Recombinant Moloney Murine Leukemia Virus Gag Polyprotein (GAG) Protein (GST)

Name: Recombinant Moloney Murine Leukemia Virus Gag Polyprotein (GAG) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02272P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Moloney murine leukemia virus (isolate Shinnick) (MoMLV) gag.

Collections: Featured viral antigens molecules, Hiv, Recombinant proteins, Viral antigen

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Product Overview

Description	Recombinant Moloney Murine Leukemia Virus Gag Polyprotein (GAG) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P03332
Target Symbol	GAG
Synonyms	gag; Gag polyprotein; Pr65gag; Core polyprotein) [Cleaved into: Matrix protein p15; MA); RNA-binding phosphoprotein p12; pp12); Capsid protein p30; CA); Nucleocapsid protein p10-Gag; NC-gag)]
Species	Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	PLRAGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWDYTTQAGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTLGDLVREAEKIFNKRETPEEREERIRRETEEKEERRRTEDEQKEKERDRRRHREMSKLL
Expression Range	216-478aa
Protein Length	Partial
Mol. Weight	57.6kDa
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.; Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex.; Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes.; Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.; Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.
Subcellular Location	[Gag polyprotein]: Virion. Host cell membrane; Lipid-anchor. Host late endosome membrane; Lipid-anchor. Host endosome, host multivesicular body.; [Matrix protein p15]: Virion.; [Capsid protein p30]: Virion.; [Nucleocapsid protein p10-Gag]: Virion.; [RNA-binding phosphoprotein p12]: Host cytoplasm.
Database References	KEGG: vg:1491870

Gene Functions References

The structure of the minimal sequence of the murine leukemia virus p12 protein necessary for the host chromatin binding was elucidated. PMID: 27707926
Phosphorylation requirement of murine leukemia virus p12 virus p12 protein necessary for the host chromatin binding was elucidated. PMID: 27707931
The N-terminal intracellular domain of the glycoGag is responsible for its effect on HIV-1 infectivity. PMID: 24403584
Authors found that mature Gag proteins MA and TM were bound to the immature core consisting of the Gag polyprotein (PrGag) and viral RNA (vRNA). PMID: 23643491
in presence of nucleocapsid (NC) chaperone, RNA dimerization occurred rapidly through a single structural intermediate; NC interacted primarily with guanosine residues; results show RNA chaperones can simplify RNA folding landscapes by weakening intramolecular interactions involving guanosine PMID: 23470731
selective packaging of dimeric RNA is explained by the nucleic acid binding domain derived from Gag binding within the virus to the sequence UCUG-UR-UCUG PMID: 20974908
results suggest a cooperative effect of p12 and capsid during the early events of MLV replication PMID: 15767417
interaction of Gag with Tsg101 and Alix favors budding from the plasma membrane and relieves a requirement for ubiquitination by Nedd4 PMID: 15908698
results indicate that glycosylated gag protein is important for M-MuLV replication in vivo and in vitro and that the protein may be involved in a late step in viral budding or release PMID: 17267509
Abl protein contribute to proper localization by playing a dominant role in trafficking of the v-Abl molecule PMID: 18367522
Basal budding and replication of the murine leukemia virus are independent of the gag L domains PMID: 18667521

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.