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| HTLV-1 p24 core recombinant protein |
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| Catalog Number: 10-663-45448 |
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| Related Product Names:
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gag-pro-pol protein; gag-pro-pol; HTLV-1 p24 core
- HTLV-1 p24 Core Recombinant; Pr160Gag-Pro-Pol |
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- Gene Information -
Information in yellow represents specific gene information and does not necessarily represent specific product details. For more information please contact sales@genwaybio.com.
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| Gene Name: gag-pro-pol |
Gene Name Synonym: N/A |
Gi #:
N/A |
NCBI Acc #:
N/A |
Swiss Prot Acc #:
P03362 |
Length (aa): N/A |
Mol. Weight (Da): 162512 |
Chrom Location: N/A |
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 Specificity: Immunoreactive with all sera of HTLV-1 infected individuals.
Purification Method: HTLV-1 p24 was purified by proprietary chromatographic technique.
Useful Applications: HTLV-1 p24 antigen can be used for ELISA and Western blots, excellent antigen for early detection of HIV seroconvertors with minimal specificity problems.
Source/Host: E. Coli
Purity/Purification: HTLV-1 p24 protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.
Format: 50mM Na-PO4 pH 6.0, containing 1mM DTT & 1mM EDTA.
Storage: HTLV-1 p24 protein is shipped at ambient temperature. Upon arrival, Store at -20 C.
Stability: Five years frozen. One month in solution at room temperature.
Shipping: Products may be shipped on ice pack or dry ice. |
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| GAG-PRO-POL PROTEIN TARGET DESCRIPTION: |
Synonym Names for gag-pro-pol protein: gag-pro-pol; HTLV-1 p24 Core Recombinant; Pr160Gag-Pro-Pol
The E.Coli derived recombinant protein contains the full-length sequence of HTLV-I p24, spanning all of p24.
Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).
Function: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity).
Function: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).
Function: Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome (By similarity).
Function: The aspartyl protease mediates proteolytic cleavages of Gag, Gag-Pro and Gag-Pro-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 (By similarity).
Function: Reverse transcriptase (RT) is a 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-Pro 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 perfom 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 perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end 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 PPT that has not been removed by RNase H as primer. PPT 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 (By similarity).
Function: Integrase 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, 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 dinucleotides OH's at the 3' ends. In the second step, the PIC access cell chromosomes during cell division. 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 (see above) are filled in and then ligated (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Catalytic Activity: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor: Binds 2 magnesium ions for reverse transcriptase polymerase activity (By similarity).
Cofactor: Binds 2 magnesium ions for ribonuclease H (RNase H) activity (By similarity).
Subunit: Interacts with human TSG101 and NEDD4. These interactions are essential for budding and release of viral particles (By similarity).
Subcellular Location: Matrix protein p19: Virion (Potential).
Subcellular Location: Capsid protein p24: Virion (Potential).
Subcellular Location: Nucleocapsid protein p15-pro: Virion (Potential).
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p19 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPPY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4 (By similarity).
Domain: The capsid protein N-terminus seems to be involved in Gag-Gag interactions (By similarity).
Ptm: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini.
Ptm: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding (By similarity).
Miscellaneous: The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs (By similarity).
Miscellaneous: HTLV-1 lineages are divided in four clades, A (Cosmopolitan), B (Central African group), C (Melanesian group) and D (New Central African group).
Similarity: Contains 2 CCHC-type zinc fingers.
Similarity: Contains 1 integrase catalytic domain.
Similarity: Contains 1 integrase-type DNA-binding domain.
Similarity: Contains 1 peptidase A2 domain [view classification].
Similarity: Contains 1 reverse transcriptase domain.
Similarity: Contains 1 RNase H domain.
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Order Confirmation: Sales order confirmations are sent out upon the receipt of all orders. Please contact GenWay if you do not receive a confirmation within 1 business day of submitting your order.
Precautions: gag-pro-pol protein is for in vitro research use only. Not for use in diagnostics or therapeutic procedures.
Important Notes: During shipment, small volumes of gag-pro-pol protein vial. For products with volumes of 200 µL or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap. Actual concentration, volume and quantity will be printed on the vial's label. Please refer to the vials label for this information.
Copyright: This GenWay TDS is copyrighted. This datasheet is produced based partially on data from Swiss-Prot/TrEMBL and NCBI. To better serve our clients with everything we know about gag-pro-pol protein, all related information, articles, resources about gag-pro-pol protein are being stored on our online database. Let us know if you have questions regarding this product.
Disclaimer: For documents and software available from this server, GenWay neither warrants nor assumes any legal liability or responsibility for the accuracy, completeness or utility of any information, product or process disclosed. |
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