35% in DPBS
cell culture | mammalian: suitable
Albumins and Transport Proteins
Palmitic acid-modified bovine serum albumin (PAB) was synthetized and found to own remarkable scavenger receptor-A (SR-A) targeting ability in vitro and in vivo, through which activated macrophages took up PAB nanoparticles (PAB NPs) 9.10 times more than bovine serum albumin nanoparticles (BSA NPs) and PAB NPs could delivery anti-inflammatory drugs celastrol (CLT) to inflamed tissues more effectively than BSA NPs. Compared with chondroitin sulfate modified BSA NPs targeting activated macrophages via CD44, PAB NPs show a more prominent targeting effect whether in vivo or in vitro. And PAB also demonstrated excellent biosafety compared to maleylated BSA, a known SR-A ligand that was lethal in our study.
Furthermore, in adjuvant-induced arthritis rats, CLT-PAB NPs significantly improved disease pathology at a lower CLT dose with high safety, compared with CLT-BSA NPs. In addition, compared with the existing ligands with SR-A targeting due to strong electronegativity, the enhanced electronegativity and introduced PA are both important for the SR-A targeting effect of PAB. Therefore, PAB provides a novel direction for the treatment of rheumatoid arthritis and design of new ligands of SR-A.
More On- www.store.genprice.com
Albumin-based Stationary Phases
BSA and HSA are closely related proteins and, consequently, the chromatographic properties of the chiral stationary phases based on these proteins are similar. Sometimes the elution order is reversed between chiral stationary phases based on these proteins; on the HSA-based phases (S)-warfarin elutes before (R)-warfarin, whereas on the BSA-based phases the opposite elution order is observed.
A variety of weakly acidic and neutral compounds are resolved on chiral stationary phases based on BSA and HSA. 2-Arylpropionic acid derivatives such as naproxen, flurbiprofen, ibuprofen, ketoprofen and fenoprofen, reduced folates such as leucovorin and 5-methyltetrahydrofolate, and benzodiazepines such as oxazepam, lorazepam and temazepam are separated. Figure 4 shows enantioseparations of leucovorin, lorazepam hemisuccinate and N-benzoyl-phenylalanine on an HSA-based column. However, cationic compounds are not resolved on BSA and HSA phases. The structure-binding relationship for benzodiazepines using HSA stationary phases reveals that the binding of benzodiazepines occurs at a site that contains both a hydrophobic pocket and an area of cationic charge, and that the chiral recognition occurs in this binding site.
Enantioselectivity of stationary phases based on BSA produced with isolated protein fragments has been investigated. The BSA fragment following peptic digest of BSA has molecular weights of about 35 kDa which is an N-terminal half of amino acid residues 1–307. The BSA fragment phases give longer retentions for benzoin and benzodiazepines, and higher enantioselectivity for lorazepam, benzoin and fenoprofen because of a higher density of chiral recognition site(s), compared with native BSA phases.
shows chromatograms of lorazepam enantiomers on BSA and BSA fragment-based columns. However, it is plausible that the conformation of the BSA fragment might be different from that of the native BSA.
Acrosome reaction induced by neoglycoproteins containing Man and GlcNAc
Several BSA-based ‘neoglycoproteins’ were shown to stimulate the acrosome reaction. The binding of Man,Flu-BSA results in a time-dependent receptor aggregation and the induction of acrosome exocytosis in capacitated sperm populations from fertile donors.200 N-acetyl-α-glucosamine (α-GlcNAc) and α-mannose (αMan-BSA) may interact with the putative receptor for one protein of zona pellucida: ZP3 in human spermatozoa.195,202–205 This binding results in the exocytosis of the sperm acrosome (AR).206 The GlcNAc-BSA-induced acrosome reaction is inhibited by a small ligand: N-acetylglucosamine (GlcNAc) and by a purified soluble hydrolase, β-N-acetylglucosaminidase. The induction of the AR with Man-BSA was inhibited by mannose, while soluble α-mannosidase was only partially effective. These data suggest that binding sites for GlcNAc and Man seem to be involved in the induction of the AR in human sperm. The induction of AR in human spermatozoa by GlcNAc-BSA could be used to predict their fertilizing ability in vitro.205
The induction of the acrosome reaction by GlcNAc-BSA and Man-BSA has been shown to involve voltage-dependent Ca2+ channels and a Gi-like guanine regulatory protein.203,207 The GlcNAc-BSA- or Man-BSA-induced AR was completely inhibited by preincubation of spermatozoa with calcium antagonists, indicating a link between the binding of sugar residues of the neoglycoproteins and channel activation. The pretreatment of spermatozoa with Pertussis toxin (PTx) inhibits GlcNAc-BSA- or Man-BSA-induced AR, whereas cholera toxin has no effect. Therefore, the transduction mechanism for GlcNAc-BSA- and Man-BSA-induced AR involves G-proteins of the inhibitory type (GI).204
The effect of ‘peritoneal fluid’ on the human sperm acrosome reaction (AR) was tested.208 When the AR was induced by GlcNAc-BSA, pre-incubation with peritoneal fluid reduced (60%) the percentage of AR, while peritoneal fluid from either the endometriosis group or infertile patients without endometriosis caused no significant differences. These data indicated that peritoneal fluid possesses a protective factor which prevents premature AR.
Cell Loading and Sedimentation
The BSA solutions will be transferred into the gradient maker apparatus. This is assembled as in Fig. 12.2 and a linear gradient will be generated from 250 mL of 2% BSA and 250 mL of 4% BSA solutions in the appropriate cell buffer chambers. Next, 50 mL of BSA will be loaded into the loading chamber. A cell suspension will be loaded and the stirrer will start to move under the tube, which makes it possible for the cells to flow through into the sedimentation chamber in about 5–7 min. The gradient valve between the two chambers will be opened to allow the two BSA solutions to mix, and then the release valve will be opened, thus allowing the BSA to flow into the syringe to generate the gradient. After 2.5 h at room temperature, cells will be collected in 12 mL fractions and eluted dropwise into 45 test tubes. Fractions will be placed on ice immediately after collection.
|31C-CH0114||Fitzgerald||50 mg||159.6 EUR|
|Testosterone 3 BSA Protein (BSA)|
|abx060856-1mg||Abbexa||1 mg||693.6 EUR|
|BSA Control for Age-BSA|
|BSA Control for AGE-BSA|
|35R-AA007||Fitzgerald||10 mg||268.8 EUR|
|abx080017-1mg||Abbexa||1 mg||510 EUR|
|abx083009-50ug||Abbexa||50 ug||460.8 EUR|
|DAG3015||Creative Diagnostics||1 mg||858 EUR|
|DAG406||Creative Diagnostics||1mg||858 EUR|
|DAGA-005B||Creative Diagnostics||1mg||1326 EUR|
|DAGA-006B||Creative Diagnostics||1mg||1076.4 EUR|
|DAGA-007B||Creative Diagnostics||1mg||1076.4 EUR|
|DAGA-008B||Creative Diagnostics||1mg||936 EUR|
|abx080012-1mg||Abbexa||1 mg||444 EUR|
|abx080038-1mg||Abbexa||1 mg||844.8 EUR|
|DAGPY6646||Creative Diagnostics||500ug||1014 EUR|
|ACT00301-50||Arthus||50µg (20µg)||289.2 EUR|
|abx080050-1mg||Abbexa||1 mg||543.6 EUR|
|DAGA-075B||Creative Diagnostics||1mg||1014 EUR|
|DAG3197||Creative Diagnostics||1mg||577.2 EUR|
|abx080052-1mg||Abbexa||1 mg||543.6 EUR|
|DAG3043||Creative Diagnostics||0.5ml||858 EUR|
|DAG3313||Creative Diagnostics||250ug||858 EUR|
|DAG3314||Creative Diagnostics||250ug||936 EUR|
|DAGA-047B||Creative Diagnostics||1mg||1014 EUR|
|DAGA-368B||Creative Diagnostics||1mg||1076.4 EUR|
|IM112||Cygnus Technologies||1 ml||342 EUR|
|70C-CR1016GAP||Fitzgerald||1 mg||516 EUR|
|70R-12462||Fitzgerald||100 ug||552 EUR|
|70-BC67||Fitzgerald||1 mg||229.2 EUR|
|10-1911||Fitzgerald||200 ul||651.6 EUR|
|10R-A139B||Fitzgerald||500 µg||925.2 EUR|
|10R-1795||Fitzgerald||100 ul||522 EUR|
|10R-10573||Fitzgerald||100 ul||418.8 EUR|
|70R-AS001||Fitzgerald||500 ug||236.4 EUR|
|20R-AR042||Fitzgerald||20 mg||392.4 EUR|
|20R-1871||Fitzgerald||100 ug||807.6 EUR|
|abx080008-1mg||Abbexa||1 mg||1345.2 EUR|