gag-pol Antibody, HRP conjugated

^{Rare Species}

說明書

中文名稱：

gag-pol兔多克隆抗體, HRP偶聯(lián)
貨號：

CSB-PA15387B0Rb
規(guī)格：

￥880
其他：

產(chǎn)品詳情
產(chǎn)品評價
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

產(chǎn)品名稱：

Rabbit anti-Human immunodeficiency virus type 1 group M subtype B gag-pol Polyclonal antibody
Uniprot No.：

P04585
基因名：

gag-pol
別名：

gag-pol antibody; Gag-Pol polyprotein antibody; Pr160Gag-Pol) [Cleaved into: Matrix protein p17 antibody; MA); Capsid protein p24 antibody; CA); Spacer peptide 1 antibody; SP1 antibody; p2); Nucleocapsid protein p7 antibody; NC); Transframe peptide antibody; TF); p6-pol antibody; p6*); Protease antibody; EC 3.4.23.16 antibody; PR antibody; Retropepsin); Reverse transcriptase/ribonuclease H antibody; EC 2.7.7.49 antibody; EC 2.7.7.7 antibody; EC 3.1.26.13 antibody; Exoribonuclease H antibody; EC 3.1.13.2 antibody; p66 RT); p51 RT; p15; Integrase antibody; IN antibody; EC 2.7.7.- antibody; EC 3.1.-.-)] antibody
宿主：

Rabbit
反應(yīng)種屬：

Human immunodeficiency virus type 1 group M subtype B
免疫原：

Recombinant Human immunodeficiency virus type 1 group M subtype B Gag-Pol polyprotein protein (1-440AA)
免疫原種屬：

Human immunodeficiency virus type 1 group M subtype B
標(biāo)記方式：

HRP
克隆類型：

Polyclonal
抗體亞型：

IgG
純化方式：

>95%, Protein G purified
濃度：

It differs from different batches. Please contact us to confirm it.
保存緩沖液：

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
產(chǎn)品提供形式：

Liquid
應(yīng)用范圍：

ELISA
Protocols：

ELISA Protocol
儲存條件：

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期：

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
用途：

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產(chǎn)品評價

靶點(diǎn)詳情

功能：

Mediates, with Gag 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). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.; Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA.; 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. Host restriction factors such as monkey 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. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.; 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.; Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding.; Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.; Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
基因功能參考文獻(xiàn)：
1. cryoelectron microscopy of HIV-1 reverse transcriptase initiation complex PMID: 29695867
2. Data show that the sequences preferred by HIV-1 RNase H are distributed in the HIV genome in a way suggesting selection for efficient RNA cleavage during replication. PMID: 29126318
3. we studied for the first time the genetic diversity of HIV-1 BF recombinants and their evolution over time through in-depth phylogenetic analysis and multiple recombination detection methods involving 337 HIV-1 nucleotide sequences (25 near full-length (NFL) and 312 partial pol gene) obtained from Argentinean MSM PMID: 29244833
4. These data imply that p53 can excise incorrect sugar in addition to base mispairs, thereby expanding the role of p53 in the repair of nucleic acids replication errors by HIV-1 reverse transcriptase. PMID: 28081035
5. Drug resistance-related mutations T369V/I in the connection subdomain of HIV-1 reverse transcriptase severely impair viral fitness. PMID: 28279801
6. Data suggest that the beta1'-beta2' motif of the RNase H domain may be responsible for displacing the connection domain from the polymerase cleft of putative monomeric p66; the unstable elongated p66 molecule may then readily dimerize with p51 to assume a stable dimeric conformation. PMID: 28627879
7. Allosteric HIV-1 integrase inhibitors promote aberrant protein multimerization by directly mediating inter-subunit interactions PMID: 27503276
8. Use of Capillary Electrophoresis to Study the Binding Interaction of Aptamers with Wild-Type, K103N, and Double Mutant (K103N/Y181C) HIV-1 RT : Studying the Binding Interaction of Wild-Type, K103N, and Double Mutant (K103N/Y181C) HIV-1 RT with Aptamers by Performing the Capillary Electrophoresis PMID: 27900665
9. HIV-1 Reverse Transcriptase Polymerase and RNase H (Ribonuclease H) Active Sites Work Simultaneously and Independently. PMID: 27777303
10. Rate-limiting Pyrophosphate Release by HIV Reverse Transcriptase Improves Fidelity PMID: 27777304
11. Data indicate that inhibition of HIV-2 reverse transcriptases (RTs) by the nucleoside (NRTIs) tested showed a very similar trend in comparison to that of HIV-1 RT with lower Mg2+ concentrations. PMID: 27936595
12. It has been found that the functional assembly of integrase through its fusion form with reverse transcriptase is critical for integrase to exert its nonenzymatic function. PMID: 27795445
13. The amino acids at positions 76-100 of gp41 are required for it to bind to integrase. PMID: 27681265
14. These results reveal an unexpected biological role ofHIV-1 Integrase binding to the viral RNA genome during virion morphogenesis and elucidate the mode of action of allosteric integrase inhibitors . PMID: 27565348
15. Results from next generation sequencing identified minority resistance mutations in the HIV-1 integrase coding region. PMID: 26587787
16. NMR characterization of HIV-1 reverse transcriptase binding to various non-nucleoside reverse transcriptase inhibitors with different activities. PMID: 26510386
17. Analysis of the zidovudine resistance mutations T215Y, M41L, and L210W in HIV-1 reverse transcriptase has been presented. PMID: 26324274
18. The protease-reverse transcriptase (Pro-RT) region was sequenced and analyzed for the identification of antiretroviral resistance-associated mutations (RAMs)in 40 samples. 39 samples possessed multiple RAMs in the reverse transcriptase genes. PMID: 26122980
19. These results suggest that the Gag-Pol assembly and budding defects are largely due to a lack of p6gag, but also in part due to size limitation. PMID: 26489905
20. RIPK1 and RIPK2 are targets of HIV-1 Protease activity during infection, and their inactivation may contribute to modulation of cell death and host defense pathways by HIV-1 PMID: 26297639
21. Role of HIV-1 matrix protein p17 variants in lymphoma pathogenesis. PMID: 26578780
22. these results show that the addition of R263K to the T66I substitution diminishes viral replicative capacity and strand transfer activity while not compromising susceptibility to dolutegravir. This supports the use of dolutegravir in second-line therapy for patients failing elvitegravir therapy who harbor the T66I resistance substitution. PMID: 26311878
23. Together, these results provide evidence for an Integrase/Pol mediated uptake of LEDGF/p75 in HIV-1 viral particles and a specific cleavage by HIV protease. PMID: 25809198
24. Study emphasizes the importance of the hydrophobic nature and SH3 fold of C-terminal domain in proper functioning of HIV integrase PMID: 25586721
25. Report interaction between HIV-1 reverse transcriptase amino acid, Lys101, and a non nucleoside RT inhibitor, GW420867X. PMID: 24965933
26. Design new inhibitors which could be effectively bypass the drug resistance of HIV-1 RT mutants. PMID: 25234608
27. Report series of calix[4]arene-based beta-diketo derivatives that may circumvent resistance to clinical HIV-1 IN inhibitors. PMID: 25682937
28. Novel 2H-pyran-2-one derivatives did not function as HIV-1 reverse transcriptase inhibitors. PMID: 25523431
29. Crystal structure of MDR769 I10V HIV-1 protease co-crystallized with TLF-PafF. PMID: 25108107
30. Dolutegravir resistance mutation R263K cannot coexist in combination with many classical integrase inhibitor resistance substitutions. PMID: 25653436
31. Overall, this study demonstrates the novel interaction between HIV-1 integrase and cellular DYNLL1 proteins and suggests the requirement of this virus-cell interaction for proper uncoating and efficient reverse transcription of HIV-1. PMID: 25568209
32. These results also indicate the importance of the RNase H N-terminal residue in the dimerization of reverse transcriptase subunits. PMID: 25392207
33. REVIEW: published computer-aided structural predictions of HIV-1 integrase in complex with its interactors PMID: 24001231
34. Data show that the same site on integrase-binding domain (IBD) of lens epithelium-derived growth factor (LEDGF) is involved in binding to MLL protein and HIV-IN (integrase), indicating an approach to target LEDGF in both leukemia and HIV infection. PMID: 25305204
35. Aggregation assays with truncated IN variants revealed that a construct with catalytic and C-terminal domains of IN only formed an open polymer associated with efficient drug-induced aggregation. PMID: 24904063
36. C-terminal residues Lys-264 and Lys-266 play an important role in the inhibitor induced aberrant multimerization of HIV-1 integrase. PMID: 25118283
37. Data suggest that the HIV-1 integrase (IN)/transportin-SR2 (TRN-SR2) interaction interface is a potential target for antiviral therapy. PMID: 25063804
38. The co-evolution of capsid protein and integrase sequences is related to steps of nuclear viral entry. PMID: 24474329
39. This study brings the cellular and test tube results in closer agreement by showing that HIV-1 reverse transcriptase is not more error prone than other reverse transcriptases and, when assayed under physiological magnesium conditions. PMID: 24850729
40. In a double drug-resistant G140S/Q148H HIV-integrase mutant, anti-HIV raltegravir spontaneously dissociates from the active site of the protein. PMID: 24205814
41. The Gag-Pol ribosomal frameshift signal plays an important role in HIV-1 RNA packaging. PMID: 24453371
42. Single-nucleotide polymorphisms in the 3' region of the pol gene modulate viral replication ability. PMID: 24478432
43. This study supports the relevance of a rare mutation at reverse transcriptase Lys65 (K65E) in nucleos(t)ide reverse transcriptase inhibitors resistance, particularly to tenofovir. PMID: 23749955
44. The presence of the N348I or M184V/N348I mutation in reverse transcriptase decreased the replication capacity of E138K virus. PMID: 24227862
45. Multiple genetic pathways involving tyrosine 143 of HIV-1 integrase are preferentially associated with specific secondary amino acid substitutions and confer resistance to raltegravir and cross-resistance to elvitegravir. PMID: 23733474
46. Increased risk of Q151M and K65R mutations in patients failing stavudine-containing first-line antiretroviral therapy in Cambodia. PMID: 24015311
47. Data indicate that thienopyrimidinones inhibite both wild type HIV-1 reverse transcriptase (HIV RT) and drug-resistant variants, and destabilize RNase H, in some instances reducing the Tm by 5 degrees C. PMID: 23631411
48. Data indicate that the stabilized peptides inhibit the interaction of HIV-1 integrase (IN) with the cellular cofactor LEDGF/p75. PMID: 23758584
49. Data indicate theat the structure provides direct determination of hydrogen atom positions in the HIV-1 protease active site. PMID: 23772563
50. Data suggest that the triad of Arg358, Gly359, and Ala360 in the major groove DNA/RNA-binding track of HIV-1 reverse transcriptase has major impacts on binding affinity, enzyme stability, and catalytic efficiency at high temperature. PMID: 24303887
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亞細(xì)胞定位：

[Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body.; [Matrix protein p17]: Virion membrane; Lipid-anchor. Host nucleus. Host cytoplasm.; [Capsid protein p24]: Virion.; [Nucleocapsid protein p7]: Virion.; [Reverse transcriptase/ribonuclease H]: Virion.; [Integrase]: Virion. Host nucleus. Host cytoplasm.
數(shù)據(jù)庫鏈接：

KEGG: vg:155348

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