Analytical Data
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Gene name
C9orf82
- Application
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Alternative Names
CAAP1; C9orf82; CAAP; Caspase activity and apoptosis inhibitor 1; Conserved anti-apoptotic Protein; CAAP
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H8G2
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Expression Region
1-361aa
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AA Sequence
MTGKKSSREKRRKRSSQEAAAALAAPDIVPALASGSSGSTSGCGSAGGCGSVSCCGNANFSGSVTGGGSGGSCWGGSSVERSERRKRRSTDSSSVSGSLQQETKYILPTLEKELFLAEHSDLEEGGLDLTVSLKPVSFYISDKKEMLQQCFCIIGEKKLQKMLPDVLKNCSIEEIKKLCQEQLELLSEKKILKILEGDNGMDSDMEEEADDGSKMGSDLVSQQDICIDSASSVRENKQPEGLELKQGKGEDSDVLSINADAYDSDIEGPCNEEAAAPEAPENTVQSEAGQINDLEKDIEKSVNEILGLAESSPNEPKAATLAVPPPEDVQPSAQQLELLELEMRARAIKALMKAGDIKKPA
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Molecular Weight
64.8 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
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Protein Description
C9orf82, a gene located on chromosome 9, has garnered significant attention in recent years due to its association with various neurodegenerative diseases, particularly frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Emerging studies have suggested that mutations and expansions within the C9orf82 gene may play a critical role in the pathogenesis of these conditions, often linked to the accumulation of toxic protein aggregates in neurons. Given its pivotal role in neuronal health, researchers have focused on characterizing the protein product of C9orf82 and understanding its biological functions. The recombinant expression of C9orf82 protein allows for in-depth investigations into its molecular properties, interactions, and effects on cellular pathways that may be disrupted in neurodegenerative disorders. Utilizing various expression systems, scientists aim to produce a stable and functional form of C9orf82 to facilitate studies on its role in cellular processes, such as autophagy and synaptic function. The insights gained from these investigations could shed light on the mechanisms underlying FTD and ALS, potentially leading to the development of therapeutic strategies targeting C9orf82-related pathways. As such, the research on C9orf82 recombinant protein not only contributes to our understanding of its specific biological functions but also provides a promising avenue for addressing the challenges posed by neurodegenerative diseases.
