Analytical Data
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Gene name
PRLR
- Application
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Alternative Names
PRLR；Prolactin receptor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16471
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Expression Region
25-234aa
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AA Sequence
QLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMND
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Molecular Weight
27.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
PRLR (Prolactin Receptor) is a critical protein involved in various physiological processes, including lactation, immune function, and reproductive health. The study of PRLR and its recombinant protein form has gained significant attention in recent years due to its potential implications in understanding endocrine signaling pathways and their associated disorders. Abnormal PRLR signaling has been linked to several pathological conditions, including breast cancer, infertility, and metabolic disorders. Researchers have focused on producing recombinant PRLR protein to elucidate its structural and functional properties, contributing to the development of therapeutic strategies targeting PRLR-mediated pathways. Advances in recombinant protein technology have facilitated the generation of PRLR variants, allowing for detailed studies on receptor-ligand interactions and downstream signaling mechanisms. By investigating PRLR's role in cellular signaling, researchers aim to identify potential biomarkers for disease diagnosis and explore novel treatments. Additionally, the recombinant PRLR protein serves as a valuable tool in pharmacological studies to assess the efficacy of drugs that modulate PRLR activity, further emphasizing its relevance in both basic research and clinical applications. Overall, the exploration of PRLR recombinant protein continues to provide insights into its biological significance and potential therapeutic avenues, underscoring its importance in health and disease.
