Ubiquitin-like protein ISG15 Recombinant Protein | ISG15 recombinant protein

Recombinant Human Ubiquitin-like protein ISG15

Cat. Num. AAA968231

• Gene Names: Isg15; G1p2; IP17; Irfp; UCRP; IGI15
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ubiquitin-like protein ISG15; Recombinant Human Ubiquitin-like protein ISG15; Interferon-induced 15 kDa proteinInterferon-induced 17 kDa protein; IP17Ubiquitin cross-reactive protein; ISG15 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-157aa; Full Length
• Sequence: AWDLKVKMLGGNDFLVSVTNSMTVSELKKQIAQKIGVPAFQQRLAHQTAVLQDGLTLSSLGLGPSSTVMLVVQNCSEPLSILVRNERGHSNIYEVFLTQTVDTLKKKVSQREQVHEDQFWLSFEGRPMEDKELLGEYGLKPQCTVIKHLRLRGGGG
• Sequence Length: 161

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for ISG15 recombinant protein

Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Can also isgylate: DDX58/RIG-I which inhibits its function in antiviral signaling response and EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A and B virus, sindbis virus (SV) and herpes simplex type-1 (HHV-1). Plays a significant role in the control of neonatal Chikungunya virus (CHIKV) infection by acting as a putative immunomodulator of proinflammatory cytokines. Protects mice against the consequences of Chikungunya virus infection by downregulating the pathogenic cytokine response, often denoted as the cytokine storm. Plays a role in erythroid differentiation. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity

Product Categories/Family for ISG15 recombinant protein

Immunology

References

Nucleotide sequence and deduced amino acid sequence of a cDNA encoding an interferon-induced mouse 15-KDa protein.Fahey D. Sequence differences between murine ISG15, human ISG15 and ubiquitin a functional divergence from ubiquitin.Garlie N.K., Haas A.L., D'Cunha J., Schilling D., Knight E. Jr., Borden E.C. Serpin 2a is induced in activated macrophages and conjugates to a ubiquitin homolog.Hamerman J.A., Hayashi F., Schroeder L.A., Gygi S.P., Haas A.L., Hampson L., Coughlin P., Aebersold R., Aderem A.J. Immunol. 168:2415-2423(2002) Identification of a ubiquitin family protein as a novel neutrophil chemotactic factor.Owhashi M., Taoka Y., Ishii K., Nakazawa S., Uemura H., Kambara H.Biochem. Biophys. Res. Commun. 309:533-539(2003) High-throughput immunoblotting. Ubiquitin-like protein ISG15 modifies key regulators of signal transduction.Malakhov M.P., Kim K.I., Malakhova O.A., Jacobs B.S., Borden E.C., Zhang D.-E.J. Biol. Chem. 278:16608-16613(2003) Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo.Lenschow D.J., Giannakopoulos N.V., Gunn L.J., Johnston C., O'Guin A.K., Schmidt R.E., Levine B., Virgin H.W. IVJ. Virol. 79:13974-13983(2005) Negative regulation of ISG15 E3 ligase EFP through its autoISGylation.Zou W., Wang J., Zhang D.-E.Biochem. Biophys. Res. Commun. 354:321-327(2007) ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP.Okumura F., Zou W., Zhang D.E.Genes Dev. 21:255-260(2007) IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses.Lenschow D.J., Lai C., Frias-Staheli N., Giannakopoulos N.V., Lutz A., Wolff T., Osiak A., Levine B., Schmidt R.E., Garcia-Sastre A., Leib D.A., Pekosz A., Knobeloch K.P., Horak I., Virgin H.W. IVProc. Natl. Acad. Sci. U.S.A. 104:1371-1376(2007) Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization of ISG15 and contributes to effective ISGylation.Okumura F., Lenschow D.J., Zhang D.E.J. Biol. Chem. 283:24484-24488(2008) Negative feedback regulation of RIG-I-mediated antiviral signaling by interferon-induced ISG15 conjugation.Kim M.J., Hwang S.Y., Imaizumi T., Yoo J.Y.J. Virol. 82:1474-1483(2008) Emerging role of ISG15 in antiviral immunity.Skaug B., Chen Z.J.Cell 143:187-190(2010) ISG15 modulates development of the erythroid lineage.Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P., Tangy F., Zhang D.E., Ghysdael J., Quang C.T.PLoS ONE 6:E26068-E26068(2011) ISG15 is critical in the control of Chikungunya virus infection independent of UbE1L mediated conjugation.Werneke S.W., Schilte C., Rohatgi A., Monte K.J., Michault A., Arenzana-Seisdedos F., Vanlandingham D.L., Higgs S., Fontanet A., Albert M.L., Lenschow D.J.PLoS Pathog. 7:E1002322-E1002322(2011) Mycobacterial disease and impaired IFN-gamma immunity in humans with inherited ISG15 deficiency.Bogunovic D., Byun M., Durfee L.A., Abhyankar A., Sanal O., Mansouri D., Salem S., Radovanovic I., Grant A.V., Adimi P., Mansouri N., Okada S., Bryant V.L., Kong X.F., Kreins A., Velez M.M., Boisson B., Khalilzadeh S., Ozcelik U., Darazam I.A., Schoggins J.W., Rice C.M., Al-Muhsen S., Behr M., Vogt G., Puel A., Bustamante J., Gros P., Huibregtse J.M., Abel L., Boisson-Dupuis S., Casanova J.L.Science 337:1684-1688(2012)

NCBI and Uniprot Product Information

• NCBI GI #: 226874851
• NCBI GeneID: 100038882
• NCBI Accession #: NP_056598.2
• NCBI GenBank Nucleotide #: NM_015783.3
• UniProt Accession #: Q64339; Q8K0H3
• Molecular Weight: 21.3 kDa
• NCBI Official Full Name: ubiquitin-like protein ISG15
• NCBI Official Synonym Full Names: ISG15 ubiquitin-like modifier
• NCBI Official Symbol: Isg15
• NCBI Official Synonym Symbols: G1p2; IP17; Irfp; UCRP; IGI15
• NCBI Protein Information: ubiquitin-like protein ISG15
• UniProt Protein Name: Ubiquitin-like protein ISG15
• Protein Family: Ubiquitin-like protein
• UniProt Gene Name: Isg15
• UniProt Synonym Gene Names: G1p2; Ucrp; IP17
• UniProt Entry Name: ISG15_MOUSE

Uniprot Description

ISG15: Ubiquitin-like protein that is conjugated to intracellular target proteins after IFN-alpha or IFN-beta stimulation. Its enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the Ub conjugation pathway at the level of a specific E2 enzyme. Targets include STAT1, SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MxA, and RIG-1. Deconjugated by USP18/UBP43. Shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. May serve as a trans-acting binding factor directing the association of ligated target proteins to intermediate filaments. May also be involved in autocrine, paracrine and endocrine mechanisms, as in cell-to-cell signaling, possibly partly by inducing IFN-gamma secretion by monocytes and macrophages. Seems to display antiviral activity during viral infections. Interacts with, and is conjugated to its targets by the UBE1L (E1 enzyme) and UBE2E2 (E2 enzyme) (Probable). Interaction with influenza B NS1 protein inhibits this conjugation. By type I interferons. Detected in lymphoid cells, striated and smooth muscle, several epithelia and neurons.

Protein type: Ubiquitin-like modifier

Cellular Component: cytoplasm; extracellular region

Molecular Function: protein binding; protein tag

Biological Process: defense response to bacterium; defense response to virus; ISG15-protein conjugation; modification-dependent protein catabolic process; negative regulation of protein ubiquitination; negative regulation of viral genome replication; positive regulation of erythrocyte differentiation; regulation of interferon-gamma production