Recombinant Mouse Endoplasmic reticulum aminopeptidase 1 (Erap1),Partial

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Code CSB-EP007760MO
MSDS
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Erap1
Uniprot No.
Research Area
Immunology
Alternative Names
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)
Source
E.coli
Expression Region
731-930aa
Target Protein Sequence
PCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
28.3kDa
Protein Length
Partial
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The gene encoding the Mouse Erap1 protein (731-930aa) creates recombinant plasmid, which is then transformed into e.coli cells. e.coli cells that can endure a specific antibiotic are selected and cultured under conditions that encourage the expression of the gene of interest. The protein features a N-terminal 10xHis tag and C-terminal Myc tag fusion. Following expression, affinity purification is employed to isolate and purify the recombinant Mouse Erap1 protein from the cell lysate. Denaturing SDS-PAGE is applied to resolve the resulting recombinant Mouse Erap1 protein, indicating a purity level exceeding 90%.

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Target Background

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.
Gene References into Functions
  1. data provide the first evidence that ERAP1 associated with exosomes plays important roles in inflammatory processes via activation of macrophages. PMID: 29567213
  2. 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
  3. 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
  4. 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
  5. These results suggest that secretion of ERAP1 is mediated by toll-like receptors via induction of intermediate cytokines PMID: 24688025
  6. ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis. PMID: 24504800
  7. 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
  8. MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo. PMID: 22522492
  9. endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma PMID: 21531727
  10. ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice PMID: 21252114
  11. 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
  12. identification of ERAAP, the aminopeptidase associated with antigen processing in the endoplasmic reticulum (ERAAP) PMID: 12368856
  13. 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
  14. 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
  15. PILSAP affects RhoA activation and that influences the proper function of endothelial cells PMID: 17385722
  16. ERAAP, in concert with major histocompatibility complex class I molecules, regulates the quality of processed peptides presented on the cell surface. PMID: 18941218

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Subcellular Location
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Protein Families
Peptidase M1 family
Database Links
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