Recombinant Human CLPS/Colipase Protein

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Leader in Biomolecular Solutions for Life Science Recombinant Human CLPS/Colipase Protein Catalog No.: RP00125 Recombinant Sequence Information Background Species Gene ID Swiss Prot The protein is a cofactor needed by pancreatic lipase for efficient dietary lipid Human 1208 P04118 hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilizing an active conformation and considerably increasing the overall Tags hydrophobic binding site. The gene product allows lipase to anchor noncovalently C-6×His to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. This cofactor is only expressed in pancreatic acinar cells, Synonyms suggesting regulation of expression by tissue-specific elements. Three transcript variants encoding different isoforms have been found for this gene. Basic Information Product Information Description Recombinant Human CLPS/Colipase Protein is produced by HEK293 expression Source Purification system. The target protein is expressed with sequence (Met1-Gln112) of human HEK293 cells > 90% by SDS- CLPS/Colipase (Accession #NP_001823.1) fused with a 6×His tag at the C-terminus. PAGE. Bio-Activity Endotoxin < 0.1 EU/μg of the protein by LAL Storage method. Store the lyophilized protein at -20°C to -80 °C for long term. After reconstitution, the protein solution is stable at -20 °C for 3 months, at 2-8 °C Formulation for up to 1 week. Lyophilized from a 0.22 μm filtered Avoid repeated freeze/thaw cycles. solution of PBS, pH 7.4.Contact us for customized product form or formulation. Reconstitution Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Contact www.abclonal.com Validation Data Recombinant Human CLPS/Colipase Protein was determined by SDS-PAGE with Coomassie Blue, showing a band at 13 kDa. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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Rat CLPS / Colipase Protein (His Tag)
Rat CLPS / Colipase Protein (His Tag) Catalog Number: 80729-R08H General Information SDS-PAGE: Gene Name Synonym: CLPS Protein Construction: A DNA sequence encoding the rat Clps (NP_037271.1) (Met1-Gln112) was expressed with a polyhistidine tag at the C-terminus. Source: Rat Expression Host: HEK293 Cells QC Testing Purity: > 95 % as determined by SDS-PAGE. Endotoxin: Protein Description < 1.0 EU per μg protein as determined by the LAL method. Colipase belongs to the colipase family. Structural studies of the complex Stability: and of colipase alone have revealed the functionality of its architecture. It is a small protein with five conserved disulphide bonds. Structural analogies Samples are stable for up to twelve months from date of receipt at -70 ℃ have been recognised between a developmental protein, the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the Predicted N terminal: Ala 18 C-terminal domain of alpha-toxin. Colipase can only be detected in Molecular Mass: pancreatic acinar cells, suggesting regulation of expression by tissue- specific elements. Colipase allows lipase to anchor noncovalently to the The recombinant rat Clps consists 106 amino acids and predicts a surface of lipid micelles, counteracting the destabilizing influence of molecular mass of 11.9 kDa. intestinal bile salts. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Colipase is a cofactor needed Formulation: by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C- terminal, non-catalytic domain of lipase, thereby stabilising as active Lyophilized from sterile PBS, pH 7.4.
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Biochemical Properties of Pancreatic Colipase from the Common Stingray
Ben Bacha et al. Lipids in Health and Disease 2011, 10:69 http://www.lipidworld.com/content/10/1/69 RESEARCH Open Access Biochemical properties of pancreatic colipase from the common stingray Dasyatis pastinaca Abir Ben Bacha†, Aida Karray†, Lobna Daoud, Emna Bouchaala, Madiha Bou Ali, Youssef Gargouri and Yassine Ben Ali* Background: Pancreatic colipase is a required co-factor for pancreatic lipase, being necessary for its activity during hydrolysis of dietary triglycerides in the presence of bile salts. In the intestine, colipase is cleaved from a precursor molecule, procolipase, through the action of trypsin. This cleavage yields a peptide called enterostatin knoswn, being produced in equimolar proportions to colipase. Results: In this study, colipase from the common stingray Dasyatis pastinaca (CoSPL) was purified to homogeneity. The purified colipase is not glycosylated and has an apparent molecular mass of around 10 kDa. The NH2-terminal sequencing of purified CoSPL exhibits more than 55% identity with those of mammalian, bird or marine colipases. CoSPL was found to be less effective activator of bird and mammal pancreatic lipases than for the lipase from the same specie. The apparent dissociation constant (Kd) of the colipase/lipase complex and the apparent Vmax of the colipase-activated lipase values were deduced from the linear curves of the Scatchard plots. We concluded that Stingray Pancreatic Lipase (SPL) has higher ability to interact with colipase from the same species than with the mammal or bird ones. Conclusion: The fact that colipase is a universal lipase cofactor might thus be explained by a conservation of the colipase-lipase interaction site.
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Polymorphisms in PNLIP, Encoding Pancreatic Lipase, and Associations with Metabolic Traits
J Hum Genet (2001) 46:320–324 © Jpn Soc Hum Genet and Springer-Verlag 2001 ORIGINAL ARTICLE Robert A. Hegele · D. Dan Ramdath · Matthew R. Ban Michael N. Carruthers · Christine V. Carrington Henian Cao Polymorphisms in PNLIP, encoding pancreatic lipase, and associations with metabolic traits Received: January 18, 2001 / Accepted: February 19, 2001 Abstract Pancreatic lipase (EC 3.1.1.3) is an exocrine se- Introduction cretion that hydrolyzes dietary triglycerides in the small intestine. We developed genomic amplification primers to sequence the 13 exons of PNLIP, which encodes pancreatic Pancreatic lipase (PL; EC 3.1.1.3), a 56-kD protein, is in- lipase, in order to screen for possible mutations in cell lines volved in the intestinal hydrolysis of dietary triglyceride to of four children with pancreatic lipase deficiency (OMIM fatty acids. PL deficiency (OMIM 246600) is associated with 246600). We found no missense or nonsense mutations in malabsorption of long-chain triglyceride fatty acids, failure these samples, but we found three silent single-nucleotide to thrive in infancy and childhood, and absence of PL secre- polymorphisms (SNPs), namely, 96A/C in exon 3, 486C/T in tion upon secretin stimulation (Sheldon 1964; Rey et al. exon 6, and 1359C/T in exon 13. In 50 normolipidemic 1966). PNLIP on chromosome 10q26.1 (Davis et al. 1991) is Caucasians, the PNLIP 96C and 486T alleles had frequen- a 13-exon gene that spans more than 20kb (Sims et al. 1993) cies of 0.083 and 0.150, respectively. The PNLIP 1359T and encodes the 465-amino acid PL mature protein (Lowe allele was absent from Caucasian, Chinese, South Asian, et al.
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Human CLPS / Colipase Protein (His Tag)
Human CLPS / Colipase Protein (His Tag) Catalog Number: 13631-H08B General Information SDS-PAGE: Gene Name Synonym: CLPS Protein Construction: A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus. Source: Human Expression Host: Baculovirus-Insect Cells QC Testing Purity: > 90 % as determined by SDS-PAGE Endotoxin: Protein Description < 1.0 EU per μg of the protein as determined by the LAL method Colipase belongs to the colipase family. Structural studies of the complex Stability: and of colipase alone have revealed the functionality of its architecture. It is a small protein with five conserved disulphide bonds. Structural analogies ℃ Samples are stable for up to twelve months from date of receipt at -70 have been recognised between a developmental protein, the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the Ala 18 Predicted N terminal: C-terminal domain of alpha-toxin. Colipase can only be detected in Molecular Mass: pancreatic acinar cells, suggesting regulation of expression by tissue- specific elements. Colipase allows lipase to anchor noncovalently to the The recombinant human CLPS consists of 105 amino acids and predicts a surface of lipid micelles, counteracting the destabilizing influence of molecular mass of 11.5 kDa. It migrates as an approximately 12 KDa band in intestinal bile salts. Without colipase the enzyme is washed off by bile salts, SDS-PAGE under reducing conditions. which have an inhibitory effect on the lipase. Colipase is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C- Formulation: terminal, non-catalytic domain of lipase, thereby stabilising as active conformation and considerably increasing the overall hydrophobic binding Lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly site.
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Quantitative Trait Loci Influencing Cholesterol and Phospholipid
Quantitative trait loci influencing cholesterol and phospholipid phenotypes map to chromosomes that contain genes regulating blood pressure in the spontaneously hypertensive rat. A Bottger, … , T W Kurtz, M Pravenec J Clin Invest. 1996;98(3):856-862. https://doi.org/10.1172/JCI118858. Research Article The frequent coincidence of hypertension and dyslipidemia suggests that related genetic factors might underlie these common risk factors for cardiovascular disease. To investigate whether quantitative trait loci (QTLs) regulating lipid levels map to chromosomes known to contain genes regulating blood pressure, we used a genome scanning approach to map QTLs influencing cholesterol and phospholipid phenotypes in a large set of recombinant inbred strains and in congenic strains derived from the spontaneously hypertensive rat and normotensive Brown-Norway (BN.Lx) rat fed normal and high cholesterol diets. QTLs regulating lipid phenotypes were mapped by scanning the genome with 534 genetic markers. A significant relationship (P < 0.00006) was found between basal HDL2 cholesterol levels and the D19Mit2 marker on chromosome 19. Analysis of congenic strains of spontaneously hypertensive rat indicated that QTLs regulating postdietary lipid phenotypes exist also on chromosomes 8 and 20. Previous studies in the recombinant inbred and congenic strains have demonstrated the presence of blood pressure regulatory genes in corresponding segments of chromosomes 8, 19, and 20. These findings provide support for the hypothesis that blood pressure and certain lipid subfractions can be modulated by linked genes or perhaps even the same genes. Find the latest version: https://jci.me/118858/pdf Quantitative Trait Loci Inﬂuencing Cholesterol and Phospholipid Phenotypes Map to Chromosomes That Contain Genes Regulating Blood Pressure in the Spontaneously Hypertensive Rat Anita Bottger,* Hein A.
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Uniprot ID Title Mass 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18
Pancreatic duct fluidpy composite proteome p biomarkers Duct fluid numbers UniProt ID Title Mass 123456789101112131415161718192021222324252627 ALBU_HUMAN Serum albumin 71317 4.34 5.54 7.87 6.24 3.14 6.62 7.87 7.87 8.82 6.62 5.89 9.33 7.87 7.87 7.02 2.06 4.34 3.14 1.14 2.56 5.89 7.87 8.82 7.87 7.87 5.54 TRFE_HUMAN Serotransferrin 79280 0.44 2.44 3.95 3.52 0.15 1.86 3.12 5.51 6.82 2.44 0.81 3.52 3.95 3.52 5.82 1.08 0.73 1.08 0.26 0.98 1.38 5.82 3.12 5.22 3.95 1.99 APOA1_HUMAN Apolipoprotein A-I 30759 0.12 3.51 1 4.07 3.51 6.18 5.39 1.53 1 0.59 4.07 7.06 0.26 0.26 1 1 1.53 3.02 2.58 0.59 A1AT_HUMAN Alpha-1-antitrypsin 46878 0.26 1 1.93 1.16 0.17 1.33 1.93 2.69 5.82 1.71 2.69 2.42 2.69 3.3 1.51 2.16 1.71 0.47 0.17 0.59 1.71 0.36 2.16 1 1.71 1.16 1 TTHY_HUMAN Transthyretin 15991 0.24 0.24 1.39 0.24 0.24 APOA2_HUMAN Apolipoprotein A-II 11282 0.83 0.35 0.83 0.35 0.83 1.47 0.35 0.35 1.47 0.35 A1AG1_HUMAN Alpha-1-acid glycoprotein 1 23725 0.81 2.29 0.56 0.56 1.44 1.11 1.84 2.29 1.84 1.44 1.44 1.84 0.56 1.44 0.16 1.44 1.44 0.81 1.11 0.35 1.11 A1AG2_HUMAN Alpha-1-acid glycoprotein 2 23873 0.56 0.81 0.81 0.56 0.56 0.81 0.35 1.1 0.56 1.1 0.81 ZA2G_HUMAN Zinc-alpha-2-glycoprotein 34465 0.23 0.23 0.11 0.11 0.23 0.87 0.37 0.68 0.23 0.23 IC1_HUMAN Plasma protease C1 inhibitor 55347 0.58 0.58 0.58 0.8 0.48 0.92 0.48 0.58 0.48 0.48 0.92 0.8 0.48 0.58 0.07 0.68 0.38 0.07 A2MG_HUMAN Alpha-2-macroglobulin 164614 0.3 1.53 0.86 0.25 0.36 2.09 0.09 0.94 0.74 2.09 0.82 1.65 2.61 0.22 0.02 0.22 0.28 1.42 0.36 1.37 0.82 0.42 CERU_HUMAN Ceruloplasmin 122983 0.03 0.51
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Principles of Physiology of Lipid Digestion
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