Recombinant Pseudomonas entomophila UPF0114 protein PSEEN0819 (PSEEN0819)

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Description

Introduction to Recombinant Pseudomonas entomophila UPF0114 protein PSEEN0819 (PSEEN0819)

Recombinant Pseudomonas entomophila UPF0114 protein PSEEN0819 (PSEEN0819) is a protein derived from the bacterium Pseudomonas entomophila. Proteins are fundamental components of biological systems, crucial in various biological processes . The primary structure of a protein refers to its amino acid sequence, which dictates its shape and function1.

Primary, Secondary, Tertiary, and Quaternary Structures of Proteins

Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary .

Pseudomonas entomophila and the PSEEN0819 Protein

Pseudomonas entomophila is a bacterium known for its insecticidal properties . Proteins such as PSEEN0819, derived from P. entomophila, may play a role in its interaction with insects.

Recombinant Production of PSEEN0819

Recombinant proteins are produced using genetic engineering techniques, where the gene encoding the protein of interest is inserted into a host organism (e.g., E. coli) that then produces the protein . Recombinant PSEEN0819 protein is often used in research and development.

Applications of Recombinant PSEEN0819

Recombinant PSEEN0819 has uses in:

  • ELISA Assays: It can be employed as an antigen in Enzyme-Linked Immunosorbent Assays (ELISA) . ELISA is a biochemical technique used to detect the presence of an antibody or an antigen in a sample.

Presenilins and γ-Secretase

Presenilins are key components of the γ-secretase complex, an intramembrane protease crucial in various cellular processes .

  • Structure of Presenilins: Presenilins, such as PSEN1 and PSEN2, are integral membrane proteins with multiple transmembrane domains .

  • Function in γ-Secretase Activity: Presenilins are catalytic subunits of γ-secretase, which cleaves other proteins within their transmembrane domains . Mutations in presenilin genes can affect γ-secretase activity and are implicated in diseases such as Alzheimer's .

The Dystrophin Complex

The dystrophin complex is vital in stabilizing the plasma membrane of muscle cells . Dystrophin, a key component, has four main functional domains:

  • An actin-binding amino-terminal domain

  • A central rod domain

  • A cysteine-rich domain

  • A carboxyl-terminus

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your format preference in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchase method and location. Please consult your local distributor for precise delivery estimates.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires advance notice and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to collect the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50%, which can serve as a guideline.
Shelf Life
Shelf life depends on several factors including storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized formulations have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquot to prevent repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.
The tag type is determined during production. If you require a specific tag, please inform us; we will prioritize its development.
Synonyms
PSEEN0819; UPF0114 protein PSEEN0819
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-162
Protein Length
full length protein
Species
Pseudomonas entomophila (strain L48)
Target Names
PSEEN0819
Target Protein Sequence
MERILENAMYASRWLLAPIYFGLSLGLLALALKFFQEIIHVLPNVFTLAEADLVLVILSL IDMSLVGGLLVMVMISGYENFVSQLDIDDSKEKLSWLGKMDSSSLKMKVAASIVAISSIH LLRVFMDAQNISTDYLMWYVIIHMTFVVSAFVMGYLDRITKH
Uniprot No.

Target Background

Database Links
Protein Families
UPF0114 family
Subcellular Location
Cell membrane; Multi-pass membrane protein.

Q&A

Basic Research Questions

  • How should recombinant PSEEN0819 be properly stored and handled in laboratory settings?

    For optimal results when working with recombinant PSEEN0819, researchers should follow these evidence-based protocols:

    Storage ParameterRecommended ConditionNotes
    Long-term storage-20°C to -80°CAliquoting necessary for multiple use
    Working aliquots4°CStable for up to one week
    Buffer compositionTris/PBS-based, 6% Trehalose, pH 8.0Optimized for stability
    ReconstitutionDeionized sterile water (0.1-1.0 mg/mL)Centrifuge vial before opening
    Cryoprotectant5-50% glycerol (final concentration)50% is standard reference

    Repeated freeze-thaw cycles should be strictly avoided as they significantly reduce protein activity . For experimental reproducibility, consistent handling practices should be maintained across studies.

  • What expression systems are used for producing recombinant PSEEN0819?

    Recombinant PSEEN0819 is predominantly produced using E. coli expression systems. The standard methodology involves:

    1. Cloning the full-length gene (nucleotides encoding amino acids 1-162) into an expression vector

    2. Adding an N-terminal His-tag for purification purposes

    3. Transforming the construct into E. coli expression strains

    4. Inducing protein expression under optimized conditions

    5. Purifying via affinity chromatography targeting the His-tag

    6. Confirming purity (>90%) using SDS-PAGE analysis

    7. Formulating in stabilizing buffer and lyophilizing

    This approach yields recombinant protein suitable for functional studies, antibody production, and structural analyses. Similar methodologies are employed for homologous proteins from P. putida (PputGB1_0714) .

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