Recombinant Mouse Ceramide synthase 2 (Cers2)

Code CSB-CF852880MO
MSDS
Size Pls inquire
Source in vitro E.coli expression system
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Product Details

Target Names
Cers2
Uniprot No.
Alternative Names
Cers2; Lass2; Trh3; Ceramide synthase 2; CerS2; LAG1 longevity assurance homolog 2; Sphingosine N-acyltransferase CERS2; Translocating chain-associating membrane protein homolog 3; TRAM homolog 3; Tumor metastasis-suppressor gene 1 protein; Very-long-chain ceramide synthase CERS2
Species
Mus musculus (Mouse)
Expression Region
1-380
Target Protein Sequence
MLQTLYDYFWWERLWLPVNLTWADLEDKDGRVYAKASDLYITLPLALLFLVIRYFFELYV ATPLAALLNVKEKTRLRAPPNATLEHFYQTSGKQPKQVEVDLLSRQSGLSGRQVERWFRR RRNQDRPSLLKKFREASWRFTYYLIAFVAGMAVTVDKPWFYDLRKVWEGYPIQSIIPSQY WYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILLCFSWFANYVRAGTLIMALHD ASDYLLESAKMFNYAGWKNTCNNLFIVFAIVFIITRLVIMPFWILHCTMIYPLELYPAFF GYYFFNFMMAVLQMLHIFWAYFILRMAHKFITGKLIEDERSDREETESSEGEETAAGAGA KSRLLANGHPILNNNHPKND
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions.
Gene References into Functions
  1. Gene expression analyses in livers of transgenic mouse mutants revealed that inactivation of CerS2 catalytic activity largely affects transcription of genes involved in lipid metabolism and cell division and is associated with the formation of hepatocellular carcinoma in 6 to 8-week-old mice. PMID: 29653252
  2. Deficiency of CerS2 influences intestinal barrier function and the severity of experimental colitis and may represent a potential mechanism for inflammatory bowel disease pathogenesis. PMID: 28699686
  3. LASS2 plays an important role in efficient liver regeneration in response to partial hepatectomy. PMID: 28958935
  4. Deletion of CerS2 strongly reduced very long-chain ceramides (Cer24:0, 24:1) but concomitantly increased long-chain ceramides and sphinganine in plasma and colon tissue. In naive CerS2(-/-) mice, the expression of tight junction proteins including ZO-1 was almost completely lost in the colon epithelium, leading to increased membrane permeability. Ceramide synthase 2 deficiency aggravates dextran induced colitis in mice. PMID: 28405720
  5. this study shows that Cers2 limits the levels of S1P in thymus and blood to maintain functional S1P gradients that mediate thymocyte emigration into the circulation PMID: 28198542
  6. that only LCBs, the substrates common for all of the CerS isoforms, but not ceramides and complex sphingolipids, were restored to the wild-type levels in the Cers2-rescued Cers1 mutant mouse brains. PMID: 27162368
  7. CerS1, -2, and -6 are hyperacetylated in the mitochondria of SIRT3-null mice. PMID: 26620563
  8. Haploinsufficiency for this enzyme altered the pattern of ceramide acylation in the liver without affecting total ceramide levels, replacing very-long-chain ceramides with long-chain C16-ceramides. PMID: 25295789
  9. Development of pheochromocytoma in ceramide synthase 2 null mice PMID: 26113602
  10. our data strongly indicate that G-CSF-induced CXCR2 expression is regulated in a CerS2-dependent manner and that CerS2 thereby promotes the migration of neutrophils, thus, contributing to inflammation and the development of EAE and MS. PMID: 25697397
  11. study is the first comparison of spatial distribution between SM molecular species and CerS isoforms, and revealed their distinct association in the brain. PMID: 26398595
  12. Data indicate that the augmented rate of death of ceramide synthase 2 (CerS2) null mice is due to elevated levels of tumor necrosis factor alpha (TNFalpha) secretion as a result of enhanced activity of TNFalpha-converting enzyme (TACE). PMID: 26183206
  13. CerS2-deficient kidneys were completely depleted of phytosphingosine-containing cortical sulfatides without any compensatio PMID: 25267995
  14. we first report that Lass2 deficiency caused the downregulation of miR-694 and the upregulation of its target gene Tnfaip3 in vivo in mice, which may be related to a high risk of occurrence of hepatocellular carcinoma PMID: 25333455
  15. The identification of specific cell types in which CerS2 protein is expressed is prerequisite to further mechanistic characterization of phenotypic abnormalities exhibited by CerS2-deficient mice. PMID: 23591958
  16. Lass2 is a protective gene against diethylnitrosamine-induced liver tumorigenesis; and upregulation of the TGF-beta1-Smad4-PAI-1 axis may contribute to the vulnerability of Lass2-knockout mice to diethylnitrosamine. PMID: 24337404
  17. Protection of a ceramide synthase 2 null mouse from drug-induced liver injury: role of gap junction dysfunction and connexin 32 mislocalization. PMID: 24019516
  18. expression and role of ceramide synthase-2 in the lung PMID: 23690971
  19. Ablation of ceramide synthase 2 causes chronic oxidative stress due to disruption of the mitochondrial respiratory chain PMID: 23283968
  20. Loss of ceramide synthase 2 alters lipid metabolic pathways by inhibiting very long acyl chain ceramide synthesis. PMID: 20110363
  21. Loss of CerS2 is associated with hepatocellular carcinoma and hepatomegaly. PMID: 20110366
  22. Results indicate that CERS2 activity supports different biological functions: maintenance of myelin, stabilization of the cerebellar as well as renal histological architecture, and protection against hepatocarcinomas. PMID: 19801672
  23. activity of CerS2 can be regulated by another bioactive sphingolipid, sphingosine 1-phosphate PMID: 18165233

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Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue Specificity
Broadly expressed, with highest levels in liver and kidney. In brain is detected in neurons, oligodentrocytes, ependymal cells and epithelial cells of the choroid plexus. In kidney is detected in collecting ducts and to a lesser degree in proximal tubules
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