ERAP2 Antibodies

Endoplasmic reticulum aminopeptidase 2 (ERAP2)

Aminopeptidase that plays a central role in peptide trimming, a measure required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them into the right length required for presentation on MHC class I molecules.

Preferentially hydrolyzes the basic residues Arg and Lys. .

Gene Information

Human
Gene Name:	ERAP2
Uniprot:	Q6P179
Entrez:	64167

Family

Belongs to:
peptidase M1 family

Alternative Names

Aminopeptidase LRAP; EC 3.4.11; EC 3.4.11.3; endoplasmic reticulum aminopeptidase 2; ERAP2; FLJ23633; FLJ23701; FLJ23807; Leukocyte-derived arginine aminopeptidase; LRAPL-RAPEC 3.4.11.-

Molecular Weight

Mass (kDA):
110.462 kDA

Genomic Context

Human
Location:	5q15
Sequence:	5; NC_000005.10 (96875939..96919716)

Tissue Specificity

Ubiquitously expressed. Highly expressed in spleen and leukocytes.

Subcellular Localizations

Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Diseases

• Autoimmunity
• Malignant Neoplasms
• Spondylitis
• Ankylosing Spondylitis
• Neoplasms
• Crohn Disease
• Autoimmune Reaction
• Sclerosis
• Melanoma
• Carcinoma
• Lymphoma
• Autoimmune Diseases
• Diabetes Mellitus

• Diabetes Mellitus, Insulin-dependent
• Inflammation
• Pre-eclampsia
• Infective Disorder
• Allelic Imbalance
• Multiple Sclerosis
• Virus Diseases

Pathways

• Immune Response
• Pathogenesis
• Adaptive Immune Response
• Transport
• Transmembrane Transport
• Developmental Process
• Fertilization
• Proteolysis
• Localization
• Antigen Processing And Presentation

• Cell Differentiation
• Angiogenesis
• Cell Recognition
• Rna Interference

PTMs

• Cleavage

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ERAP2

Steven Boster Bio and History - The Best Uses of the ERAP2 Marker

In this article we will examine Steven Boster's bio and history, and the best uses of the erap2 marker. We will also consider the anti-ERAP2 movement, which has gained a great deal of popularity in recent years. In addition, we'll explore why the erap2 marker is important, as well as some of the most controversial claims. We'll also discuss Steven Boster's work on eradicating cancer.

Steven Boster's history

If you're looking for the best place to look up Steve Boster's history, look no further. Listed below are public records for Steven Boster. These records include Steve Boster's current home address, previous residences, phone numbers, email addresses, and known relatives. You can even filter his information by age or state to see who he lived with most recently. You can even get an idea of his social life by looking up his public records.

Steve Boster was born on November 19, 1952 in Joliet, IL. He was a manager in the retail industry for years. He also served in the U.S. Army and was a member of Concordia Hall in Staunton, VA. He leaves behind his wife of nearly a decade, Natosha Peck, and two daughters, Crystal Boster and Natosha Peck. His family includes his brother Jack Boster and his sister Kimberly. There are several nieces and nephews who are also surviving Steve's death.

Best Uses Of The ERAP2 Marker

Among the most common cancer markers are the ERAP genes. They are involved in the renin-angiotensin system. In cancer patients, ERAP2 expression is associated with better prognosis. This suggests that the ERAP2 gene may be an immunotherapeutic target for SqCLC. In addition to these potential immunotherapeutic applications, ERAP2 genes are involved in maintaining the immune system.

TCGA data reveal that erap2 expression is highly enriched in a variety of pathways in various cancer types. The high levels of ERAP2 expression have been linked to the PI3K-Akt signaling pathway and the JAK-STAT/Toll-like receptor pathway. However, the role of this gene in cancer diagnosis remains uncertain. Further studies are needed to determine its role in cancer.

Anti-ERAP2 Marker

The Anti-ERAP2 Marker is a novel monoclonal antibody that recognizes human leukocyte antigen erap2. This molecule is selective for HLA-A29 peptides. Unlike HLA-A28, ERAP2 binds to the P1 residue of HLA-A29 peptides. ERAP2 enhances the abundance of the peptide-motif, as shown in Figure 1.

The Boster Bio Anti-ERAP2 antibody reacts with Human cytoplasmic antigens and can be stored at -20degC for up to a year or at 4degC for up to one month. This antibody is supplied in PBS containing 0.02% sodium azide. It was raised against a 17 amino acid peptide. The cost of the blocking peptide is variable, depending on the length of the immunogen. It has been validated using WB and IHC.

The global assessment of 9-11-mers confirms the effects of ERAP2 on P1. The effect of ERAP2 is consistent across HLA class I ligands and allotypes. P1 enrichment is observed for residues A, K, and R. The data are consistent with previous findings, which suggest that ERAP2 may exert selective pressure on the HLA-A29 repertoire.

The resulting clusters of RNAi containing RNAi-dependent peptides were examined by western blot. Peptides with low or non-existent RNA-binding activity were not detected, indicating that RNA-interference was the most likely cause of sensitivity. Further studies are necessary to confirm these findings. For example, the RNA-binding molecule ERAP2 interacts with many other RNA-interfering proteins.

The crystal structure of ERAP2 shows that P7 is accommodated in a hydrophobic pocket. In addition, the RNA-binding protein's hydrophobic pockets have a lower P2 content than those without it. This suggests that ERAP2 RNA-interactions occur with both RNA-binding and non-RNA-binding peptides.

The Anti-ERAP2 Marker in Boston Bio is a novel monoclonal antibody that recognizes RNA-binding RNA. The antibody is made of RNA molecules. The antigen itself is not specific to one species but is present in a wide range of species. The Anti-ERAP2 Marker is available in two formats, one containing eight million SNP markers, while the other contains RNA-binding proteins.

The RNA-binding property of the Anti-ERAP2 peptides is highly specific for HLA-A29. Recent advances in BCR pathophysiology have identified several interesting signaling pathways. Eventually, these peptides could serve as biomarkers for the diagnosis, response to therapy, and stratification of patients. Further research is needed to determine whether these molecules are biomarkers for BCR.