Analytical Data
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Gene name
gland
- Application
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Alternative Names
/
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Species
Dog
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01002
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Expression Region
1-115aa
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Molecular Weight
17.8 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
The study of gland recombinant proteins has garnered significant attention due to their potential applications in biotechnology and medicine. Recombinant proteins are expressed from cloned genes inserted into host cells, often allowing for the production of proteins that are either difficult to purify from natural sources or not feasible to obtain in sufficient quantities. Glands, which are specialized organs that secrete hormones, enzymes, and other substances, serve as crucial sources of proteins with diverse biological functions. By utilizing recombinant DNA technology, researchers can manipulate the genes responsible for producing these proteins, enabling the study of their structure, function, and interactions in a controlled environment. This approach is particularly valuable for the production of therapeutic proteins, such as insulin and monoclonal antibodies, as well as for understanding endocrine functions and developing new treatments for diseases related to glandular dysfunction. Furthermore, recombinant gland proteins can be engineered to enhance their efficacy, stability, and specificity, facilitating advances in drug development and therapeutic strategies. The ongoing research in this field not only aims to improve protein production methods but also to unravel the complex roles these proteins play in physiological and pathological processes, paving the way for innovative medical interventions and applications in personalized medicine.
