ISG15 Antibodies

Ubiquitin-like protein ISG15 (ISG15)

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 between E1, E2, and E3 enzymes that catalyze the conjugation of ISG15 to a lysine residue in the target protein.

Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Can also isgylate: EIF2AK2/PKR which contributes to its activation, DDX58/RIG-I which inhibits its function in antiviral signaling reaction, EIF4E2 which enhances its cap structure-binding activity and translation- inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB that prevents its ability to interact with the upstream activators of the JNK cascade therby inhibiting IFNA- induced JNK signaling.

Gene Information

Human
Gene Name:	ISG15
Uniprot:	P05161
Entrez:	9636

Family

Belongs to:
No superfamily

Alternative Names

G1P2; G1P2interferon-induced 17-kDa/15-kDa protein; IFI15; IFI15hUCRP; interferon, alpha-inducible protein (clone IFI-15K); Interferon-induced 15 kDa protein; Interferon-induced 17 kDa protein; interferon-stimulated protein, 15 kDa; IP17; ISG15 ubiquitin-like modifier; ISG15; Ubiquitin cross-reactive protein; ubiquitin-like protein ISG15; UCRP; UCRPIP17

Molecular Weight

Mass (kDA):
17.888 kDA

Genomic Context

Human
Location:	1p36.33
Sequence:	1; NC_000001.11 (1013497..1014540)

Tissue Specificity

Detected in lymphoid cells, striated and smooth muscle, several epithelia and neurons. Expressed in neutrophils, monocytes and lymphocytes. Enhanced expression seen in pancreatic adenocarcinoma, endometrial cancer, and bladder cancer, as compared to non-cancerous tissue. In bladder cancer, the increase in expression exhibits a striking positive correlation with more advanced stages of the disease.

Subcellular Localizations

Cytoplasm. Secreted. Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins.

Diseases

• Virus Diseases
• Malignant Neoplasms
• Neoplasms
• Innate Immune Response
• Hepatitis
• Hepatitis C
• Infective Disorder
• Influenza
• Hepatitis C, Chronic
• Endometrial Polyp
• Hepatitis, Chronic
• Carcinoma
• Fish Diseases

• Bacterial Infections
• Cell Transformation, Neoplastic
• Inflammation
• Mammary Neoplasms
• Malignant Neoplasm Of Breast
• Stomatitis
• Malignant Paraganglionic Neoplasm

Interacting Proteins

• FLNB
• PPM1B
• UBA7
• USP18

Pathways

• Conjugation
• Immune Response
• Innate Immune Response
• Pathogenesis
• Translation
• Secretion
• Cell Cycle
• Viral Replication
• Localization
• Inflammatory Response
• Cell Growth
• Cell Proliferation
• Hypersensitivity

• Rna Interference
• Response To Virus
• Regulation Of Gene Expression
• Reverse Transcription
• Autophagy
• Cell Adhesion
• Insemination

PTMs

• Isgylation
• Phosphorylation
• Ubiquitination
• Cleavage

• Methylation
• Sumoylation
• Nitrosylation
• Acetylation

• Dephosphorylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ISG15

Boster Bio - Best Uses Of The ISG15 Marker

The ISG15 biomarker could be used as therapeutic target molecule in breast cancers that are resistant to drugs. It is a dimer containing two ubiquitin-like domains. ELISA kits from Boster Biologicals are accessible through tebu-bio. For more information on ISG15, please read the following article. It will provide an explanation of its mechanism of action, its best uses and the best ways to utilize it in research.

ISG15 is an ubiquitin-like protein

Ubiquitin-like proteins are small molecule that bind to target proteins. These proteins are strongly regulated by IFNs. The functional C-terminal sequence of the ISG15 protein (a precursor of 165 amino acids) is revealed by processing. This ubiquitin-like protein has two domains with ubiquitin-like characteristics that share more than 32% of the sequence with ubiquitin. The C-terminal region is a canonical LRGG motif. This protein is connected to ubiquitin target proteins through isopeptide bonds.

Boster Bio researchers discovered that ISG15 is one of the subunits in the ubiquitinase protein that is akin to ubiquitin. The E1 enzyme is responsible in making the first ISG15 protein isopeptide bond. The E1 enzyme is responsible for catalyzing the activation of the carboxyl groups on ISG15, and is then transferred to the lysine groups of target proteins. This enzyme is crucial for conjugation reactions in vitro. The E1 enzyme is not yet approved for clinical diagnosis. The guarantee period for the primary antibody is one-year.

BECN1-silenced H4 cells were transfected wild-type or mutant BECN1 expression vectors, and stimulated with IFNA2 at 2 nM for 48 h. Cells were then harvested and western-blotted for EGFR/TUBA ratios. This study is the first to demonstrate that the ubiquitin-like protein ISG15 is capable rescuing EGFR degradation by modifying BECN1.

ISG15 cDNA was developed to determine whether ISG15 reduces HeLa cell proliferation. The cDNA encoding mature ISG15 was amplified using primers 5'-GACCGCGGTCTCGGGGGCGGTTGCGTGAAAAGGTGAAGATGC-3'. The recombinant ISG15 protein was purified using Strep-tactin columns and dialyzed against phosphate-buffered sodium.

It is a linear dimer

ISG15 was first identified as an UBL (unstructured branched loop kinase) in the late 2000s. In 2002 the first substrates for ISG15-conjugation was discovered. One of the substrates, Serpin2a is a host-induced bacteria protein that has a surprisingly large molecular mass. We identified Serpin2a as the PTM for mouse ISG15 activation by immunoprecipitationusing SDS-PAGE, immunoprecipitation and immuno. A high-throughput Western blot screen of samples from human thymus revealed four additional ISG15-conjugation targets.

Despite the low degree of conservation between mammals and chimpanzees We have found ISG15 in many species, including humans. While we aren't sure what chimpanzee, opossum or other teleost species are carrying ISG15 We have cloned the protein from several teleost species and it has low amino acid homology to mammals.

Type I interferon strongly regulates the expression of ISG15 and has been demonstrated that it has the ability to influence interferon signaling through the induction of the extracellular cytokine IFN g. It is an essential player in ISGylation that involves the covalent modification proteins by the ubiquitin-like proteins. Inhibition of ISGylation through USP18 or a similar ubiquitin-like carboxyterminal hydrolase was found to reverse ISGylation.

ISG15 is an important substrate for IFN-mediated signaling. The IFN receptor facilitates the interaction of ISG15 and ubiquitin. The activation of IFN-mediated signaling has been identified as one of the major sources of UbE1L. This interaction requires a high amount of MG132 to prevent degradation. Three substrates have been identified that hinder the expression of IFN by 293T cells transfected UbE1L.

It has two domains that resemble ubiquitins.

Two domains ubiquitin-like are found in the ISG15 protein. It is able to either bind to its target protein in a free state or conjugated. This process is referred to as ISGylation. In ISGylation, the ISG15 molecule binds itself to the lysine protein of the protein targeted for. ISG15 can also attach to CHMP5 or IFIH2/MDA5. These interactions enable ISG15 to increase oligomerization the target protein. Additionally, ISG15 plays a key part in the innate immune response that fights different pathogens, such as Ebola virus.

While the purpose of ISG15 is unclear but the protein modification does not appear to promote proteasome-mediated degradation. While ISG15-WBP2 conjugates tend to have one molecule in them, many substrates contained at least two ISG15 molecules. The ISG15 protein might play a significant role in stabilizing proteins susceptible to degradation by Ub.

ISG15 is crucial for immune regulation and also regulates viral replication and release. It has also been shown to regulate type I interferon signaling in humans. It is also believed to interact with other intracellular proteins that regulate other functions of the cell. These interactions and their molecular mechanism require more research. These findings may open new possibilities for treating diseases and infections.

ISG15 binds to lysine residues of newly synthesized proteins through the E1 activating enzyme. ATP is essential for this process and the E1 ligase is responsible for this process by forming a thioester bond with ISG15. Then, the E2 ligase transfer the conjugated ISG15 to its protein of choice. It is then removed from native conjugates by USP18 protease.

It may be a target for a molecule that can be used in the treatment of cancers of the breast that are resistant to drugs.

In addition to its potential use in the treatment of breast cancers resistant to drugs, Boster Bio may also be a suitable candidate for cancer immunotherapy. The drug could work by targeting the Rac1 signaling pathway which is involved in the proliferation of cancer cells cell cycle, apoptosis, invasion, migration, angiogenesis, and stemness. It also inhibits EGFR expression which is a protein found in more than 25% of breast carcinoma cells.

Although different studies have shown a similar result, the mechanisms that cause resistance to drugs vary. These results could be a reflection of the different cell models employed in the research. Further research is required to understand the underlying mechanisms. However, Boster Bio may be an effective therapeutic candidate for breast tumors resistant to chemotherapy. However, its success isn't an assurance of resistance to drugs. Further research is needed to determine the exact mechanisms.

Only a handful of studies have been conducted to evaluate the efficacy of chemotherapy for drug-resistant breast cancers. This promising potential has been enhanced by boster bio's availability both in China and the United States. Its pharmacological actions are well-known and must be evaluated in breast cancer patients. It is crucial as it could be a new treatment for breast cancers that are drug resistant.

Combining boster bio with anti-HER2 antibody trastuzumab may be an attractive combination for chemotherapy for breast cancer. It can be used in combination with trastuzumab and lapatinib. Combining these agents could provide a new perspective on combined treatment strategies. Innovative treatment strategies will be crucial to the success of these drugs. Further clinical research should examine new clinical trial techniques and research designs that explore the role of genes in breast cancer.

It is possible to detect it using PCR

The Boster Bio ISG15 marker is found in the genome of a variety of types of cells. The ISG15 gene is a key element of HBV's life cycle and may be involved in the production of antibodies that combat the virus. However, the exact mechanism behind ISGylation has not yet been fully elucidated. This article will explore the process of ISGylation as well as how it can assist in the detection of HBV.

The ISG15 gene has been shown to promote cancerous proliferation as well as migration and cell cycle. This protein, when it is expressed in cells, has been proven to boost the cell cycle and can be used as a predictor of future health. To identify the ISG15 gene we used a Boster Bio ISG15 marker to perform a PCR reaction. Our results come from three independent experiments conducted on three different dishes.

The ISG15 marker connects to the lysine lysine residues present in newly synthesized proteins. A series of conjugating enzymes are responsible for this process. The activating E1 enzyme forms a highly energetic thiolester intermediary and then transfers the ISG15 peptide to specific E3 ligases and intracellular substrates. The ISG15-peptide fusions are broken down by a USP18 protein, which is a protease.

This gene is vital in combating bacterial infections. To fight the bacteria, infected cells release Cytokines. These cytokines also play a role in fighting infections such as listeria. Human cells also have a defense program that triggers the production of hundreds of genes. Several of these genes are anti-bacterial or antiviral. The ISG15 protein is a biubiquitin, which means it is able to chemically join with other proteins. Although the ISG15 protein is known to aid cells in fighting infections that are bacterial and viral, it hasn't been confirmed as a valuable tool for treating human cancer.