Analytical Data
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Gene name
ERP44
- Application
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Alternative Names
ERP44；KIAA0573；TXNDC4;Endoplasmic reticulum resident Protein 44
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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
Q9BS26
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Expression Region
30-406aa
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AA Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWAGSMEITSLDTENIDE ILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVD CDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKS DPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAF LSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKC VPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEK GTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIP GKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLA PSEYRYTLLRDRDEL
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Molecular Weight
48 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
ERP44, also known as endoplasmic reticulum protein 44, is a key player in the endoplasmic reticulum (ER) quality control system, which ensures that only properly folded proteins are transported to their destinations. This protein is primarily involved in the retention of misfolded proteins within the ER, facilitating their degradation via the ER-associated degradation (ERAD) pathway. Research into ERP44 has gained momentum due to its implications in various diseases, including neurodegenerative disorders and certain cancers, where protein misfolding and ER stress play crucial roles. Additionally, ERP44 has been implicated in the regulation of cellular homeostasis and the inflammatory response, making it a potential target for therapeutic interventions. Understanding the structure and function of ERP44 at the molecular level can provide insights into its mechanism of action and its interactions with other cellular components. Recent studies utilizing recombinant protein techniques have explored the functional properties of ERP44, focusing on its interaction with misfolded proteins and its role in the UPR (unfolded protein response). This growing body of research underscores the importance of ERP44 in cellular health and disease, opening avenues for innovative treatments aimed at restoring ER function and alleviating the consequences of protein misfolding. As such, ERP44 continues to be a vital subject of investigation in the fields of molecular biology and medicine, with potential implications for understanding the fundamental mechanisms underlying protein homeostasis and the development of novel therapeutic strategies.
