Analytical Data
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Gene name
NACA
- Application
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Alternative Names
NACA;Nascent polypeptide-associated complex subunit alpha
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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
Q13765
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Expression Region
1-215aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMPGEATETVPATEQELPQPQAETGSGTESD SDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAM SKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIED LSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKD IELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM
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Molecular Weight
26 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
NACA, or Nascent Polypeptide-Associated Complex, is a protein complex implicated in the co-translational folding and targeting of nascent polypeptides. Its research background is rooted in the need to understand the intricacies of protein synthesis and folding within the endoplasmic reticulum (ER). The intricate processes of protein synthesis and folding are crucial for cellular function and overall organismal health. Misfolded proteins can lead to numerous diseases, including neurodegenerative disorders and various types of cancer. NACA plays a significant role in assisting the nascent polypeptide chains as they emerge from the ribosome, helping to ensure that they fold correctly and are properly directed to their functional locations within the cell. Investigating NACA and its interactions with other chaperones and folding factors provides valuable insights into the mechanisms underlying protein homeostasis and the cellular stress responses. This research is particularly relevant in the context of developing therapeutic strategies aimed at mitigating the effects of protein misfolding and aggregation. Moreover, the study of NACA contributes to a broader understanding of cellular stress response pathways and their implications in various diseases, thereby highlighting the importance of protein quality control systems in maintaining cellular integrity. Overall, the exploration of NACA and its biological functions is essential for advancing our knowledge of molecular biology and developing potential interventions for diseases linked to protein misfolding.
