Analytical Data
-
Gene name
SERP1
- Application
-
Alternative Names
D3Ucla1; Ramp4; Ribosome associated membrane protein 4; Ribosome attached membrane protein 4; Ribosome-attached membrane protein 4; Serp1; SERP1_HUMAN; Stress associated endoplasmic reticulum protein 1; Stress-associated endoplasmic reticulum protein 1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y6X1
-
Expression Region
1-66 aa
-
AA Sequence
MVAKQRIRMANEKHSKNITQRGNVAKTSRNAPEEKASVGPWLLALFIFVVCGSAIFQIIQSIRMGM
-
Molecular Weight
32.89 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
SERP1 (Stress-Associated Endoplasmic Reticulum Protein 1) plays a crucial role in cellular responses to stress, particularly in the context of the endoplasmic reticulum (ER). It is known to be involved in protecting cells from various stress-induced damages, including those caused by protein misfolding and oxidative stress. Recent studies have highlighted its significance in maintaining ER homeostasis and promoting cell survival under adverse conditions. SERP1 has gained attention in the fields of cancer research and neurodegenerative diseases, where ER stress is often implicated in disease progression. Furthermore, the potential of SERP1 as a therapeutic target is being explored, particularly in the development of strategies to enhance cell resilience. The recombinant expression of SERP1 allows for detailed studies of its structure-function relationships and its interactions with other proteins, paving the way for insights into its biological roles. As researchers continue to unravel the complexities of ER stress responses, understanding SERP1's mechanistic pathways could lead to novel interventions for diseases linked to ER dysfunction, ultimately offering hope for improved treatment options in multifaceted health conditions.
