Analytical Data
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Gene name
Gbal
- Application
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Alternative Names
Gbal；CTR；Guanine nucleotide-binding Protein subunit alpha homolog
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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
A0A1L8FDF0
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Expression Region
1-519aa
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AA Sequence
MWSWFLPILGVLVLARGSSGGRLCAPLNFGQSSVVCQCNATYCDTLDPIVVPSVGNFSVYETSQSGKRLQVMSGTFTKRQPSPMDLVLTLNDKKKFQTIKGFGGAVTDSAALNILSLSDETKENLLRSYFSEEGIGYNILRVPMGSCDFSTRIYTYLDTEGDFSMKTFSLQVEDTKLKIPLIQKAKELSNRSISLFASPWTSPPWMKTNGAITGKGTLKGKPGDQYHKTWANYFIRFLDEYAKLNVTFWAVTVENEPTAGLVTDYPFQSLGFTPEHMRDFIASDLGPAFANSSHKQVKIMILDDNRLLLPYWAKVILSDLKAARYVHGIAVHWYLDAIVPADVTLGRTHQLYPDYFLFASEACTGFTPWNKGVQLGCWDRGNQYSHRIIEDLNYYVTGWTDWNLALDIEGGPTWVENNVDSPIIVDLSKDVFYKQPMFYHMAHFSKFIPEGSRRVGLDLNQGSQLETVAFLSPDGSVAVVVVLNRESVDVKFLISDPSLGVIDTVSPANSIQTYIWRRQ
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Molecular Weight
58.1 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
Gbal, a novel recombinant protein, has gained attention in the field of biomedical research due to its potential applications in therapeutic interventions and biopharmaceuticals. The backdrop of Gbal research is rooted in the increasing demand for efficient protein-based solutions to address various health challenges, particularly in the realms of cancer treatment, immunotherapy, and regenerative medicine. Researchers have focused on the unique structural and functional properties of Gbal, which is derived from specific genetically engineered organisms, allowing for enhanced purity, stability, and bioactivity compared to naturally occurring proteins. The optimization of Gbal’s expression and purification processes has also been a focal point, aiming to reduce production costs while maintaining high yields. Furthermore, studies exploring the protein's interaction with biological pathways are crucial in understanding its mechanisms of action, which may pave the way for novel drug development. As Gbal progresses through preclinical evaluations, its potential as a therapeutic agent continues to be elucidated, highlighting the importance of ongoing research in recombinant protein technologies. Overall, Gbal represents a significant step forward in the field, offering promising avenues for future innovation and application in medicine.
