Recombinant Human Carbamoyl-Phosphate Synthase [Ammonia], Mitochondrial (CPS1) Protein (His)

Name: Recombinant Human Carbamoyl-Phosphate Synthase [Ammonia], Mitochondrial (CPS1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04739P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Carbamoyl-Phosphate Synthase [Ammonia], Mitochondrial (CPS1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P31327
Target Symbol	CPS1
Synonyms	Carbamoyl phosphate synthase [ammonia]; Carbamoyl phosphate synthase [ammonia] mitochondrial; Carbamoyl phosphate synthase; Carbamoyl phosphate synthetase 1; Carbamoyl phosphate synthetase 1 mitochondrial; Carbamoyl phosphate synthetase I; Carbamoyl-phosphate synthase [ammonia]; Carbamoyl-phosphate synthetase I; Carbamoylphosphate synthase; Carbamoylphosphate synthetase 1; Carbamoylphosphate synthetase I; CPS 1; Cps1; CPSase 1; CPSase I; CPSASE1; CPSM_HUMAN; mitochondrial; MS738
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
Expression Range	1354-1500aa
Protein Length	Partial
Mol. Weight	20.5 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Subcellular Location	Mitochondrion. Nucleus, nucleolus.
Database References	HGNC: 2323 OMIM: 237300 KEGG: hsa:1373 STRING: 9606.ENSP00000402608 UniGene: PMID: 29441491 Allele and genotype frequencies of the p.Thr1406Asn polymorphism did not differ between the infants with and without NEC, but the minor A-allele was less frequent in the group of 64 infants with the combined outcome NEC or death before 34 weeks of corrected gestational age than in the infants without this outcome. A significant negative association of the A-allele with the combined outcome NEC or death was found. PMID: 27833157 HNF3beta plays a vital role in regulation of CPS1 gene and could promote the metabolism of ammonia by regulating CPS1 expression. PMID: 28272778 CPS1 maintains pyrimidine pools and DNA synthesis in KRAS/LKB1-mutant lung cancer cells PMID: 28538732 CPS1 knockdown reduced cell growth, decreased levels of metabolites associated with nucleic acid biosynthesis. PMID: 28376202 These results may offer an increasing understand that CPS1 might have a function in differentiation. PMID: 27425868 Molecular structure of CPS1 has been deciphered. PMID: 26592762 CPS1 and CPS1IT1 may be potential prognostic indicators for patients with intrahepatic cholangiocarcinoma. PMID: 26499888 CPS1 is involved in the urea cycle in weight maintenance. PMID: 26938218 These results suggest that glycine metabolism and/or the urea cycle represent potentially novel sex-specific mechanisms for the development of atherosclerosis. PMID: 26822151 Mechanism for Switching On/Off the Urea Cycle PMID: 26059772 More HCC cells could be identified by the antibody cocktail for CPS1 and P-CK compared with a single antibody. PMID: 24763545 characterized the only currently known recurrent CPS1 mutation, p.Val1013del found in eleven unrelated patients of Turkish descent; mutation p.V1013del inactivates CPS1 but does not render the enzyme grossly unstable or insoluble PMID: 25410056 Overexpression of CPS1 is associated with rectal cancers. PMID: 25099619 study examined patient characteristics, including genetic polymorphism, to identify risk factors associated with development of hyperammonemia during valproic acid-based therapy; found CPS1 4217C>A polymorphism may not be associated with development of hyperammonemia in Japanese population PMID: 24888247 Findings support the disease-causing role of the mutations reported to affect the CPS1 deficiency, revealing a key role of the small CPS1 domain of unknown function (UFSD) for proper enzyme folding. PMID: 24813853 CPS1 becomes readily detectable upon hepatocyte apoptotic and necrotic death. Its abundance and short serum half-life suggest that it may be a useful prognostic biomarker in acute liver injury. PMID: 24924744 Data show that carbamoyl phosphate synthetase 1, an enzyme involved in the urea cycle, 8-oxoguanine DNA glycosylase 1 and DNA polymerase beta, enzymes involved in DNA repair, were expressed at higher levels in Batten disease cells than in normal cells. PMID: 22692827 the human CPS unknown function domains are spatially located in a region that corresponds to the a/b subunits interface in Escherichia coli CPS. [Review] PMID: 22521883 Mutation analysis in these patients identified 17 genetic lesions, 9 of which were new confirming their "private" nature. PMID: 22173106 Case Report: Late-onset carbamoyl phosphate synthetase 1 deficiency in an adult cured by liver transplantation. PMID: 21837743 This is the first large-scale report of CPS1 mutations spanning a wide variety of molecular defects highlighting important regions in this protein. PMID: 21120950 DNA methylation is a key mechanism of silencing CPS1 expression in human hepatocellular carcinoma cells. PMID: 21281797 structure-function analysis and pathogenicity-testing of mutations in CPS1 PMID: 20800523 Data reported five of the CPS1 mutations (p.T471N, p.Q678P, p.P774L, p.R1453Q, and p.R1453W) in severe CPS1D patients. PMID: 20578160 The present study in preterm infants did not confirm the earlier reported association between CPS1 genotype and L-arginine levels in term infants. PMID: 20520828 These data confirm a recent finding that CPS1 is a locus influencing homocysteine levels in women and suggest that genetic effects on Hcy may differ across developmental stages. PMID: 20154341 Meta-analysis and genome-wide association study of gene-disease association. (HuGE Navigator) PMID: 20383146 Observational study and genome-wide association study of gene-disease association and gene-gene interaction. (HuGE Navigator) PMID: 20154341 CPS1, MUT, NOX4, and DPEP1 is associated with plasma homocysteine in healthy Women. PMID: 20031578 Allelic imbalance may explain clinical variability in CPS1 deficiency in some families. PMID: 19793055 The entire DNA sequence of the human CPS1 gene is presented, including all exon-intron boundaries. PMID: 12655559 CPSI T1405N genotype appears to be an important new factor in predicting susceptibility to pulmonry hypertension following surgical repair of congenital cardiac defects in children. PMID: 17188582 CPPS1 T1404N polymorphism may be associated with the risk of necrotizing enterocolitis in preterm infants. PMID: 17597649 Tight hydrogen binding mode is supported by the observation of reduced NAG affinity upon mutation of N-acetyl-L-glutamate-interacting residues of CPSI PMID: 19754428 The differential expression of Hep Par 1(carbamoyl phosphate synthetase I) in dysplastic vs malignant tumors of the small intestine may be diagnostically useful in difficult cases. PMID: 19926579

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.