Capsid protein p24. Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity).. Nucleocapsid protein p7. Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.. p6-gag. Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.
See full target information gag

Additional targets

gag,gag

Publications (50)

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

Science advances 11:eadz8980 PubMed40938996

2025

Elucidating the mechanism by which HIV-1 nucleocapsid mutations confer resistance to integrase strand transfer inhibitors.

Applications

Unspecified application

Species

Unspecified reactive species

Yuta Hikichi,Ryan C Burdick,Sean C Patro,Si-Yuan Ding,Brian T Luke,Erin D Clark,Sherimay D Ablan,Xiaolin Wu,Vinay K Pathak,Eric O Freed

Proceedings of the National Academy of Sciences of the United States of America 122:e2503988122 PubMed40838881

2025

Negative interplay between HIV-1 Gag and amyloid precursor protein centers around competition for VPS4A and TSG101.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Gu,Mojgan H Naghavi

Science advances 11:eadv4356 PubMed40344051

2025

Structural maturation of the matrix lattice is not required for HIV-1 particle infectivity.

Applications

Unspecified application

Species

Unspecified reactive species

Long Chen,Yuta Hikichi,Juan S Rey,Caner Akıl,Yanan Zhu,Hana Veler,Yao Shen,Juan R Perilla,Eric O Freed,Peijun Zhang

Journal of virology 98:e0135624 PubMed39475279

2024

IFI27 inhibits HIV-1 replication by degrading Gag protein through the ubiquitin-proteasome pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Wen-Qiang He,Wei Pang,Na Li,An-Qi Li,Yi-Hui Li,Ying Lu,Fan Shen,Rong Xin,Tian-Zhang Song,Ren-Rong Tian,Liu-Meng Yang,Yong-Tang Zheng

iScience 27:110405 PubMed39108735

2024

Immunogen characterization reveals an intrinsic hindrance in eliciting neutralizing antibodies against JN.1 variant.

Applications

Unspecified application

Species

Unspecified reactive species

Junhao Fan,Yao Zhang,Shixiong Li,Qingshan Li,Qiong Zi,Xiaoli Mou,Jihao Zheng,Xinyue Wang,Xinyu Guo,Jizheng Chen,Jingyou Yu

PLoS pathogens 20:e1011830 PubMed38512975

2024

Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.

Applications

Unspecified application

Species

Unspecified reactive species

Bailey Layish,Ram Goli,Haley Flick,Szu-Wei Huang,Robert Z Zhang,Mamuka Kvaratskhelia,Melissa Kane

iScience 27:108813 PubMed38318349

2024

Antiviral response and HIV-1 inhibition in sickle cell disease.

Applications

Unspecified application

Species

Unspecified reactive species

Namita Kumari,Asrar Ahmad,Clemilson Berto-Junior,Andrey Ivanov,Fayuan Wen,Xionghao Lin,Sharmin Diaz,Iheanyi Okpala,James G Taylor,Marina Jerebtsova,Sergei Nekhai

Viruses 15: PubMed38140642

2023

Early Emerging SARS-CoV-2 Spike Mutants Are Diversified in Virologic Properties but Elicit Compromised Antibody Responses.

Applications

Unspecified application

Species

Unspecified reactive species

Junhao Fan,Shixiong Li,Yao Zhang,Jihao Zheng,Dongfang Wang,Yunxi Liao,Zhibo Cui,Dongyu Zhao,Dan H Barouch,Jingyou Yu

EMBO molecular medicine 15:e17932 PubMed37970627

2023

Propylene glycol inactivates respiratory viruses and prevents airborne transmission.

Applications

Unspecified application

Species

Unspecified reactive species

Christine T Styles,Jie Zhou,Katie E Flight,Jonathan C Brown,Charlotte Lewis,Xinyu Wang,Michael Vanden Oever,Thomas P Peacock,Ziyin Wang,Rosie Millns,John S O'Neill,Alexander Borodavka,Joe Grove,Wendy S Barclay,John S Tregoning,Rachel S Edgar

Frontiers in immunology 14:1186478 PubMed37529048

2023

Combined intranasal and intramuscular parainfluenza 5-, simian adenovirus ChAdOx1- and poxvirus MVA-vectored vaccines induce synergistically HIV-1-specific T cells in the mucosa.

Applications

Unspecified application

Species

Unspecified reactive species

Ashley C Beavis,Edmund G-T Wee,Belkis M Akis Yildirim,Nicola Borthwick,Biao He,Tomáš Hanke
View all publications

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