Recombinant Human CAD protein (CAD), partial

Code CSB-YP326741HU
MSDS
Size $276
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Activity
Not Test
Target Names
CAD
Uniprot No.
Research Area
Others
Species
Homo sapiens (Human)
Source
Yeast
Expression Region
1456-1846aa
Target Protein Sequence
MTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPD
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
43.5 kDa
Protein Length
Partial
Tag Info
C-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
Gene References into Functions
  1. CAD dihydroorotase and aspartate transcarbamoylase domains self-assembles into dimers and trimers. PMID: 28552578
  2. Detection of the CAD-ALK gene fusion in urine tr-DNA anticipated radiological confirmation of disease progression. Analysis of plasma ctDNA identified ALK kinase mutations that emerged during treatment with the ALK inhibitor entrectinib PMID: 28368455
  3. Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes. PMID: 28833948
  4. This study showed that CAD deficiency co-occurrence of anaemia, anisopoikilocytosis, global developmental delay, and seizures. PMID: 28007989
  5. Previous study found three metal ions in huDHOase active site; in the present study, the putative third metal binding site in type II enzymes, such as StDHOase and ScDHOase, was created and identified. PMID: 26446564
  6. Changes in glycosylation in caused by mutations in CAD. PMID: 25678555
  7. These results establish CAD as a downstream effector of Rheb and suggest a possible role of Rheb in regulating de novo pyrimidine nucleotide synthesis PMID: 25422319
  8. Recombinant aspartate carbamoyltransferase domain from the CAD enzyme complex forms homotrimers in solution. PMID: 24316846
  9. The results obtained indicate that mLST8 bridges between CAD and mTOR, and plays a role in the signaling mechanism where CAD is regulated in the mTOR pathway through the association with mLST8 PMID: 23594158
  10. preliminary X-ray diffraction analysis of the dihydroorotase domain of human CAD PMID: 23143245
  11. findings show that in prostate tumor cells, CAD fosters androgen receptor translocation into the nucleus and stimulates its transcriptional activity; in radical prostatectomy specimens, CAD expression was not correlated with proliferation markers, but a higher CAD mRNA level was associated with local tumor extension and cancer relapse PMID: 21982950
  12. the cad gene is regulated by a nonclassical ERalpha/Sp1-mediated pathway. PMID: 12746293
  13. Data show that PRMT5 can be found in association with hSWI/SNF complexes and is involved in regulating the expression of carbamoyl-phosphate synthase-aspartate carbamoyltransferase-dihydroorotase. PMID: 14559996
  14. the nuclear import of CAD appears to promote optimal cell growth PMID: 15890648
  15. cad gene expression is repressed by hypoxia-inducible factor-1alpha, which represents a functional link between hypoxia and cell-cycle arrest. PMID: 16155188
  16. hCPS_DeltaA was not able to fully assume the catalytically competent conformation, with specific activity of CP formation decreased 700-fold. PMID: 18679823

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Involvement in disease
Epileptic encephalopathy, early infantile, 50 (EIEE50)
Subcellular Location
Cytoplasm. Nucleus. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth.
Protein Families
Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily
Database Links

HGNC: 1424

OMIM: 114010

KEGG: hsa:790

STRING: 9606.ENSP00000264705

UniGene: Hs.377010

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