Aminopeptidase PILS/ARTS1 Recombinant Protein Antigen

Novus Biologicals | Catalog # NBP2-59005PEP

Novus Biologicals
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Key Product Details

Source

E. coli

Tag

N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

Applications

Antibody Competition
View all Aminopeptidase PILS/ARTS1 Proteins and Enzymes »

Product Specifications

Description

A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to Aminopeptidase PILS/ARTS1.

Source: E. coli

Amino Acid Sequence: FQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLS

Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions.

Purity

>80% by SDS-PAGE and Coomassie blue staining

Predicted Molecular Mass

32 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Applications

Antibody Competition (10 - 100 molar excess)

Application Notes

This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-59005.

It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.

For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com

Protein / Peptide Type

Recombinant Protein Antigen

Formulation, Preparation, and Storage

NBP2-59005PEP
Formulation PBS and 1M Urea, pH 7.4.
Preservative No Preservative
Concentration Please see the vial label for concentration. If unlisted please contact technical services.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at -20C. Avoid freeze-thaw cycles.

Background: Aminopeptidase PILS/ARTS1

The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) is a 120 kDa protein localized to the lumen of the ER, which removes NH2-terminal residues from many antigenic precursors for MHC class I peptide presentation. Peptides that are presented by MHC class I on the surface of a cell must be 8-11 residues long, and ERAP1 specifically trims peptides of 9 amino acids or more. ERAP1 is also induced by interferon-gamma. The gene encoding human ERAP1 maps to chromosome 5q15. ERAP1 has previously been characterized as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1). A-LAP is thought to inactivate several bioactive peptides, including angiotensin II and, subsequently, may be involved in the regulation of blood pressure. PILS-AP is described as playing a role in angiogenesis by regulating the proliferation and migration of endothelial cells, and ARTS-1 is characterized as a TNFR1 binding protein that promotes TNFR1 shedding. Further research will be necessary to fully elucidate the functions of this protein.

Long Name

Aminopeptidase Puromycin-insensitive Leucyl-specific

Alternate Names

A-LAP, ARTS1, ERAAP1, ERAP1, PILS-AP

Gene Symbol

ERAP1

Additional Aminopeptidase PILS/ARTS1 Products

Product Documents for Aminopeptidase PILS/ARTS1 Recombinant Protein Antigen

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot or batch number in the search box below.

Product Specific Notices for Aminopeptidase PILS/ARTS1 Recombinant Protein Antigen

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

Related Research Areas

Metalloproteases and Regulators

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