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AB63911

Anti-HIV1 Reverse Transcriptase antibody

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(8 Publications)

Rabbit Polyclonal POL antibody. Suitable for ELISA, WB and reacts with Human immunodeficiency virus samples. Cited in 8 publications.

View Alternative Names

HIV 1 Reverse transcriptase, HIV1 RT, Human Immunodeficiency Virus 1, Reverse transcriptase p51 subunit, Reverse transcriptase p66 subunit, p51 RT, p66 RT

2 Images
Western blot - Anti-HIV1 Reverse Transcriptase antibody (AB63911)
  • WB

Unknown

Western blot - Anti-HIV1 Reverse Transcriptase antibody (AB63911)

All lanes:

Western blot - Anti-HIV1 Reverse Transcriptase antibody (ab63911) at 1/2500 dilution

Lane 1:

Extract of MT4 cells

Lane 2:

Extract of MT4 cells infected with HIV-1 (LAI strain)

Observed band size: 51 kDa,66 kDa

false

Western blot - Anti-HIV1 Reverse Transcriptase antibody (AB63911)
  • WB

Unknown

Western blot - Anti-HIV1 Reverse Transcriptase antibody (AB63911)

All lanes:

Western blot - Anti-HIV1 Reverse Transcriptase antibody (ab63911) at 1/2500 dilution

All lanes:

Western blot - Recombinant HIV1 Reverse Transcriptase protein (Active) (<a href='/en-us/products/proteins-peptides/recombinant-hiv1-reverse-transcriptase-protein-active-ab63979'>ab63979</a>) at 0.01 µg

Secondary

All lanes:

Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution

true

Exposure time: 90s

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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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 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.

HIV1 Reverse Transcriptase also known as HIV-1 RT or HIV RT is an essential enzyme in the lifecycle of the Human Immunodeficiency Virus type 1. This enzyme consists of two subunits p66 and p51 with a combined molecular mass of approximately 116 kDa. It expresses within the viral particles of HIV-1 where the enzyme catalyzes the conversion of viral RNA into DNA a process fundamental to viral replication. This ability to reverse transcribe RNA makes HIV1 Reverse Transcriptase a primary focus for antiretroviral therapy in the treatment of HIV infections as it is a unique feature absent in host cells.
Biological function summary

HIV1 Reverse Transcriptase acts as a central player in the viral replication process by establishing an integrated provirus from the viral RNA genome. The enzyme is not part of a larger complex but works closely with other HIV-1 proteins such as integrase to facilitate the integration of the newly synthesized viral DNA into the host genome. This integration is a critical step in the viral life cycle and ensures the persistence of the virus in infected cells which then leads to the continuous production of new viral particles.

Pathways

HIV1 Reverse Transcriptase functions in the retroviral replication pathway. The enzyme's activity links intimately with other viral enzymes like HIV-1 integrase which assist in embedding the newly formed DNA into the host cell's DNA. This process aligns with the broader reverse transcription pathway including interactions with host cellular machinery that contribute to subsequent viral transcription and replication phases. Understanding these interactions helps in designing effective therapeutic strategies that target various stages of the HIV replication cycle.

HIV1 Reverse Transcriptase directly relates to HIV and AIDS primarily due to its fundamental role in the HIV replication process. Therapies targeting this enzyme aim to hinder viral replication and decrease viral load in infected individuals. Furthermore resistance mutations in HIV1 Reverse Transcriptase can lead to challenges in treatment requiring the development of new inhibitors. The enzyme's interaction with other HIV-1 proteins such as protease also highlights its significance in resistance mechanisms and therapeutic targeting in the fight against HIV/AIDS.

Product protocols

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

Publications (8)

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

Journal of virology 98:e0053424 PubMed38899932

2024

The interferon-regulated host factor hnRNPA0 modulates HIV-1 production by interference with LTR activity, mRNA trafficking, and programmed ribosomal frameshifting.

Applications

Unspecified application

Species

Unspecified reactive species

Fabian Roesmann,Helene Sertznig,Katleen Klaassen,Alexander Wilhelm,Delia Heininger,Stefanie Heß,Carina Elsner,Rolf Marschalek,Mario L Santiago,Stefan Esser,Kathrin Sutter,Ulf Dittmer,Marek Widera

Journal of virology 96:e0134921 PubMed34643428

2021

Perturbing HIV-1 Ribosomal Frameshifting Frequency Reveals a Preference for Gag-Pol Incorporation into Assembling Virions.

Applications

Unspecified application

Species

Unspecified reactive species

Bayleigh E Benner,James W Bruce,Jacob R Kentala,Magdalena Murray,Jordan T Becker,Pablo Garcia-Miranda,Paul Ahlquist,Samuel E Butcher,Nathan M Sherer

Journal of virology 95:e0132321 PubMed34523971

2021

Natural Occurring Polymorphisms in HIV-1 Integrase and RNase H Regulate Viral Release and Autoprocessing.

Applications

Unspecified application

Species

Unspecified reactive species

Tomozumi Imamichi,John G Bernbaum,Sylvain Laverdure,Jun Yang,Qian Chen,Helene Highbarger,Ming Hao,Hongyan Sui,Robin Dewar,Weizhong Chang,H Clifford Lane

Structure (London, England : 1993) 27:1581-1593.e3 PubMed31471129

2019

Conformational Changes in HIV-1 Reverse Transcriptase that Facilitate Its Maturation.

Applications

Unspecified application

Species

Unspecified reactive species

Ryan L Slack,Tatiana V Ilina,Zhaoyong Xi,Nicholas S Giacobbi,Gota Kawai,Michael A Parniak,Stefan G Sarafianos,Nicolas Sluis Cremer,Rieko Ishima

Journal of virology 91: PubMed27795445

2016

Critical Contribution of Tyr15 in the HIV-1 Integrase (IN) in Facilitating IN Assembly and Nonenzymatic Function through the IN Precursor Form with Reverse Transcriptase.

Applications

Unspecified application

Species

Unspecified reactive species

Tatsuro Takahata,Eri Takeda,Minoru Tobiume,Kenzo Tokunaga,Masaru Yokoyama,Yu-Lun Huang,Atsuhiko Hasegawa,Tatsuo Shioda,Hironori Sato,Mari Kannagi,Takao Masuda

Journal of virology 90:6906-6917 PubMed27194769

2016

Stability of HIV Frameshift Site RNA Correlates with Frameshift Efficiency and Decreased Virus Infectivity.

Applications

Unspecified application

Species

Unspecified reactive species

Pablo Garcia-Miranda,Jordan T Becker,Bayleigh E Benner,Alexander Blume,Nathan M Sherer,Samuel E Butcher

Cell host & microbe 15:717-728 PubMed24922574

2014

A cell-intrinsic inhibitor of HIV-1 reverse transcription in CD4(+) T cells from elite controllers.

Applications

Unspecified application

Species

Unspecified reactive species

Jin Leng,Hsin-Pin Ho,Maria J Buzon,Florencia Pereyra,Bruce D Walker,Xu G Yu,Emmanuel J Chang,Mathias Lichterfeld

Retrovirology 9:37 PubMed22554282

2012

Protein kinase C-delta regulates HIV-1 replication at an early post-entry step in macrophages.

Applications

WB

Species

Unspecified reactive species

Xavier Contreras,Olfa Mzoughi,Fabrice Gaston,Matija B Peterlin,Elmostafa Bahraoui
View all publications

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