Analytical Data
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Gene name
TMUB2
- Application
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Alternative Names
TMUB2；Transmembrane and ubiquitin-like domain-containing Protein 2
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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
Q71RG4-2
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Expression Region
37-245aa
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AA Sequence
YVADSGSNQL LGAIVSAGDT SVLHLGHVDH LVAGQGNPEP TELPHPSEGN DEKAEEAGEG RGDSTGEAGA GGGVEPSLEH LLDIQGLPKR QAGAGSSSPE APLRSEDSTC LPPSPGLITV RLKFLNDTEE LAVARPEDTV GALKSKYFPG QESQMKLIYQ GRLLQDPART LRSLNITDNC VIHCHRSPPG SAVPGPSASL APSATEPPS
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Molecular Weight
24 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
TMUB2, or Transmembrane and Ubiquitin-like Domain containing protein 2, has garnered attention in recent years due to its crucial role in various cellular processes, including protein folding, degradation, and signal transduction. As a member of the TMUB family, TMUB2 is known to interact with a range of proteins involved in the endoplasmic reticulum (ER) stress response and ubiquitin-proteasome system, which are essential for maintaining cellular homeostasis. Dysregulation of TMUB2 has been implicated in multiple pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders. Research has demonstrated that TMUB2 can modulate the activity of key signaling pathways, thereby influencing cell survival and apoptosis. The study of TMUB2 recombinant protein allows for the exploration of its functional mechanisms and interactions at both molecular and cellular levels, providing insights into its potential as a therapeutic target. Understanding TMUB2's role in disease states could pave the way for novel intervention strategies, emphasizing the importance of this protein in biomedical research. The ongoing investigation into the structure-function relationship of TMUB2 and its implications in human health underscores its significance in the broader context of cellular biology and disease.
