Analytical Data
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Gene name
RPN2/Ribophorin II
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简介
RPN2/riboprotein II is a key subunit of the oligosaccharyltransferase (OST) complex, which catalyzes the initial glycan transfer during co-translational protein N-glycosylation. This critical step occurs in the nascent polypeptide chain and involves the transfer of defined glycans from polyhydroxypyrophosphate to asparagine residues in the Asn-X-Ser/Thr motif. RPN2/Ribophorin II Protein, Human (HEK293, Fc) is the recombinant human-derived RPN2/Ribophorin II protein, expressed by HEK293 , with C-hFc labeled tag.
- Application
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Alternative Names
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2; RIBIIR; RPN-II; RPN2
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Species
Human
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04844-1
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Expression Region
M1-V540
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Protein Length
Partial
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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
RPN2, also known as Ribophorin II, is a crucial component of the N-glycosylation pathway and is primarily associated with the endoplasmic reticulum (ER). It is integral to the proper folding and maturation of glycoproteins, influencing various cellular processes, including protein synthesis and trafficking. Given its role in glycoprotein biosynthesis, RPN2 has been implicated in several diseases, including cancer and neurodegenerative disorders. The study of recombinant RPN2/Ribophorin II proteins is pivotal for understanding its functional mechanisms and interactions, particularly concerning its role in the ER and the Golgi apparatus. By producing RPN2 in a recombinant form, researchers aim to obtain a purified, functional protein that can be used to elucidate its structural and biochemical properties. This research not only aids in deciphering the biological role of RPN2 but also provides potential avenues for therapeutic interventions targeting diseases linked to its dysfunction. The ability to manipulate RPN2 expression and function could lead to innovative strategies in biotechnology and medicine, promoting the development of novel treatments for conditions arising from aberrant glycoprotein processing.
