Recombinant Human PLTP Protein

Beta LifeScience SKU/CAT #: BLA-7136P

Recombinant Human PLTP Protein

Beta LifeScience SKU/CAT #: BLA-7136P
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Product Overview

Host Species Human
Accession P55058
Synonym BPI fold containing family E BPIFE HDLCQ9 High density lipoprotein cholesterol level quantitative trait locus 9, included Lipid transfer protein II OD107 Phospholipid transfer protein Plasma phospholipid transfer protein Pltp PLTP_HUMAN
Description Recombinant Human PLTP Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
AA Sequence FPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGHFYYNISEV KVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFLKVYDFLST FITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLM KDPVASTSNLDMDFRGAFFPLTERNWSLPNRAVEPQLQEEERMVYVAFSE FFFDSAMESYFRAGALQLLLVGDKVPHDLDMLLRATYFGSIVLLSPAVID SPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQPEVQLSSMTMD ARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLRE VIEKNRPADVRASTAPTPSTAAV
Molecular Weight 72 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Mediates the transfer of phospholipids and free cholesterol from triglyceride-rich lipoproteins (low density lipoproteins or LDL and very low density lipoproteins or VLDL) into high-density lipoproteins (HDL) as well as the exchange of phospholipids between triglyceride-rich lipoproteins themselves. Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Plays an important role in HDL remodeling which involves modulating the size and composition of HDL. Also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer phosphatidylcholine from phospholipid vesicles to HDL, and an inactive form that lacks this capability.
Subcellular Location Secreted. Nucleus.
Protein Families BPI/LBP/Plunc superfamily, BPI/LBP family
Database References
Tissue Specificity Widely expressed. Highest level of expression in the ovary, thymus and placenta, with moderate levels found in the pancreas, small intestine, testis, lung and prostrate. Low level expression in the kidney, liver and spleen, with very low levels found in t

Gene Functions References

  1. Study demonstrated that PLTP is overexpressed in synovial tissue of patients with chronic inflammatory rheumatisms, such as rheumatoid arthritis (RA), when compared to osteoarthritis patients (OA); and that RA but not OA patients displayed elevated levels of PLTP activity in synovial fluid, which were correlated with pro-inflammatory cytokine levels. PMID: 29565987
  2. These results indicate that PLTP and MASP-1 can serve as plasma biomarkers for the early diagnosis and treatment of Age-related macular degeneration , which is critical for preventing Age-related macular degeneration -related blindness. PMID: 27605007
  3. PLTP activity did not affect this metric. Thus, deviations in PLTP activity from the wild-type level reduce HDL mass and ex vivo cholesterol efflux capacity, but not the rate of macrophage cholesterol efflux to plasma or in vivo mRCT. PMID: 28137768
  4. serum CETP and PLTP activity in patients diagnosed with hypothyroidism, was examined. PMID: 27899788
  5. PLTP may regulate cigarette smoke extract-induced IL-8 expression via the ERK1/2 signaling pathway in human pulmonary epithelial cells PMID: 27596005
  6. LPL and PLTP appear to be novel glioma-associated proteins and play a role in the progression of human glioma PMID: 27864281
  7. association of PON-1 activity with PLTP activity was lost in analysis which included large HDL particles PMID: 26656640
  8. a novel association between PLTPa and PON1 activity PMID: 26009633
  9. The domain of apolipoprotein E4 required for PLTP activation resides within its amino-terminal 1-185 region. PMID: 26337529
  10. Elevated baseline plasma levels of PLTP are associated with an increased risk of long-term all-cause mortality in patients with diabetes and known or suspected coronary disease. PMID: 25710294
  11. This review summarizes the recent progresses made in the PLTP research field and focuses on the complexity of the implication of PLTP in obesity, insulin resistance and type 2 diabetes mellitus. [review] PMID: 25107452
  12. Elevated plasma PLTP activity may predict an increased risk of T2DM in men PMID: 25304745
  13. High systemic PLTP expression does not contribute significantly to a renal phenotype despite being implicated in systemic atherosclerosis in ApoE deficient mice. PMID: 25651711
  14. proteolytic cleavage of PLTP by cathepsin G may enhance the injurious inflammatory responses that occur in COPD PMID: 24532668
  15. PLTP is actively involved in lipid transfer, cholesterol efflux, HDL genesis, and remodeling at the blood-brain barrier. PMID: 24369175
  16. Lower plasma CETP or higher PLTP activity was each associated with a significantly increased risk of cardiovascular disease. PMID: 23477743
  17. Higher PLTP activity is associated with depressed LV systolic function in a dose-dependent manner. PMID: 23545183
  18. In all the models with ApoE deficiency, elevated human PLTP expression causes higher levels of diet-induced atherosclerosis coinciding with decreased plasma levels of HDL cholesterol. PMID: 23313246
  19. The physiological relevance of PLTP in intracellular lipid metabolism and signal transduction. [Review] PMID: 21736953
  20. PLTP mediates PL transfer and participates in reverse cholesterol transport pathways at the fetoplacental barrier. PMID: 22492872
  21. we provide evidences that induction of TGF-B1 production and Smad3 phosphorylation by Ox-LDL is mediated by Ras/ERK/PLTP pathway in human alveolar epithelial cells. PMID: 22034170
  22. diabetes-environment and diabetes-gene interactions govern plasma PLTP activity PMID: 21973210
  23. Pltp expression is increased in GDM with hyperglycemia and/or hyperinsulinemia contributing. High PLTP activity in fetal serum may enhance conversion of HDL into cholesterol-accepting particles, thereby increasing maternal-fetal cholesterol transfer. PMID: 22090281
  24. PLTP activity could contribute to elevated cardiovascular risk in the presence of obesity and insulin resistance PMID: 21481395
  25. PLTP has anti-inflammatory capabilities in macrophages. PMID: 21782857
  26. Increased PLTP activity in human tear fluid in dry eye syndrome patients suggests an ocular surface protective role for this lipid transfer protein. PMID: 21514421
  27. Data show that the removal of the carbohydrate chains had a quantitative impact on cellular secretion of PLTP and its phospholipid transfer activity. PMID: 21515415
  28. data show the existence of small inactive plasma PLTP complexes, and show that variation in the amount of the two clusters of inactive PLTP complexes and specific activity of active PLTP contribute to the variation in plasma PLTP specific activity. PMID: 21303701
  29. the SR-BI pathway contributes in unique ways to cholesterol metabolism and atherosclerosis susceptibility even in the presence of CETP PMID: 21454568
  30. Human PLTP expression in transgenic rabbits worsens atherosclerosis as a result of increased levels of atherogenic apoB-containing lipoproteins. PMID: 21252068
  31. CETP and PLTP activities were negatively related with the ratio of HDL-C/LDL-C. PMID: 20937151
  32. a dual role for PLTP in human tear fluid PMID: 20724654
  33. Our results indicate that there is no genetic association between PLTP and Alzheimer's disease PMID: 20714154
  34. PLTP was overexpressed in the ER-negative breast cancer group. PMID: 20805453
  35. Data show that biglycan (BGN) induces of phospholipid transfer protein (PLTP) in aortic valve interstitial cells via stimulation of Toll-like receptor 2, so increased BGN in stenotic valves contributes to the production of PLTP via TLR 2. PMID: 20382708
  36. A gene score based on 2 PLTP single nucleotide polymorphisms is associated with lower PLTP transcription and activity, an increased number of HDL particles, smaller HDL size, and decreased risk of cardiovascular disease PMID: 20644014
  37. apoA-I enhances the phospholipid transfer activity of PLTP secreted from macrophage foam cells without affecting the PLTP mass. PMID: 20534134
  38. PLTP was found to mediate transfer of anionic phospholipids to HDL/LDL lipoproteins thereby neutralizing the effect of procoagulant liposomes, resulting in a reduction of procoagulant activity. PMID: 20088939
  39. PLTP activity is strongly influenced by PLTP region polymorphisms and metabolic factors. PMID: 19965587
  40. serum PLTP is involved in the clearance of postprandial lipoproteins and this process is attenuated in diabetes. PMID: 20108050
  41. PLTP activity may represent a novel marker of left ventricular systolic dysfunction in patients with known or suspected coronary artery disease. PMID: 19446293
  42. Human PLTP expressed in plasma from transgenic mice contributes to the formation of pre beta-HDL, whereas the expression of human cholesterol ester transfer protein does not affect this process. PMID: 11716766
  43. This protein and pre-beta-high density lipoprotein are degraded by mast cell chymase, the high affinity efflux of cholesterol from macrophage foam cells is impaired. PMID: 12531890
  44. The phospholipid transfer protein gene is a liver X receptor target expressed by macrophages in atherosclerotic lesions. PMID: 12612088
  45. Elevation of PLTP activity results in rapid disposal of cholesterol from the body via increased conversion into bile acids and subsequent excretion. PMID: 12649089
  46. PLTP is expressed by macrophages, is regulated by cholesterol loading, and is present in atherosclerotic lesions PMID: 12730304
  47. elevated PLTP activity in hypertriglyceridemia is related to insulin resistance and not to increased PLTP mass PMID: 12754275
  48. HepG2-derived PLTP resembles in several aspects the high-activity form of PLTP found in human plasma PMID: 12810820
  49. PLTP is present in human atherosclerotic lesions, and its distribution suggests roles for PLTP in both cellular cholesterol metabolism and lipoprotein retention on extracellular matrix PMID: 12835223
  50. seminal PLTP concentrations represented 25% of the concentration measured in blood plasma; seminal PLTP activity was partially associated with prostasomes; higher PLTP activity was measured in seminal plasma samples with low seminal vesicle secretions PMID: 12837922

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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.

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