| Product Name | UMPS, 1-480aa, Human, Baculovirus |
|---|---|
| Description | UMPS, also known as uridine 5'-monophosphate synthase, is a bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis. It is an indispensable component in this metabolic pathway and is a target for antimalarial and antitumor drugs. Its expression in colorectal carcinoma tissues is not correlated with the toxicities of 5-FU-based regimen, but It in the normal tissues can help predict the toxicities associated with 5-FU. Recombinant human UMPS, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Synonyms | Uridine 5'-monophosphate synthase, UMPS, OPRT |
| Host | Virus |
| Molecular Weight |
65.1kDa (592aa) 70-100kDa (SDS-PAGE under reducing conditions) |
| Amino Acid Sequence | 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 HHHHHH |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol. |
| Concentration | 1mg/ml (determined by Absorbance at 280nm) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Zhang Y., et al. (2013) J Biol Chem. 288:34746-34754. Dong Q., et al. (2012) Nan Fang Yi Ke Da Xue Xue Bao. 32:1179-1181. |
| Background | UMPS, also known as uridine 5'-monophosphate synthase, is a bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis. It is an indispensable component in this metabolic pathway and is a target for antimalarial and antitumor drugs. Its expression in colorectal carcinoma tissues is not correlated with the toxicities of 5-FU-based regimen, but It in the normal tissues can help predict the toxicities associated with 5-FU. Recombinant human UMPS, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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