Analytical Data
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Gene name
C11orf72
- Application
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Alternative Names
C11orf72Uncharacterized Protein C11orf72
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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
Q8NBR9
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Expression Region
1-251aa
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AA Sequence
MTQLPELGLR SPNNKSPTGP HPLEHLLARL LKRRRRSTLM SSPRSLLCSI SGPGSHLLST HPILCHSVYQ PPQPASRPQA KRYQGLLPVP LAPHPLCLSG QLYLPNIPCT VIDGCGPVIS HLKLTMYPWG LPPSHLGSSS PFSANMEQWD YYKSQTRFAP FLPESFCGSP LPSEQSSRPF GLAFKVLCAA TCQPPQFQLL WLCPYKLDLH QRICLPPNLA LVLLGALWTS PPPGSFLQPP YNRPYKLYKT N
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Molecular Weight
27.88 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
C9orf72 gene, located on chromosome 9, is the most common genetic cause of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). The disease is associated with an expanded hexanucleotide repeat (GGGGCC) in the non-coding region of the gene, leading to the production of toxic dipeptide repeat proteins (DPRs) through a process called repeat-associated non-AUG (RAN) translation. These DPRs, which include poly-Glycine (Gly), poly-Arginine (Arg), and poly-Proline (Pro), accumulate in neuronal and glial cells, contributing to cellular dysfunction and neurodegeneration. Research has shown that these proteins can disrupt various cellular functions, including nucleocytoplasmic transport, RNA metabolism, and mitochondrial integrity. Moreover, the presence of DPRs has been linked to pathological features such as the formation of intracellular aggregates and impairment of autophagy. Understanding the mechanisms by which C9orf72-derived proteins lead to neurodegeneration is crucial for developing targeted therapeutic strategies. Studies continue to explore the pathophysiological roles of these proteins, with a focus on their toxic effects and potential interventions that could mitigate their impact on neuron health and function. Investigating the interactions between DPRs and cellular pathways may reveal new insights into the underlying mechanisms of FTD and ALS, ultimately guiding the development of effective treatments for these debilitating diseases.
