Analytical Data
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Gene name
UBQLNL
- Application
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Alternative Names
UBQLNLUbiquilin-like Protein
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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
Q8IYU4
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Expression Region
1-475 aa
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AA Sequence
MWHAISRTSR MSQSGCPSGL LADKNISSSA TRVIVKTAGN QKDFMVADDI SVRQFKEMLL AHFQCQMDQL VLVFMGCLLK DHDTLSQRGI MDGHTIYLVI KSKQGSRSLA HSFRDLPTND PCHRDRNTKG NSSRVHQPTG MNQAPVELAH FVGSDAPKVH TQNLEVSHPE CKAQMLENPS IQRLLSNMEF MWQFISEHLD TQQLMQQNPE VSRLLLDNSE ILLQTLELAR NLAMIQEIMQ IQQPSQNLEY PLNPQPYLGL ETMPGGNNAL GQNYADINDQ MLNSMQDPFG GNPFTALLAG QVLEQVQSSP PPPPPSQEQQ DQLTQHPATR VIYNSSGGFS SNTSANDTLN KVNHTSKANT AMISTKGQSH ICATRQPAWI PALPSIELTQ QLQEEYKDAT VSLSSSRQTL KGDLQLSDEQ SSSQITGGMM QLLMNNPYLA AQIMLFTSMP QLSEQWRQQL PTFLQQTQIS DLLSA
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Molecular Weight
52.8 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
UBQLNL (Ubiquilin 1-like protein) is a member of the ubiquitin-like protein family, which plays a critical role in regulating protein degradation and cellular homeostasis. Recent studies have highlighted its involvement in various cellular processes, including autophagy, proteasomal degradation, and the regulation of misfolded proteins. Dysregulation of UBQLNL has been linked to several neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, where protein aggregation contributes to cellular toxicity. The study of UBQLNL as a recombinant protein is gaining traction due to its potential therapeutic implications; understanding its structure and function could lead to novel strategies for modulating misfolded protein clearance. The production of UBQLNL as a recombinant protein provides a means to explore its biochemical properties and interactions with other cellular components, facilitating the development of targeted therapies that can enhance protein degradation pathways. Consequently, research on UBQLNL not only contributes to the fundamental knowledge of protein quality control mechanisms but also holds promise for advancing treatment options for diseases characterized by protein aggregation.
