Analytical Data
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Gene name
Granulin
- Application
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Alternative Names
Granulin-3
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Species
Cyprinus carpio
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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
P81015
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Expression Region
1-57aa
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Molecular Weight
13.3 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
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Protein Description
Granulin is a cysteine-rich protein that plays a critical role in various biological processes, including cell proliferation, wound healing, and inflammation. It is composed of multiple granulin motifs and exists in several forms, with granulin A being one of the most studied. Research has shown that granulin is implicated in several diseases, particularly in neurodegenerative conditions such as frontotemporal dementia, where abnormal granulin levels are associated with disease progression. The ability to produce recombinant granulin proteins has become crucial for advancing our understanding of their function and therapeutic potential. Recombinant granulin can be utilized in various experimental settings, allowing researchers to elucidate its role in cellular mechanisms and its interactions with other proteins. Furthermore, studying granulin in its recombinant form can pave the way for the development of targeted therapies that modulate its activity, potentially offering new avenues for the treatment of diseases linked to granulin dysregulation. Understanding the structure-function relationship of granulin through recombinant techniques is essential for harnessing its biological properties and developing innovative strategies for disease intervention. As the research landscape continues to evolve, granulin remains a compelling target for further investigation, particularly concerning its therapeutic applications and implications in health and disease.
