Analytical Data
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Gene name
UMPS
- Application
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Alternative Names
UMPS；Uridine 5'-monophosphate synthase
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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
P11172
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Expression Region
1-480aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV
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Molecular Weight
54 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
UMPS (uridine monophosphate synthetase) is a key enzyme in the pyrimidine nucleotide biosynthesis pathway, catalyzing the conversion of orotate to uridine monophosphate (UMP) through a two-step reaction involving orotate phosphoribosyltransferase and orotidine-5'-monophosphate decarboxylase. Research on UMPS has gained momentum due to its critical role in nucleic acid metabolism, which is essential for cell proliferation, growth, and differentiation. Aberrations in UMPS activity are associated with various pathological conditions, including certain cancers and metabolic disorders. As a result, UMPS has emerged as a promising target for drug development, and generating recombinant UMPS protein is crucial for understanding its structure-function relationships and for screening potential inhibitors. The production of recombinant UMPS allows for detailed kinetic studies and structural analyses, facilitating insights into its enzymatic mechanism and regulation. Furthermore, understanding UMPS's role in the context of cellular metabolism may unveil novel therapeutic strategies for diseases linked to altered nucleotide synthesis. This research not only contributes to the fundamental understanding of UMPS but also paves the way for innovative approaches in designing drugs that can modulate its activity for therapeutic purposes.
