gag Antibody

Code: CSB-PA365907XA01RHO

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0.1ml

0.1ml1ml

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Species Reactivity: Rous sarcoma virus (strain Prague C) (RSV-PrC)

Raised in: Rabbit

Application: ELISA, WB (ensure identification of antigen)

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Target Background

Product Details

Uniprot NO.

P03322

Target Names

gag

Alternative Names

gagGag polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27 antibody; alternate cleaved 1; Capsid protein p27 antibody; alternate cleaved 2; Spacer peptide antibody; SP antibody; p3); Nucleocapsid protein p12; Protease p15 antibody; EC 3.4.23.-)] antibody

Raised in

Rabbit

Species Reactivity

Rous sarcoma virus (strain Prague C) (RSV-PrC)

Immunogen

Recombinant Rous sarcoma virus (strain Prague C) (RSV-PrC) gag protein

Conjugate

Non-conjugated

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Tested Applications

ELISA, WB (ensure identification of antigen)

Lead Time

Made-to-order (14-16 weeks)
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Value-added Deliverables

① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);

Quality Guarantee

① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;

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Target Background

Function(From Uniprot)

The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains).; Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro.; Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.; Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube 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.

Gene References into Functions

Taken together, the authors interpret these results to mean that Gag membrane interaction is cooperative in that it depends on the ability of Gag to multimerize. PMID:26676779
The resulting model of the RSV Gag lattice shows features and dynamics of the capsid protein with implications for the maturation process, and confirms the stabilizing role of the upstream and downstream regions of Gag, namely p10 and SP-NC. PMID:26118533
The structure of immature virus-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly. PMID:26223638
RSV Gag is highly flexible and can adopt a folded-over conformation on a lipid bilayer, implicating both the N and C termini in membrane binding. PMID:26246573
Taken together, these results provide strong evidence for the formation of a critical six-helix bundle in Gag assembly. PMID:24599998
These data suggest a possible connection between Gag nuclear trafficking and phosphoinositide-dependent plasma membrane targeting. PMID:23325682
Taken together, the authors interpret these results to mean that Rous sarcoma virus Gag membrane association is driven by electrostatic interactions and not by any specific association with phosphatidylinositol-(4,5)-bisphosphate. PMID:21813603
Directionality of nucleocytoplasmic transport of the retroviral gag protein depends on sequential binding of karyopherins and viral RNA. PMID:20435918
The authors conclude that the wild-type capsid protein sequence represents an evolutionary compromise between competing requirements for optimization of Gag assembly (of the immature virion) and capsid assembly (in the maturing virion). PMID:20427531
These data support a model in which the gag protein LYPSL motif of Rous sarcoma virus mediates budding through an interaction with the ESCRT adaptor protein Alix. PMID:20392845
ubiquitination of Gag is dependent upon Nedd4 binding to the L domain during RSV budding pathway PMID:15564502
the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors. PMID:16439536
These results indicate that the p10 NES domain of Gag is critical for virus replication and that it plays overlapping roles required for the nuclear shuttling of Gag and for the maintenance of proper virion core morphology. PMID:17634229
these experimental results strongly suggest that Rous sarcoma virus Gag proteins are capable of interacting within the nucleus. PMID:17977961
These findings provide important biological evidence in support of a significant conformational change involving the dimerization helix and the major homology region during capsid protein maturation. PMID:18433823
Taken together, these results define a short assembly domain between the folded portions of CA and NC, which is essential for formation of the immature Gag shell. PMID:18448521
cryo-electron microscopic analyses of two in-vitro-assembled capsids of Rous sarcoma virus PMID:19194444
Inserting a bipartite nuclear localization signal into Gag enhanced nuclear localization and restored RNA packaging in mutant viruses. PMID:19369339

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Subcellular Location

[Matrix protein p19]: Virion.; [Capsid protein p27, alternate cleaved 1]: Virion.; [Capsid protein p27, alternate cleaved 2]: Virion.; [Nucleocapsid protein p12]: Virion.; [Gag polyprotein]: Host nucleus, host nucleolus. Host nucleus, host nucleoplasm.

Database Links

KEGG: vg:1491923

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