Analytical Data
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Gene name
OSTM1
- Application
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Alternative Names
OSTM1；GL；Osteopetrosis-associated transmembrane Protein 1
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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
Q86WC4
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Expression Region
1-284aa
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AA Sequence
MEPGPTAAQR RCSLPPWLPL GLLLWSGLAL GALPFGSSPH RVFHDLLSEQ QLLEVEDLSL SLLQGGGLGP LSLPPDLPDL DPECRELLLD FANSSAELTG CLVRSARPVR LCQTCYPLFQ QVVSKMDNIS RAAGNTSESQ SCARSLLMAD RMQIVVILSE FFNTTWQEAN CANCLTNNSE ELSNSTVYFL NLFNHTLTCF EHNLQGNAHS LLQTKNYSEV CKNCREAYKT LSSLYSEMQK MNELENKAEP GTHLCIDVED AMNITRKLWS RTFNCSVPCS DTVP
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Molecular Weight
30 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
OSTM1 (OST-48, hOST-48, or Oligosaccharyltransferase Subunit 1) is a critical protein involved in the N-glycosylation process, which plays a vital role in protein folding, stability, and function. Research into OSTM1 has gained momentum due to its implications in various cellular processes and diseases, including its potential role in cancer progression and autoimmune disorders. OSTM1 is part of the oligosaccharyltransferase complex responsible for transferring oligosaccharides to nascent proteins in the endoplasmic reticulum (ER). Proper glycosylation is essential for protein maturation and function, and any dysregulation can lead to pathological conditions. Investigating the structure, function, and regulation of OSTM1 not only enhances our understanding of glycosylation but also provides insights into therapeutic strategies for diseases associated with glycosylation defects. Advances in recombinant protein technology have enabled the expression and purification of OSTM1, facilitating detailed studies of its biochemical properties and interactions with other cellular components. This research is crucial for elucidating the mechanisms by which OSTM1 contributes to cellular homeostasis and identifying potential molecular targets for drug development, offering promising avenues for innovative treatments in the context of glycosylation-related disorders.
