Analytical Data
-
Gene name
SPPL3
- Application
-
Alternative Names
SPPL3; IMP2; PSL4; Signal peptide peptidase-like 3; SPP-like 3; EC 3.4.23.-; Intramembrane protease 2; IMP-2; Presenilin homologous protein 1; PSH1; Presenilin-like protein 4
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8TCT6
-
Expression Region
1-384 aa
-
AA Sequence
MAEQTYSWAYSLVDSSQVSTFLISILLIVYGSFRSLNMDFENQDKEKDSNSSSGSFNGNSTNNSIQTIDSTQALFLPIGASVSLLVMFFFFDSVQVVFTICTAVLATIAFAFLLLPMCQYLTRPCSPQNKISFGCCGRFTAAELLSFSLSVMLVLIWVLTGHWLLMDALAMGLCVAMIAFVRLPSLKVSCLLLSGLLIYDVFWVFFSAYIFNSNVMVKVATQPADNPLDVLSRKLHLGPNVGRDVPRLSLPGKLVFPSSTGSHFSMLGIGDIVMPGLLLCFVLRYDNYKKQASGDSCGAPGPANISGRMQKVSYFHCTLIGYFVGLLTATVASRIHRAAQPALLYLVPFTLLPLLTMAYLKGDLRRMWSEPFHSKSSSSRFLEV
-
Molecular Weight
68.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SPPL3 (signal peptide peptidase-like 3) is an intramembrane aspartyl protease involved in the process of protein maturation and the modulation of cellular signaling pathways. Research into SPPL3 has gained traction due to its pivotal role in the release of bioactive peptides from precursor proteins, particularly in immune responses and neurodegenerative diseases. The enzyme is known to cleave specific signal peptides, influencing various physiological processes, including T cell activation and inflammation. Recent studies have highlighted its significance in the endoplasmic reticulum, where it facilitates the generation of lipid-modifying enzymes and regulates cholesterol metabolism. Given its involvement in crucial cellular functions, SPPL3 has emerged as a potential therapeutic target for various disorders, including cancer and autoimmune diseases. Understanding the structure and function of SPPL3 through recombinant protein studies is essential for elucidating its mechanisms of action and may pave the way for novel interventions in diseases associated with dysregulated peptide processing.
