Analytical Data
-
Gene name
PRL
- Application
-
Alternative Names
PRL；Prolactin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01236
-
Expression Region
1-227aa
-
AA Sequence
MNIKGSPWKGSLLLLLVSNLLLCQSVAPLPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHTSSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIEEQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSHKIDNYLKLLKCRIIHNNNC
-
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
PRL (Prolactin) recombinant proteins have gained significant attention in biomedical research due to their pivotal role in various physiological processes, including lactation, reproduction, and immune regulation. With the advancement of recombinant DNA technology, producing PRL in a controlled laboratory environment allows for the investigation of its structure-function relationships and potential therapeutic applications. The study of PRL and its signaling pathways has expanded our understanding of endocrine functions, particularly in conditions like hyperprolactinemia and related disorders. Furthermore, recombinant PRL can be utilized in drug development, providing insights into its action mechanisms and interactions with other hormones and growth factors. As a result, the exploration of PRL recombinant proteins not only enhances basic scientific knowledge but also opens new avenues for clinical interventions in reproductive health, metabolic diseases, and beyond. This growing body of research underscores the importance of PRL in both health and disease, demonstrating the need for continued investigation into its molecular biology and therapeutic potential.
