Recombinant Human Pancreatic triacylglycerol lipase (PNLIP)

Code CSB-YP018262HU
MSDS
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Source Yeast
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Code CSB-EP018262HU
MSDS
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Source E.coli
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Code CSB-EP018262HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018262HU
MSDS
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Source Baculovirus
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Code CSB-MP018262HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PNLIP
Uniprot No.
Alternative Names
lipase, pancreatic; LIPP_HUMAN; Pancreatic lipase; Pancreatic triacylglycerol lipase; PL; PNLIP; PNLIPD; PTL; Triacylglycerol acylhydrolase
Species
Homo sapiens (Human)
Expression Region
17-465
Target Protein Sequence
KEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC
Protein Length
Full Length of Mature 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.

Customer Reviews and Q&A

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Target Background

Function
Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones.
Gene References into Functions
  1. Serum lipase subtype analysis cannot replace the standard lipase measurement for the diagnosis of acute pancreatitis, but the test demonstrated adequate sensitivity for use in triage or as an add-on test for serum lipase elevation. PMID: 27243230
  2. Presence of methionine at position 221 in the PNLIP protein sequence causes protein misfolding and aggregation. PMID: 25862608
  3. All these findings support the use of YLLIP2 in enzyme replacement therapy for the treatment of pancreatic exocrine insufficiency, a pathological situation in which an acidification of intestinal contents occurs. PMID: 24650780
  4. In patients with intraductal papillary mucinous neoplasm without a history of pancreatitis, serum pancreatic lipase and amylase outside normal range are associated with risk of malignancy. PMID: 25239347
  5. a novel mutation in the PNLIP gene in two brothers with congenital pancreatic lipase deficiency PMID: 24262094
  6. Low PNLIP expression is associated with pancreatic cancer. PMID: 23918603
  7. Triacylglycerol lipase and alpha-amylase are highly over-expressed in pancreatic cyst fluids in patients with mucinous pancreatic neoplasms. PMID: 22393262
  8. Combination of two mutations with a promising one at the entrance of the catalytic cavity (K80E) negatively affected the lipase activity at neutral pH but not that at acidic pH. PMID: 20150178
  9. the amplitude of the lid opening measured in solution or in a frozen solution in the presence of amphiphiles PMID: 20136147
  10. Review. The structure and function of the pancreatic lipase C2 domains, based on the recent 3D structures and improved sequence alignments are reviewed. PMID: 12369922
  11. analysis of human pancreatic lipase from pancreatic juice (BCR693) and a recombinant form (BCR694) PMID: 12667003
  12. examination of tryptophan changes in pancreatic lipase PMID: 14580194
  13. a specific method of measuring classical pancreatic lipase in human serum PMID: 15316225
  14. analysis of a lid hydrophobicity pattern in pancreatic lipase PMID: 16179352
  15. pancreatic lipase-colipase interactions in the presence of bile salt micelles are mediated by Val-407 and Ile-408 of PL PMID: 16431912
  16. Electron paramagnetic resonance spectroscopy along with site-directed spin labeling was used to monitor the conformational changes in the human PL lid in solution to assess the effects of partners of the lipase, i.e. colipase and bile salts. PMID: 17269661
  17. Introducing a negative charge close to the catalytic histidine induced a shift of the pH optimum toward acidic values but strongly reduced the lipase activity. PMID: 18353248
  18. The disulfide bridge between the hinges of the lid kept the secondary structure of the lid intact, whereas the HPL was completely unfolded. PMID: 19113953
  19. Trp-107 and Trp-253 contribute to the change in steady state fluorescence that is triggered by mixed micelles of inhibitor and bile salt. PMID: 19346257

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Involvement in disease
Pancreatic lipase deficiency (PNLIPD)
Subcellular Location
Secreted.
Protein Families
AB hydrolase superfamily, Lipase family
Database Links

HGNC: 9155

OMIM: 246600

KEGG: hsa:5406

STRING: 9606.ENSP00000358223

UniGene: Hs.501135

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