Analytical Data
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Gene name
HERPUD1
- Application
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Alternative Names
HERPUD1;HERP;KIAA0025;MIF1;Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 Protein
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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
Q15011
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Expression Region
1-263aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD
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Molecular Weight
32 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
HERPUD1 (Homocysteine Inducible, Endoplasmic Reticulum Stress-Related Protein) is a protein that plays a crucial role in the cellular response to endoplasmic reticulum (ER) stress. The accumulation of misfolded proteins in the ER triggers a stress response that can lead to cellular dysfunction and apoptosis if not properly managed. HERPUD1 is known to be upregulated under conditions of oxidative stress and is implicated in various pathological processes, including neurodegenerative diseases and cancer. Research indicates that HERPUD1 contributes to the proteostasis network by facilitating the degradation of misfolded proteins through an autophagic pathway, thereby maintaining cellular homeostasis. The recombination and characterization of HERPUD1 provide valuable insights into its structural and functional properties, helping to elucidate its specific mechanisms in regulating ER stress responses. Understanding HERPUD1’s role could unveil potential therapeutic targets for diseases associated with ER stress and protein misfolding. Moreover, the recombinant protein can be utilized in further studies to explore its interactions with other cellular components, paving the way for novel strategies in drug design and therapeutic interventions. Thus, HERPUD1 serves as a significant focus in the context of cellular stress responses, highlighting the importance of maintaining protein quality control systems in health and disease.
