Analytical Data
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Gene name
OGFOD2
- Application
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Alternative Names
2-oxoglutarate and iron-dependent oxygenase domain containing 2 ; 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2; DKFZp686H15154; FLJ13491; FLJ37501; MGC120434; MGC120436; OGFD2_HUMAN; OGFOD2
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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
Q6N063
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Expression Region
1-350 aa
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AA Sequence
MATVGAPRHF CRCACFCTDN LYVARYGLHV RFRGEQQLRR DYGPILRSRG CVSAKDFQQL LAELEQEVER RQRLGQESAA RKALIASSYH PARPEVYDSL QDAALAPEFL AVTEYSVSPD ADLKGLLQRL ETVSEEKRIY RVPVFTAPFC QALLEELEHF EQSDMPKGRP NTMNNYGVLL HELGLDEPLM TPLRERFLQP LMALLYPDCG GGRLDSHRAF VVKYAPGQDL ELGCHYDNAE LTLNVALGKV FTGGALYFGG LFQAPTALTE PLEVEHVVGQ GVLHRGGQLH GARPLGTGER WNLVVWLRAS AVRNSLCPMC CREPDLVDDE GFGDGFTREE PATVDVCALT
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Molecular Weight
38.9 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
OGFOD2 (Oxidative Stress Response Protein 2) is a relatively newly identified protein implicated in various cellular processes, particularly related to oxidative stress and protein homeostasis. Research has shown that OGFOD2 plays a crucial role in regulating the stability and function of proteins by catalyzing the formation of specific disulfide bonds, thus influencing protein folding and degradation pathways. Dysregulation of OGFOD2 has been linked to several diseases, including cancer and neurodegenerative disorders, where oxidative stress is a critical contributing factor. Additionally, the protein's involvement in cellular responses to fluctuating environmental conditions has garnered interest for its potential role in metabolic and age-related diseases. Recent studies have focused on the characterization of OGFOD2's enzymatic mechanisms, its interactions with other cellular components, and its significance in the cellular stress response. Understanding OGFOD2's functional capabilities and regulatory mechanisms may provide insights into therapeutic strategies targeting oxidative stress-related conditions, highlighting its potential as a relevant biomarker or therapeutic target in disease contexts. This ongoing research into OGFOD2 emphasizes its importance not only in fundamental biology but also in translational medicine, where manipulating its activity could lead to innovative treatments or interventions to combat diseases associated with oxidative damage and protein misfolding.
