Apolipoproteins have multiple roles. One role is to increase the overall solubility of the lipid particle, helping it to dissolve in the aqueous environment of the blood (apolipoproteins are amphipathic, or detergent-like proteins). Apolipoproteins can also function as enzyme co-factors (receptor ligands), facilitating the transfer of their lipid cargo to specific cells. Thus, the apoliproteins are the smart or working-end of the lipoprotein particle. The apolipoproteins dictate where the particles will dock and where they can bind, and in so doing the apolipoproteins regulate lipid metabolism in the body. So although the particles are composed of phospholipids and have lipid cargo, the few proteins on their surface are what give them their collective name of lipoproteins ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Apolipoproteins have important structural and functional roles in several lipoprotein particles. Apolipoproteins regulate lipid metabolism, adipose tissue, and energy production and serve major...
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Polyclonal antibody for APOA I/APOA1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. APOA I/APOA1 information: Molecular Weight: 30778 MW; Subcellular Localization: Secreted; Tissue Specificity: Major protein of
We have brought together our full range of anti-APO antibodies into one place, making it easier for you to locate exactly what you need.
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Apolipoprotein A-IV is a member of the apo A-I/C-III/A-IV gene cluster. In order to investigate its hypothetical coordinated regulation, an acute phase was induced in pigs by turpentine oil injection. The hepatic expression of the gene cluster as well as the plasma levels of apolipoproteins were monitored at different time periods. Furthermore, the involvement of the inflammatory mediators interleukins 1 and 6 and tumor necrosis factor in the regulation of this gene cluster was tested in cultured pig hepatocytes, incubated with those mediators and apo A-I/C-III/A-IV gene cluster expression at the mRNA level was measured. In response to turpentine oil-induced inflammation, a decreased hepatic apo A-IV mRNA expression was observed (independent of apo A-I and apo C-III mRNA) not correlating with the plasma protein levels. The distribution of plasma apo A-IV experienced a shift from HDL to larger particles. In contrast, the changes in apo A-I and apo C-III mRNA were reflected in their corresponding plasma
In a previous proteomics study using pooled cerebrospinal fluid (CSF) samples, we proposed apolipoprotein AI, apolipoprotein AIV, vitronectin, plasminogen, semaphorin 7A, and ala-β-his-dipeptidase as candidate biomarkers associated with the conversion to clinically definite multiple sclerosis (CDMS) in patients with clinically isolated syndromes (CIS). Here, we aimed to validate these results in individual CSF samples using alternative techniques. In a first replication study, levels of apolipoproteins AI and AIV, vitronectin, and plasminogen were measured by ELISA in CSF and serum of 56 CIS patients (29 patients who converted to CDMS (MS converters) and 27 patients who remained with CIS during follow-up (MS non-converters)) and 26 controls with other neurological disorders. Semaphorin 7A and ala-β-his-dipeptidase levels were determined by selected reaction monitoring (SRM) in CSF of 36 patients (18 MS converters, 18 non-converters) and 20 controls. In a second replication study, apolipoprotein AI
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The RT² qPCR Primer Assay is the most reliable SYBR® Green-based quantitative real-time PCR assay for gene expression analysis. Our experimentally verified design algorithm yields gene-specific qPCR assays characterized by uniform and high PCR efficiencies and standardized amplification conditions. Every RT² Primer Assay is subjected to rigorous experimental verification. Single product amplification of the correct size and high PCR efficiency are guaranteed when using the appropriate RT² qPCR Master Mixes. The uniform PCR amplification efficiencies and PCR conditions of the RT² qPCR Primer Assays provide an accurate and scalable solution for multiple gene expression analyses. Browse Primer Assays By Gene ...
The RT² qPCR Primer Assay is the most reliable SYBR® Green-based quantitative real-time PCR assay for gene expression analysis. Our experimentally verified design algorithm yields gene-specific qPCR assays characterized by uniform and high PCR efficiencies and standardized amplification conditions. Every RT² Primer Assay is subjected to rigorous experimental verification. Single product amplification of the correct size and high PCR efficiency are guaranteed when using the appropriate RT² qPCR Master Mixes. The uniform PCR amplification efficiencies and PCR conditions of the RT² qPCR Primer Assays provide an accurate and scalable solution for multiple gene expression analyses. Browse Primer Assays By Gene ...
Looking for online definition of apoA-IV in the Medical Dictionary? apoA-IV explanation free. What is apoA-IV? Meaning of apoA-IV medical term. What does apoA-IV mean?
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High-density lipoprotein is predominantly composed of the apolipoproteins apoAI and apoAII. These apolipoproteins are responsible for collecting lipids from arteries and transporting them back to the liver for reutilization, which provides protection against cardiovascular diseases. While many studies examine the cardiovascular effects of HDL and its apolipoproteins, few have looked at whether these molecules maintain the health of other bodily systems and organs. In this study, the authors show that apoA1 maintains pulmonary function in mice. Along with inhibiting stressors such as proinflammatory HDL formation and the activity of paranoxonase 1 (PON1) and 3-nitrotyrosine (3NT) in the plasma, apoA1 was shown to limit pulmonary inflammation and oxidative stress markers, such as 3NT, 4-hydroxynonenal adducts (4-HNE), transforming growth factor-β (TGFβ), xanthineoxidase, myeloperoxidase and endothelial nitric oxide synthase in the lung milieu. Additionally, apoA1 was shown to enhance arterial ...
Blog on anti-Apo antibody product: The Apo lpa (Catalog #MBS534186) is an Antibody produced from Goat and is intended for research purposes ...
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|strong|Sheep anti Human Apolipoprotein A1 antibody|/strong| reacts with human apolipoprotein A1 and does not react with other human plasma proteins. In ELISA the following reactivities are observed:|…
Recombinant mammalian apolipoproteins have been expressed in a variety of cultured mammalian cell lines (Reardon et al. 1986; Mallory et al. 1987; Blackhart et al. 1990; Yao et al. 1991), transgenic...
This highly specific human protein microarray specificity validated APOAIV antibody is suitable for use in IHC-P and is guaranteed to work as stated on the product data sheet. | V8552
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APOA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (24-366 a.a.) and having a molecular mass of 41.3kDa.
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To explore the potential of the common marmoset monkey (Callithrix jacchus) as a model for human plasma lipoprotein metabolism, several marmoset apolipoproteins were isolated and characterized in this study. Based on several properties, including molecular weight, amino acid composition, and sequence, the marmoset apolipoproteins are strikingly similar to human apolipoprotein (apo) A-I, A-II, C-III, and A-IV. The first 54 residues of marmoset apo A-I showed 87% sequence identity with the corresponding region of human apo A-I. Amino-terminal sequence analysis of a minor basic apo A-I isoform revealed that it contained an amino-terminal hexapeptide extension (Arg-His-Phe-Gln-Gln-) identical to that found in human proapo A-I. Like apo A-II in most nonhuman primates, marmoset apo-A-II differed from human apo A-II in that it did not contain cysteine and therefore existed as a monomer. The complete amino acid sequence of marmoset apo A-II was deduced. The protein contains 77 amino acids, as does human ...
Site-directed mutagenesis and other molecular biology-based techniques are now available for probing the amphipathic alpha-helix structural motif in the exchangeable apolipoproteins. Here we survey the published literature on lipid-binding and functional domains in apolipoproteins A-I, A-II, A-IV, C-I, C-II, C-III, and E and compare these results with recently developed computer methods for analysis of the location and properties of amphipathic helixes. This comparison suggests that there are at least three distinct classes of amphipathic helixes (classes A, Y, and G*) in the exchangeable apolipoproteins whose distribution varies within and between the seven apolipoproteins. This comparison further suggests that lipid affinity resides largely in class A amphipathic helixes (Segrest, J. P., et al. 1990. Proteins. 8: 103) and that variations in structure and/or numbers of class A domains in individual apolipoproteins allow a range of lipid affinities from high to low. The positions of the four a ...
The expression of the apolipoprotein A-I (apo A-I) gene was investigated in the myelinating sciatic nerve. Hybridization analysis with an apo A-I cDNA probe obtained from a cDNA library of mRNA isolated from rapidly myelinating chick sciatic nerve indicated that apo A-I coding transcripts increase during development in the chick sciatic nerve in parallel with the increase of myelin lamellae. Substantial apo A-I-like immunoreactivity in chick sciatic nerve homogenates was detected by Western blotting. The amount of antigen increased from the 15-d embryonic stage to 1 d posthatch and then decreased. Two subcellular fractions corresponding to the cytoplasmic compartments were particularly enriched in apo A-I. apo A-I immunoreactivity was also found in highly purified myelin preparations. Immunohistochemical staining provided further evidence for the presence of apo A-I in the endoneurial compartment of the sciatic nerve. Electron microscopic examination of these fractions after negative staining ...
Apolipoproteins are proteins that bind lipids (oil-soluble substances such as fat and cholesterol) to form lipoproteins. They transport the lipids through the lymphatic and circulatory systems. The lipid components of lipoproteins are insoluble in water. However, because of their detergent-like (amphipathic) properties, apolipoproteins and other amphipathic molecules (such as phospholipids) can surround the lipids, creating the lipoprotein particle that is itself water-soluble, and can thus be carried through water-based circulation (i.e., blood, lymph). Apolipoproteins also serve as enzyme cofactors, receptor ligands, and lipid transfer carriers that regulate the metabolism of lipoproteins and their uptake in tissues. In lipid transport, apolipoproteins function as structural components of lipoprotein particles, cofactors for enzymes and ligands for cell-surface receptors. In particular, apoA1 is the major protein component of high-density lipoproteins; apoA4 is thought to act primarily in ...
TY - JOUR. T1 - Purification of biologically active apolipoproteins by chromatofocussing. AU - McLeod, Roger. AU - Lacko, Andras G.. AU - Pritchard, P. Haydn. AU - Frohlich, Jiri. PY - 1986/1/1. Y1 - 1986/1/1. N2 - Chromatofocussing has been used to isolate homogeneous apolipoproteins (apo) from human very-low-density lipoproteins and high-density lipoproteins with protein recovery of 70%. The inclusion of sulfhydryl-reducing agent (dithiothreitol) was required during solubilization of the lipoproteins (following delipidation) to achieve reproducible elution profiles. Removal of polyvalent buffers from apoproteins was rapidly accomplished on small columns of hydroxylapatite. The biological activity of purified apo AI and apo CII was confirmed by assessment of their ability to activate lecithin:cholesterol acyltransferase or lipoprotein lipase, respectively. Functional properties of isolated apo E were assessed by in vitro interaction with the low-density lipoprotein receptor expressed by ...
This Human Apo AIV ELISA is used to measure & quantify Apo AIV levels in Metabolism research. Find MSDS or SDS, a COA, data sheets and more information.
Tsao YK, Wei CF, Robberson DL, Gotto AM, Chan L (Dec 1985). Isolation and characterization of the human apolipoprotein A-II gene. Electron microscopic analysis of RNA:DNA hybrids, nucleotide sequence, identification of a polymorphic MspI site, and general structural organization of apolipoprotein genes. The Journal of Biological Chemistry. 260 (28): 15222-31. PMID 2415515 ...
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ProSpecs Apolipoproteins include: Clusterin Human Recombinant, Clusterin Rat Recombinant, Apolipoprotein-D Human Recombinant, Human Apolipoprotein-J, Apolipoprotein-J Canine Recombinant
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The role of HDL and its main protein component the apolipoprotein A-I as being antiatherogenic is well established. Experimental data give support for the involvement of at least three different types of mechanism: (1) the reverse cholesterol transport, (2) anti-inflammatory mechanisms and (3) antit …
References for Abcams Human Apolipoprotein A I peptide (ab66674). Please let us know if you have used this product in your publication
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Approach and Results-We analyzed Lp(a) levels in 532 359 subjects from 2 data sets: (1) in 531 144 subjects from a referral laboratory and (2) in 915 patients from a tertiary referral center. Lp(a) mass levels were measured by immunoturbidometric assays in both centers and expressed as mg/dL. At the referral laboratory, median age (interquartile range) of the subjects was 57.0 (46-67) years, and 51.9% were female. Lp(a) levels were skewed rightward as expected. The mean±SD levels were 34.0±40.0 mg/dL, and median (interquartile range) levels were 17 (7-47) mg/dL, with range 0 to 907 mg/dL. Lp(a) levels at 75%, 80%, 90%, 95%, 99%, and 99.9% percentiles were ,47, ,60, ,90, ,116, ,180, and ,245 mg/dL, respectively. At the referral laboratory, Lp(a) levels ,30 and ,50 mg/dL were present in 35.0% and 24.0% of subjects, respectively, and at the tertiary referral center, 39.5% and 29.2%, respectively. Females had higher mean (SD) (37.0 [42.7] versus 30.7 [36.7]; P,0.0001) and median (interquartile ...
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Apolipoprotein A2 antibody (HRP) (apolipoprotein A-II) for ELISA. Anti-Apolipoprotein A2 pAb (GTX40825) is tested in Human samples. 100% Ab-Assurance.
Polyclonal antibodies raised against a range of seed apolipoproteins from the family Cruciferae have been used for the first time for low resolution epitope characterisation. Antibodies were raised against the major seed apolipoproteins of Brassica napus, Sinapis alba and Raphanus sativum. In each case, the antibodies recognized, in addition to the 19-20 kDa apolipoprotein to which they were raised, similar 19-20 kDa apolipoproteins from a wide range of species in the family Cruciferae, but not in other plant families. Homologous or heterologous two-sites (sandwich) assays were performed with the format [antibody A - test apolipoprotein - antibody B - 2° antibody]. The results showed a drastically reduced antibody B binding by apolipoproteins preincubated with an antibody A. This indicated the presence of a single major epitope on many of the apolipoproteins. The antigenicity of native and denatured apolipoproteins was similar, although the antigenicity of the former was much more readily ...
Apolipoproteins A: Structural proteins of the alpha-lipoproteins (HIGH DENSITY LIPOPROTEINS), including APOLIPOPROTEIN A-I and APOLIPOPROTEIN A-II. They can modulate the activity of LECITHIN CHOLESTEROL ACYLTRANSFERASE. These apolipoproteins are low in atherosclerotic patients. They are either absent or present in extremely low plasma concentration in TANGIER DISEASE.
Apolipoprotein A-II: The second most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. It has a high lipid affinity and is known to displace APOLIPOPROTEIN A-I from HDL particles and generates a stable HDL complex. ApoA-II can modulate the activation of LECITHIN CHOLESTEROL ACYLTRANSFERASE in the presence of APOLIPOPROTEIN A-I, thus affecting HDL metabolism.
Abstract: Enzyme-linked immunosorbent assay (ELISA) has been used formeasuring apolipoproteins A-I and B in the urine. ApoB is absentin urine of healthy subjects, and apoA-I is determined in tracequantity. In patients with chronic glomerulonephritis quantity ofapoA-I in urine was 117 times as much as in control group. ApoBis present in urine of patients in considerable quantity(1528*315 *g/l).) The ELISA method for determining apoA-I andapoB in urine makes it possible to evaluate the gravity ofpathological process in kidney ...
Apolipoproteins are carrier proteins that bind lipids to form water-soluble lipoprotein particles that can be carried through blood and lymph. Several different classes and subclasses of apolipoproteins are known. Apolipoprotein B (ApoB) is the primary apolipoprotein in chylomicrons (lipoprotein particles that contain triglycerides, phospholipids, cholesterol, and proteins) and low-density lipoprotein (LDL). It is also known as FLDB and LDLCQ4. High levels of ApoB can lead to plaques that cause atherosclerosis, and ApoB levels can be a better indicator of heart disease risk than total cholesterol or LDL. The APOB transcript is subject to tissue-specific RNA editing, resulting in two major isoforms, ApoB-100 and ApoB-48.. ...
Human apolipoprotein (apo) A-I is secreted as a proprotein of 249 amino acids and is processed extracellularly to the mature form (243 amino acids) by removal of a six-residue propeptide segment. We have examined the role of the apoA-I propeptide in intracellular transport and secretion using transfected baby hamster kidney cells that secreted either proapoA-I (from the wild-type cDNA, A-Iwt) or mature-form apoA-I (from A-I delta pro, a cDNA in which the propeptide sequence was deleted). Deletion of the propeptide from the apoA-I sequence did not affect the rate of apoA-I synthesis, nor did it affect the fidelity of proteolytic removal of the prepeptide. However, the propeptide deletion caused mature-form apoA-I to accumulate within the cells as determined by pulse-chase experiments; the intracellular retention times for the mature-form apoA-I in which the propeptide was prematurely removed was three times longer than that of proapoA-I (t1/2 , 3 h compared with approximately 50 min). There was ...
Anti-Apolipoprotein A-II Goat pAb Anti-Apolipoprotein A-II, goat polyclonal, recognizes human apolipoprotein A-II. Does not cross-react with other apolipoproteins. It is validated for immunoelectrophoresis and immunoprecipitation. - Find MSDS or SDS, a COA, data sheets and more information.
Apolipoprotein A-I (apo A-I) is the most abundant protein in high-density lipoprotein (HDL) particles, and it plays an important role in HDL metabolism. Both apo A-I and HDL cholesterol (HDL-C) levels are inversely associated with risk of cardiovascular disease. Segregation analyses suggest apo A-I levels are under the control of one or more major loci. Since HDL particles are heterogeneous in their composition and size, genetic influence on its subfractions (i.e., HDL2 and HDL3) could vary. A previous report showed evidence of a major locus controlling HDL3-C levels in a subset of the current study population. Because quantitative trait loci involved in complex diseases are likely to have pleiotropic effects on several related traits, it is possible to have a common major gene involved in regulating apo A-I and HDL3-C levels. We performed a bivariate segregation analysis of apo A-I and HDL3-C levels in 1,006 individuals from 137 families ascertained through probands undergoing elective, diagnostic
Recombinant Human Apolipoprotein A I Full length protein datasheet (ab50239). Abcam offers quality products including antibodies, assays and other reagents.
TY - JOUR. T1 - Genetic control of apolipoprotein A-I distribution among HDL subclasses. AU - Rainwater, David L.. AU - Blangero, John. AU - Moore, Perry H.. AU - Shelledy, Wendy R.. AU - Dyer, Thomas D.. PY - 1995. Y1 - 1995. N2 - We conducted genetic analyses to determine the components of variation for size distributions of apolipoprotein (apo) A-I among human plasma lipoproteins resolved on the basis of size. Analyses used data for 717 individuals in 26 pedigrees. Apo A-I distributions among lipoprotein size classes were measured by nondenaturing gradient gel electrophoresis (GGE) and immunoblotting procedures. Curves were fitted to apo A-I absorbance profiles to estimate fractional absorbance in each of five high-density lipoprotein (HDL) subclasses. Multivariate regression analyses revealed several covariates (sex, age, diabetes, and apo A-I concentrations) that were significantly associated with variation in one or more HDL subclasses. Female gender and elevated apo A-I concentrations ...
We hypothesized that impaired protection of HDL against apoB-containing lipoprotein oxidation in the 11.1 transgenic mouse model could play a role in its enhanced atherosclerosis susceptibility. This line of human apoA-II in transgenic mice presented a relative increase in the area stained with antibodies that recognize LDL oxidation epitopes compared with control or 25.3 mice. However, a concomitant increase in plasma markers of oxidative stress was not found, which suggests that the level of oxidation of plasma lipoproteins was similar in the three mouse lines studied. Thus, the main difference in oxidation susceptibility may occur in the subendothelial space. In this milieu, the antioxidant and anti-inflammatory properties of HDL may confer vital protection.38. Lipoproteins that undergo oxidation are known to increase their electrophoretic mobility. This property can be used to establish the degree of LDL oxidation and has been used previously to assess HDL protectivity.39 Using this ...
Apo-A1 is a 29.0 kDa protein produced in the liver and intestine, and secreted as the predominant constituent of nascent high-density lipoprotein (HDL) particle. Apo-A1, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol. This Apo- 1 ability enables HDL to remove excess peripheral cholesterol and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is though to inhibit atherogenesis. For this reason HDL is also known as the good cholesterol. The therapeutic potential of Apo-A1 has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of Apo-A1 (called Apo-A1 Milano). The availability of recombinant normal Apo-A1 should facilitate further investigation into the potential usefulness of apoA-I in preventing atherosclerotic vascular diseases. Recombinant human Apo-A1 is a 28.2 kDa protein of 244 amino acid residues ...
PubMed journal article: Associations among apolipoproteins, oxidized high-density lipoprotein and cardiovascular events in patients on hemodialysis. Download Prime PubMed App to iPhone, iPad, or Android
Buy our Natural Human Apolipoprotein CI. Ab77901 is a full length protein produced in Nativesyntheticaly and has been validated in SDS-PAGE. Abcam provides…
Principal Investigator:MATSUBARA Etsuro, Project Period (FY):2002 - 2003, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Neurology
Apolipoproteins AI/B/E gene polymorphism and their plasma levels in patients with coronary artery disease in a tertiary care-center of Eastern India ...
ABCA1 expression and co-localization with [1-93]ApoA-I and ApoA-I. (A) Western blot analysis with anti-ABCA1 antibodies of cell lysates prepared from HepG2 ce
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