Recombinant Human Herpesvirus 1 Envelope Glycoprotein G (GG) Protein (His-SUMO)

Name: Recombinant Human Herpesvirus 1 Envelope Glycoprotein G (GG) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10232P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Herpesvirus 1 Envelope Glycoprotein G (GG) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P06484
Target Symbol	GG
Synonyms	gG; US4; Envelope glycoprotein G; gG; gG-1
Species	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	VPTNVSSTTQPQLQTTGRPSHEAPNMTQTGTTDSPTAISLTTPDHTPPMPSIGLEEEEEEEGAGDGEHLEGGDGTRDTLPQSPGPAFPLAEDVEKDKPNRPVVPSPDPNNSPARPETSRPKTPPTIIGPLATRPTTRLTSKGRPLVPTPQHTPLFSFLTASPALD
Expression Range	25-189aa
Protein Length	Partial
Mol. Weight	33.4 kDa
Research Area	Others
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	Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Subcellular Location	Virion membrane; Single-pass type I membrane protein.
Protein Families	Alphaherpesvirinae glycoprotein G family
Database References	KEGG: vg:2703404

Gene Functions References

HSV-1 Us3 is a multifunctional protein that plays various roles in the viral life cycle by phosphorylating a number of viral and cellular substrates. [review] PMID: 29896662
It regulates the pathogenicity of herpes simplex virus type-1 PMID: 28484184
This study identifies the alphaherpesvirus-specific Us3 kinase as an mTORC1 activator that subverts the host cell energy-sensing program to support viral productive growth irrespective of physiological stress. PMID: 28468873
findings show that Us8A is a virulence factor for HSV-1 infection in mice, and the function of Us8A for viral invasion into the central nervous system from peripheral sites is regulated by Us3-mediated phosphorylation of the protein at Ser-61. PMID: 27030266
The difference between HSV-1 and HSV-2 Us3 kinases appeared to be due to the fact that some Us3 phosphorylation sites in HSV-1 proteins are not conserved in the corresponding HSV-2 proteins. PMID: 26491159
Us3 enables the nucleus to cytoplasm capsid translocation. Nevertheless, Us3 is not essential for the production of infective progeny viruses. PMID: 25588052
HSV-1-encoded Us3 protein interrupted TCR signaling and interleukin-2 production by inactivation of the linker for activation of T cells. PMID: 25907557
Ablation of this phosphorylation abolished herpes simplex virus 1 US3-mediated downregulation of CD1d expression, suggesting that phosphorylation of KIF3A is the primary mechanism of viral suppression of CD1d expression. PMID: 25878107
This study demonstrated that herpes simplex virus 1 protein kinase US3 significantly inhibited NF-kappaB activation via hyperphosphorylation of p65 and decreased the expression of inflammatory chemokine interleukin-8 (IL-8). PMID: 24807716
Sufficient dUTPase activity was required for efficient herpes simplex virus 1 replication and Us3 phosphorylation of viral dUTPase Ser-187 upregulated dUTPase activity in host cells with low cellular dUTPase activity. PMID: 24760895
STING is stable in cancer-derived HEp-2 or HeLa cells infected with wild-type HSV-1 but is degraded in cells infected with mutants lacking the genes encoding functional infected cell protein 0 (ICP0), ICP4, or the US3 protein kinase PMID: 24449861
Herpes simplex virus 1 US3 hyperphosphorylates IRF3 and inhibits beta interferon production. PMID: 24049179
Human herpesvirus 1 US3 is necessary and sufficient for inhibiting TLR2 signaling at or before the stage of TRAF6 ubiquitination. PMID: 23478027
US3 plays a significant role in down-regulation of membrane biosynthesis. PMID: 22789738
These results suggested that Us3 phosphorylation of UL47 Ser-77 promoted the nuclear localization of UL47 in cell cultures and played a critical role in viral replication and pathogenesis in vivo. PMID: 21734045
identified gB and US3 as two viral factors that together downregulate CD1d surface expression; results suggest that HSV-1 uses gB and US3 to rapidly inhibit NKT cell function in the initial antiviral response PMID: 21653669
The authors demonstrated that Us3 phosphorylation of glycoprotein B Thr-887 upregulated the accumulation of endocytosed of glycoprotein B from the surfaces of infected cells. PMID: 21389132
Us3 is an Akt surrogate with overlapping substrate specificity to activate mTORC1, stimulating translation and virus replication PMID: 21123650
Us3 phosphorylation of gB Thr-887 played a critical role in viral replication in vivo and in HSV-1 pathogenesis PMID: 19846518
This prostein accumulates in cells infected with the mutant lacking the gene encoding ICP22 mediated the phosphorylation of histone deacetylase. PMID: 15956590
U(S)3 and U(S)3.5 protein kinases of herpes simplex virus 1 differ with respect to their functions in blocking apoptosis and in virion maturation and egress. PMID: 16571792
U(S)3 protein kinase blocks histone deacetylation by a mechanism distinct from that of ICP0. PMID: 16785443
It was concluded that US3 was mediating the suppression of mitochondrial respiration following HHV-1 infection. PMID: 16847111
Us3, Us5, and Us12 viral genes each have unique inhibitory effects on the different T lymphocyte cytotoxic effects PMID: 16987059
US3 blocks the proteolytic cleavage that generates active caspase 3 from the transfected zymogen procaspase 3, concomitant with inhibition of apoptosis. PMID: 17634220
These results supported the hypothesis that Us3 phosphorylates gB and downregulates the cell surface expression of gB in HSV-1-infected cells. PMID: 18945776
The majority of the US3-dependent phosphorylation of gB involved the CT domain and amino acid T887, a residue present in a motif similar to that recognized by US3 in other proteins. PMID: 19158241
US3-mediated phosphorylation of UL31 is critical to regulate nuclear egress. PMID: 19279109
regulation of Us3 activity by autophosphorylation appeared to play a critical role in viral replication in vivo and in HSV-1 pathogenesis PMID: 19297494
regulatory and functional effects differ from Us3 protein kinase in herpes simplex virus 2 PMID: 19740999

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.