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Brand: ProteoGenix

VSVG Protein- Drosophila VSVG NJ Recombinant Protein

Host species:
Insect
Origin species:
Drosophila
Uniprot ID:
P15425
Molecular weight:
59.11kDa

$250.00

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Full-length Yes
size
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VSVG Protein- Drosophila VSVG NJ Recombinant Protein

VSVG Protein- Drosophila VSVG NJ Recombinant Protein

Product name VSVG Protein- Drosophila VSVG NJ Recombinant Protein
Uniprot ID P15425
Uniprot link http://www.uniprot.org/uniprot/P15425
Origin species Drosophila
Expression system Eukaryotic expression
Sequence MLSYLILAIVVSPILGKIEIVFPQHTTGDWKRVPHEYNYCPTSADKNSHGTQTGIPVELTMPKGLTTHQVDGFMCHSALW MTTCDFRWYGPKYITHSIHNEEPTDYQCLEAIKAYKDGVSFNPGFPPQSCGYGTVTDAEAHIITVTPHSVKVDEYTGEWI DPHFIGGRCKGKICETVHNSTKWFTSSDGESVCSQLFTIVGGTFFSDSEEITSMGLPETGIRSNYFPYISTEGICKMPFC RKPGYKLKNDLWFQITDPDLDKKVRDLPHIKDCDLSSSIITPGEHATDISLISDVERILDYALCQSTWSKIEAGEPVTPV DLSYLGPKNPGVGPVFTIINGSLHYFTSKYLRVELESPVIPRMEGKVAGTRIVRQLWDQWFPFGEAEIGPNGVLKTKQGY KFPLHIIGTGEVDSDIKMERTVKHWEHPHIEAAQTYLKKDDTEEVIYYGDTGVSKNPVELVEGWFSGWRSSIMGVVAVIF GFVILILLIRLIGVLSSLFRPKKRPIYKSDVEMAHFRGGHNHRHKH
Molecular weight 59.11kDa
Protein delivered with Tag? Yes
Purity estimated 90%
Buffer PBS, pH 7.5
Form Frozen
Delivery condition Dry Ice
Delivery lead time in business days 10-25
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Insect
Fragment Type Full-length
Protein Accession NP_476656.1
Spec:Entrez GeneID 33271
Spec:NCBI Gene Aliases CG3966, NINAA, DmelCG3966, ninA, NinaA
Spec:SwissProtID P15425
NCBI Reference NP_476656.1
Aliases /Synonyms VSVG, neither inactivation nor afterpotential A, Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme, PPIase, Rotamase
Reference PX-P2099
Note For research use only
Molecular Constructor
Full-length Yes
Product name VSVG Protein- Drosophila VSVG NJ Recombinant Protein
Uniprot ID P15425
Uniprot link http://www.uniprot.org/uniprot/P15425
Origin species Drosophila
Expression system Eukaryotic expression
Sequence MLSYLILAIVVSPILGKIEIVFPQHTTGDWKRVPHEYNYCPTSADKNSHGTQTGIPVELTMPKGLTTHQVDGFMCHSALW MTTCDFRWYGPKYITHSIHNEEPTDYQCLEAIKAYKDGVSFNPGFPPQSCGYGTVTDAEAHIITVTPHSVKVDEYTGEWI DPHFIGGRCKGKICETVHNSTKWFTSSDGESVCSQLFTIVGGTFFSDSEEITSMGLPETGIRSNYFPYISTEGICKMPFC RKPGYKLKNDLWFQITDPDLDKKVRDLPHIKDCDLSSSIITPGEHATDISLISDVERILDYALCQSTWSKIEAGEPVTPV DLSYLGPKNPGVGPVFTIINGSLHYFTSKYLRVELESPVIPRMEGKVAGTRIVRQLWDQWFPFGEAEIGPNGVLKTKQGY KFPLHIIGTGEVDSDIKMERTVKHWEHPHIEAAQTYLKKDDTEEVIYYGDTGVSKNPVELVEGWFSGWRSSIMGVVAVIF GFVILILLIRLIGVLSSLFRPKKRPIYKSDVEMAHFRGGHNHRHKH
Molecular weight 59.11kDa
Protein delivered with Tag? Yes
Purity estimated 90%
Buffer PBS, pH 7.5
Form Frozen
Delivery condition Dry Ice
Delivery lead time in business days 10-25
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Insect
Fragment Type Full-length
Protein Accession NP_476656.1
Spec:Entrez GeneID 33271
Spec:NCBI Gene Aliases CG3966, NINAA, DmelCG3966, ninA, NinaA
Spec:SwissProtID P15425
NCBI Reference NP_476656.1
Aliases /Synonyms VSVG, neither inactivation nor afterpotential A, Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme, PPIase,Rotamase
Reference PX-P2099
Note For research use only
Molecular Constructor
Full-length Yes

General Information on VSVG NJ Protein:

Vesicular stomatitis virus (VSV) glycoproteins mediate both cell attachment and membrane fusion. Unlike many other low-pH-induced viral fusion proteins, their fusogenic conformational transitions is reversible. VSV-G has a three-stage fusion kinetics:
I. G-protein conformational change which is reversible and pH-dependent.
II. Reversible trimerization and clustering of the G-protein fusion loops.
III. Folding back of a cluster of extended trimers into their post-fusion conformations.
VSV NJ glycoprotein contains 517 amino acids and is glycosylated at position 178 and 335. Unlike VSV Indiana (VSIV), another major serotype of VSV, VSV NJ is not acylated. The two serotypes also differentiate in terms of antigenic structure. VSV NJ has a faster glycoprotein folding intracellularly and with less dependence on glycosylation.

  • Lenhard T, Reiländer H. Engineering the folding pathway of insect cells: generation of a stably transformed insect cell line showing improved folding of a recombinant membrane protein. Biochem Biophys Res Commun. 1997 Sep 29;238(3):823-30. PubMed PMID: 9325175.
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  • Bentrop J, Schwab K, Pak WL, Paulsen R. Site-directed mutagenesis of highly conserved amino acids in the first cytoplasmic loop of Drosophila Rh1 opsin blocks rhodopsin synthesis in the nascent state. EMBO J. 1997 Apr 1;16(7):1600-9. PubMed PMID: 9130705; PubMed Central PMCID: PMC1169764.
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  • Fouillet A, Levet C, Virgone A, Robin M, Dourlen P, Rieusset J, Belaidi E, Ovize M, Touret M, Nataf S, Mollereau B. ER stress inhibits neuronal death by promoting autophagy. Autophagy. 2012 Jun;8(6):915-26. doi: 10.4161/auto.19716. Epub 2012 Jun 1. PubMed PMID: 22660271; PubMed Central PMCID: PMC3427257.
  • Mitra A, Chinchore Y, Kinser R, Dolph PJ. Characterization of two dominant alleles of the major rhodopsin-encoding gene ninaE in Drosophila. Mol Vis. 2011;17:3224-33. Epub 2011 Dec 14. PubMed PMID: 22194648; PubMed Central PMCID: PMC3244490.
  • Ahmad ST, Natochin M, Barren B, Artemyev NO, O'Tousa JE. Heterologous expression of bovine rhodopsin in Drosophila photoreceptor cells. Invest Ophthalmol Vis Sci. 2006 Sep;47(9):3722-8. PubMed PMID: 16936079.
  • Ozaki K, Nagatani H, Ozaki M, Tokunaga F. Maturation of major Drosophila rhodopsin, ninaE, requires chromophore 3-hydroxyretinal. Neuron. 1993 Jun;10(6):1113-9. PubMed PMID: 8318232.

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