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AB8327

Anti-HIV protease 抗体 [1696]

Anti-HIV protease antibody [1696]

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(8 Publications)

Mouse Monoclonal POL antibody. Suitable for Dot and reacts with Synthetic peptide samples. Cited in 8 publications.

別名を表示する

HIV-1 protease, Human immunodeficiency virus protease, PR, Retropepsin

1 Images
Dot Blot - Anti-HIV protease antibody [1696] (AB8327)
  • Dot

Supplier Data

Dot Blot - Anti-HIV protease antibody [1696] (AB8327)

Dot blot analysis of ab8327. The total amount of ab8327 spotted on the nitrocellulose membrane are indicated in left column.

Lane 1 : ab8327; 0.2 μg/ml

Lane 2 : ab8327; 1.0 μg/ml

Lane 3 : ab8327; 2.0 μg/ml

Key facts

宿主種

Mouse

クローン性

Monoclonal

クローン番号

1696

アイソタイプ

IgG1

キャリアフリー

No

アプリケーション

Dot

applications

特異性

The antibody recognizes free N-terminus of mature HIV protease (HIV-1 and HIV-2). The antibody does not react with the precursor.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "Dot" : {"fullname" : "Dot Blot", "shortname":"Dot"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Synthetic peptide": { "Dot-species-checked": "testedAndGuaranteed", "Dot-species-dilution-info": "", "Dot-species-notes": "<p></p>" } } }
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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Protein A
バッファー組成
pH: 7.4 Preservative: 0.098% Sodium azide Constituents: PBS
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
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補足情報

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

HIV protease also known as aspartyl protease or protein catabolite is an enzyme vital for the maturation of the HIV virus. It is a homodimer each monomer having a mass of about 11 kilodaltons contributing to a total mass of roughly 22 kilodaltons. This enzyme is specifically expressed in HIV-infected cells where it plays a critical role in the life cycle of the virus. HIV protease cleaves newly synthesized polyproteins at specific sites to create the mature protein components of the infectious HIV particle.
Biological function summary

HIV protease is essential for the production of functional viral proteins facilitating viral particle assembly. It is not part of a larger complex but acts on its own to ensure correct protein maturation. Without the activity of this protease the virus cannot replicate efficiently as it fails to produce infectious viral particles. This makes HIV protease an ideal target for antiretroviral drugs which aim to inhibit its function and hinder the progression of the virus.

Pathways

The HIV protease plays a core role in the viral replication and maturation pathway essential for generating infectious virions. It interacts directly with the gag and gag-pol polyprotein precursors cleaving them into functional units necessary for structural components and replication machinery of the virus. Besides its action upon these precursor proteins integrates it tightly into the intricate machinery of HIV's lifecycle ensuring that all viral components become functionally active for subsequent infections.

HIV protease is intimately associated with the Human Immunodeficiency Virus (HIV) infection that leads to Acquired Immunodeficiency Syndrome (AIDS). This enzyme represents a critical target for antiretroviral therapy including protease inhibitors which aim to block its activity and viral replication. The enzyme's inhibition reduces viral load therefore managing the progression of the disease. Moreover resistance mutations in HIV protease can influence the effectiveness of protease inhibitors linking it to challenges in long-term HIV treatment strategies.
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製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:
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ターゲットの情報

See full target information HIV protease
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文献 (8)

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

PloS one 17:e0262477 PubMed35085286

2022

Amino acid substitutions at the HIV-1 transframe region significantly impair virus infectivity.

Applications

Unspecified application

Species

Unspecified reactive species

Fu-Hsien Yu,Kuo-Jung Huang,Chin-Tien Wang

Oncology letters 20:785-793 PubMed32566005

2020

Continuous progression of hemorrhage of sphenoid ridge meningioma causing cerebral hernia: A case report and literature review.

Applications

Unspecified application

Species

Unspecified reactive species

Song Han,Yakun Yang,Zuocheng Yang,Ning Liu,Xueling Qi,Changxiang Yan,Chunjiang Yu

Cell metabolism 29:1258-1273.e11 PubMed30930170

2019

Metabolic Reprogramming in Astrocytes Distinguishes Region-Specific Neuronal Susceptibility in Huntington Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Aris A Polyzos,Do Yup Lee,Rupsa Datta,Meghan Hauser,Helen Budworth,Amy Holt,Stephanie Mihalik,Pike Goldschmidt,Ken Frankel,Kelly Trego,Michael J Bennett,Jerry Vockley,Ke Xu,Enrico Gratton,Cynthia T McMurray

Frontiers in microbiology 6:1220 PubMed26583013

2015

A cell-free enzymatic activity assay for the evaluation of HIV-1 drug resistance to protease inhibitors.

Applications

WB

Species

Unspecified reactive species

Satoko Matsunaga,Takashi Masaoka,Tatsuya Sawasaki,Ryo Morishita,Yasumasa Iwatani,Masashi Tatsumi,Yaeta Endo,Naoki Yamamoto,Wataru Sugiura,Akihide Ryo

Emerging microbes & infections 2:e83 PubMed26038447

2013

Slow immunological progression in HIV-1 CRF07_BC-infected injecting drug users.

Applications

WB

Species

Unspecified reactive species

Pi-Han Lin,Chung-Chih Lai,Jia-Ling Yang,Hui-Lin Huang,Ming-Siang Huang,Mao-Song Tsai,Chia-Jui Yang,Chien-Ling Cheng,Yi-Ching Su,Shu-Fang Chang,Wen-Chun Liu,Chien-Ching Hung,Sui-Yuan Chang,Shan-Chwen Chang

Retrovirology 3:58 PubMed16956392

2006

HIV-2 Protease resistance defined in yeast cells.

Applications

WB

Species

Unspecified reactive species

Najoua Ben M'Barek,Gilles Audoly,Didier Raoult,Pablo Gluschankof

Molecular biology and evolution 23:764-72 PubMed16423863

2006

Diversification and specialization of HIV protease function during in vitro evolution.

Applications

WB

Species

Unspecified reactive species

Taryn L O'Loughlin,Dina N Greene,Ichiro Matsumura

Protein science : a publication of the Protein Society 8:2686-96 PubMed10631984

2000

Inhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibody.

Applications

Unspecified application

Species

Unspecified reactive species

J Lescar,J Brynda,P Rezacova,R Stouracova,M M Riottot,V Chitarra,M Fabry,M Horejsi,J Sedlacek,G A Bentley
View all publications
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