Provided herein are new compositions and methods to target and deliver agents to pathological areas by utilizing multifunctional compounds. These compounds include three or more domains: (i) a vimentin-binding peptide, (ii) a linker, and (iii) a drug binding, a capturing reagent, or a detectable moiety. These compounds can be used to detect, isolate, and/or treat cancerous cells such as circulating tumor cells.

Provided herein are new compositions and methods to target and deliver agents to pathological areas by utilizing multifunctional compounds. These compounds include three or more domains: (i) a vimentin-binding peptide, (ii) a linker, and (iii) a drug binding, a capturing reagent, or a detectable moiety. These compounds can be used to detect, isolate, and/or treat cancerous cells such as circulating tumor cells.

Membranes having an average pore size of 5 nm to 5,000 nm and a porosity of 15% or more, said membrane being obtainable by a process comprising curing a composition comprising: 5 to 64 wt % of (i) a cross-linking agent comprising at least one cationic group; and 36 to 95 wt % of (ii) inert solvent(s).

The membranes are useful for detecting, filtering and/or purifying biomolecules.

The present invention relates to a method for separating a mature von Willebrand Factor (mat-VWF) from von Willebrand Factor pro-peptide (VWF-PP) by incubating a composition comprising inducing dissociation of mat-VWF and VWF-PP by disruption of the non-covalently associated mat-VWF and VWF-PP, wherein said dissociation is induced by: (i) addition of at least one chelating agent, or (ii) increasing the pH to a pH of at least 7, and then collecting said mat-VWF to obtain a high purity, propeptide depleted mature VWF (mat-VWF).

The present invention relates to a method for separating a mature von Willebrand Factor (mat-VWF) from von Willebrand Factor pro-peptide (VWF-PP) by incubating a composition comprising inducing dissociation of mat-VWF and VWF-PP by disruption of the non-covalently associated mat-VWF and VWF-PP, wherein said dissociation is induced by: (i) addition of at least one chelating agent, or (ii) increasing the pH to a pH of at least 7, and then collecting said mat-VWF to obtain a high purity, propeptide depleted mature VWF (mat-VWF).

A method of separating free target analyte from protein-bound target analyte is described. Such can include obtaining an aqueous sample containing a target analyte in a free form (free target analyte) and the target analyte in a protein-bound form (protein-bound target analyte), passing the aqueous sample through a size exclusion chromatography matrix with a molecular weight cut off sufficient to allow the free target analyte to permeate into pores of the size exclusion chromatography matrix and exclude the protein-bound target analyte, whereupon the free target analyte adheres to and is immobilized by the size exclusion chromatography matrix and the protein-bound target analyte does not adhere to by the size exclusion chromatography matrix, separating the free target analyte from the protein-bound analyte by removing the protein-bound target analyte from the size exclusion chromatography matrix, and eluting the free target analyte from the size exclusion chromatography matrix with an organic solvent.

A method of separating free target analyte from protein-bound target analyte is described. Such can include obtaining an aqueous sample containing a target analyte in a free form (free target analyte) and the target analyte in a protein-bound form (protein-bound target analyte), passing the aqueous sample through a size exclusion chromatography matrix with a molecular weight cut off sufficient to allow the free target analyte to permeate into pores of the size exclusion chromatography matrix and exclude the protein-bound target analyte, whereupon the free target analyte adheres to and is immobilized by the size exclusion chromatography matrix and the protein-bound target analyte does not adhere to by the size exclusion chromatography matrix, separating the free target analyte from the protein-bound analyte by removing the protein-bound target analyte from the size exclusion chromatography matrix, and eluting the free target analyte from the size exclusion chromatography matrix with an organic solvent.

Provided are a platelet-derived growth factor B derivative, the encoding nucleic acid molecule thereof, and a vector and host cell having the nucleic acid molecule. Also provided are a preparation method for the mutant, and the use of the mutant in preparing medications for promoting cell division, cell proliferation, wound healing, skin regeneration, bone and tooth defect regeneration, and joint repair.

Provided are a platelet-derived growth factor B derivative, the encoding nucleic acid molecule thereof, and a vector and host cell having the nucleic acid molecule. Also provided are a preparation method for the mutant, and the use of the mutant in preparing medications for promoting cell division, cell proliferation, wound healing, skin regeneration, bone and tooth defect regeneration, and joint repair.

A method for preparing needle coke for ultra-high power (UHP) electrodes from heavy oil is provided. In this method, heavy oil is used as a raw material. The size exclusion chromatography (SEC) is conducted with polystyrene (PS) as a packing material to separate out specific components with a relative molecular weight of 400 to 1,000. The ion-exchange chromatography (IEC) is conducted to remove acidic and alkaline components to obtain a neutral raw material. The neutral raw material is subjected to two-stage consecutive carbonization to obtain green coke, and the green coke is subjected to high-temperature calcination to obtain the needle coke for UHP electrodes. The needle coke has a true density of more than 2.13 g/cm.sup.3 and a coefficient of thermal expansion (CTE) of ≤1.15×10.sup.−6/° C. at 25° C. to 600° C.