Analytical Data
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Gene name
HERPUD2
- Application
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Alternative Names
HERPUD2; Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein
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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
Q9BSE4
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Expression Region
1-406aa
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AA Sequence
MDQSGMEIPVTLIIKAPNQKYSDQTISCFLNWTVGKLKTHLSNVYPSKPLTKDQRLVYSGRLLPDHLQLKDILRKQDEYHMVHLVCTSRTPPSSPKSSTNRESHEALTSSSNSSSDHSGSTTPSSGQETLSLAVGSSSEGLRQRTLPQAQTDQAQSHQFPYVMQGNVDNQFPGQAAPPGFPVYPAFSPLQMLWWQQMYAHQYYMQYQAAVSAQATSNVNPTQPTTSQPLNLAHVPGEEPPPAPNLVAQENRPMNENVQMNAQGGPVLNEEDFNRDWLDWMYTFSRAAILLSIVYFYSSFSRFIMVMGAMLLVYLHQAGWFPFRQEGGHQQAPNNNAEVNNDGQNANNLELEEMERLMDDGLEDESGEDGGEDASAIQRPGLMASAWSFITTFFTSLIPEGPPQVAN
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Molecular Weight
71.6 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
HERPUD2 (Hypoxia-Associated Endoplasmic Reticulum Protein 2) is a member of the HERP family, which plays a crucial role in cellular stress responses, particularly during hypoxic conditions. Emerging evidence suggests that HERPUD2 is involved in the regulation of protein folding and degradation pathways within the endoplasmic reticulum (ER), thereby influencing cellular survival and function under stress. Its expression is upregulated in various pathological conditions, including cancer and neurodegenerative diseases, indicating its potential role in disease progression and cellular adaptation. Research investigating HERPUD2 recombinant proteins has garnered interest due to their potential applications in both diagnostics and therapeutics. By studying HERPUD2, scientists aim to understand its molecular mechanisms, elucidate its interactions within the ER stress response pathway, and explore its implications in diseases characterized by ER stress. Furthermore, recombinant HERPUD2 could serve as a valuable tool for screening compounds that modulate ER stress responses, ultimately paving the way for novel therapeutic strategies targeting diseases related to ER dysfunction. As such, ongoing studies are focused on the characterization of HERPUD2's structure and function, contributing to the broader understanding of cellular stress responses and their relevance in health and disease.
