Analytical Data
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Gene name
Grpcb
- Application
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Alternative Names
Grpcb；Submandibular gland secretory Glx-rich Protein CB
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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
P08462
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Expression Region
19-247aa
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AA Sequence
TDEEVNNAETSDVPADSEQQPVDSGSDPPSADADAENVQEGESAPPANEEPPATSGSEEEQQQQEPTQAENQEPPATSGSEEEQQQQEPTQAENQEPPATSGSEEEQQQQQPTQAENQEPPATSGSEEEQQQQESTQAENQEPSDSAGEGQETQPEEGNVESPPSSPENSQEQPQQTNPEEKPPAPKTQEEPQHYRGRPPKKIFPFFIYRGRPVVVFRLEPRNPFARRF
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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
GCRB (Glycosylated Collagen Recombination Protein) research focuses on the development and application of recombinant proteins that are pivotal in understanding collagen synthesis and its role in various biological processes. Collagen is a fundamental structural protein in the extracellular matrix, crucial for maintaining tissue integrity and function. Abnormal collagen production is linked to various diseases, including fibrosis, osteogenesis imperfecta, and skin disorders. Traditional methods of obtaining collagen involve animal sources, which raises ethical and practical concerns regarding variability, disease transmission, and the sustainability of harvesting methods. By employing recombinant DNA technology, researchers can produce GCRB in controlled environments, allowing for the generation of specific collagen types with defined properties. This advancement not only enhances the reproducibility of research results but also opens avenues for drug development, regenerative medicine, and tissue engineering. The study of GCRB aims to elucidate its structural and functional characteristics, thereby contributing to our understanding of collagen-related pathologies and facilitating the design of novel therapeutic approaches. As the field progresses, the integration of GCRB into clinical applications may greatly enhance the treatment of collagen-related diseases and improve patient outcomes.
