Analytical Data
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Gene name
WDR92
- Application
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Alternative Names
FLJ31741; Monad; OTTHUMP00000205522; WD repeat domain 92; WD repeat-containing Protein 92; WD repeat-containing Protein Monad; Wdr92; WDR92_HUMAN
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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
Q96MX6
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Expression Region
1-357 aa
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AA Sequence
MSAFEKPQII AHIQKGFNYT VFDCKWVPCS AKFVTMGNFA RGTGVIQLYE IQHGDLKLLR EIEKAKPIKC GTFGATSLQQ RYLATGDFGG NLHIWNLEAP EMPVYSVKGH KEIINAIDGI GGLGIGEGAP EIVTGSRDGT VKVWDPRQKD DPVANMEPVQ GENKRDCWTV AFGNAYNQEE RVVCAGYDNG DIKLFDLRNM ALRWETNIKN GVCSLEFDRK DISMNKLVAT SLEGKFHVFD MRTQHPTKGF ASVSEKAHKS TVWQVRHLPQ NRELFLTAGG AGGLHLWKYE YPIQRSKKDS EGIEMGVAGS VSLLQNVTLS TQPISSLDWS PDKRGLCVCS SFDQTVRVLI VTKLNKI
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Molecular Weight
39.7 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
WDR92, or WD repeat domain 92, is a protein that has garnered increasing attention in the field of molecular biology due to its potential roles in various cellular processes. It belongs to the WD-repeat protein family, characterized by the presence of tandem repeats of tryptophan-aspartic acid (WD) motifs, which are often implicated in protein-protein interactions. Research indicates that WDR92 may be involved in critical biological functions, including cell signaling, apoptosis, and the regulation of gene expression. Its expression levels have been correlated with various diseases, particularly cancer, where it may contribute to tumorigenesis and progression. Additionally, WDR92 has been suggested to play a role in immune response and cellular stress, making it a candidate for further investigation in therapeutic contexts. The study of WDR92, particularly in the context of its interaction networks and functional mechanisms, is essential for understanding its contribution to normal physiology and disease pathology. Recent advances in recombinant protein technology have enabled the production of WDR92 in a laboratory setting, facilitating detailed biochemical analyses and the exploration of its structure-function relationship. Understanding the functional significance of WDR92 may pave the way for novel diagnostics and therapeutic strategies targeting related pathological conditions. Thus, ongoing research into this protein is not only relevant for basic science but also holds promise for translational applications in medicine.
