Analytical Data
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Gene name
RLN2
- Application
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Alternative Names
H2; RLXH2; Relaxin H2; Prorelaxin H2; Relaxin,Ovarian,Of Pregnancy; Prorelaxin H2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04090
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Expression Region
Met1~Cys185
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Molecular Weight
22&44kDa
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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
RLN2, or Relaxin-2, is a peptide hormone that belongs to the relaxin family, primarily involved in reproductive processes and tissue remodeling. Its research has gained significant attention due to its potential therapeutic applications in various medical fields, including cardiology, reproductive medicine, and fibrotic diseases. RLN2 is known for its ability to induce vasodilation, promote angiogenesis, and modulate collagen synthesis, making it a candidate for treating conditions like heart failure and hypertension. Furthermore, its role in pregnancy and childbirth has significant implications in obstetrics. The recombinant production of RLN2 has enabled researchers to obtain this hormone in a controlled and efficient manner, facilitating extensive studies into its biology and therapeutic properties. Analyzing RLN2’s mechanisms of action at the molecular level can lead to the development of novel treatments that leverage its beneficial effects on tissue repair and regeneration. Overall, the research into RLN2 recombinant protein holds promise for enhancing our understanding of its physiological roles and translating these insights into clinical applications.
