Recombinant Mouse Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) Protein (His&Myc)

Name: Recombinant Mouse Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03806P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9EQH2
Target Symbol	ERAP1
Synonyms	Erap1; Appils; Arts1Endoplasmic reticulum aminopeptidase 1; EC 3.4.11.-; ARTS-1; Adipocyte-derived leucine aminopeptidase; A-LAP; Aminopeptidase PILS; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; VEGF-induced aminopeptidase
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	PCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL
Expression Range	731-930aa
Protein Length	Partial
Mol. Weight	28.3kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.
Subcellular Location	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Protein Families	Peptidase M1 family
Database References	KEGG: mmu:80898 STRING: 10090.ENSMUSP00000133166 UniGene: PMID: 29567213 we have shown that the loss of ERAAP leads to shifts in the nature and lengths of peptides presented by MHC I molecules on the cell surface PMID: 27371725 results suggest that several aminopeptidases play important roles in the maximum synthesis of NO in activated macrophages in a substrate peptide-dependent manner and ERAP1 is one of the aminopeptidases involved in the NO synthesis PMID: 25577645 This study clarifies ERAP1's role in shaping immunodominance through creation and destruction of peptides in vivo and demonstrates the functional significance of ERAP1 in modulating T-cell killing based upon this role. PMID: 25087231 These results suggest that secretion of ERAP1 is mediated by toll-like receptors via induction of intermediate cytokines PMID: 24688025 ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis. PMID: 24504800 Absence of Tpn or ERAAP independently altered the peptide repertoire by causing loss as well as gain of new pMHC I. ERAAP defined the characteristic amino termini of canonical MHC I peptides. PMID: 23863903 MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo. PMID: 22522492 endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma PMID: 21531727 ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice PMID: 21252114 The characteristic peptide length, as well as composition, of class I histocompatibility peptide cargo is determined not only by the class-I peptide-binding groove, but also by ERAAP proteolysis in the endoplasmic reticulum. PMID: 20173027 identification of ERAAP, the aminopeptidase associated with antigen processing in the endoplasmic reticulum (ERAAP) PMID: 12368856 Data show that loss of endoplasmic reticulum aminopeptidase 1 (ERAP1) in the antigen-processing pathway results in a marked shift in the hierarchy of immunodominance in viral infections. PMID: 16754858 Although PILSAP may not function in the initial generation of Flk-1 positive mesodermal precursors, it does play a role in growth of vascular, hematopoietic, and muscular lineage population from those precursors. PMID: 16824192 PILSAP affects RhoA activation and that influences the proper function of endothelial cells PMID: 17385722 ERAAP, in concert with major histocompatibility complex class I molecules, regulates the quality of processed peptides presented on the cell surface. PMID: 18941218

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Mouse Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) Protein (His&Myc)

Recombinant Mouse Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) Protein (His&Myc)

Product Overview

Target Details

FAQs