Abstract: Engineered FGF1 and FGF2 polypeptides, polynucleotides encoding these polypeptides and DNA constructs, vectors and compositions including these engineered polypeptides are provided herein. The engineered FGF1 and FGF2 polypeptides are more stable than their wild-type counterparts and may be more effective at treating a variety of conditions that FGF1 and FGF2 are useful for treating such as wound healing.

Abstract: Engineered FGF1 and FGF2 polypeptides, polynucleotides encoding these polypeptides and DNA constructs, vectors and compositions including these engineered polypeptides are provided herein. The engineered FGF1 and FGF2 polypeptides are more stable than their wild-type counterparts and may be more effective at treating a variety of conditions that FGF1 and FGF2 are useful for treating such as wound healing.

Abstract: Engineered FGF1 and FGF2 polypeptides, polynucleotides encoding these polypeptides and DNA constructs, vectors and compositions including these engineered polypeptides are provided herein. The engineered FGF1 and FGF2 polypeptides are more stable than their wild-type counterparts and may be more effective at treating a variety of conditions that FGF1 and FGF2 are useful for treating such as wound healing.

Abstract: The present invention relates to the development of stable mutants of FGF-1 and FGF-2. In particular, it relates to novel engineered FGF-1 and FGF-2 polypeptides as well as polynucleotides, DNA constructs, and vectors encoding such polypeptides. In another aspect, pharmaceutical compositions and hydrogels including the disclosed polypeptides, polynucleotides, DNA constructs, and vectors are provided. In a still further aspect, methods of treating conditions using the compositions disclosed herein are provided.

Abstract: In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine.

Abstract: The present invention relates to the development of stable mutants of FGF-1 and FGF-2. In particular, it relates to novel engineered FGF-1 and FGF-2 polypeptides as well as polynucleotides, DNA constructs, and vectors encoding such polypeptides. In another aspect, pharmaceutical compositions and hydrogels including the disclosed polypeptides, polynucleotides, DNA constructs, and vectors are provided. In a still further aspect, methods of treating conditions using the compositions disclosed herein are provided.

Abstract: In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine.

Abstract: Compositions including chitosan covalently linked to a cytokine or growth factor are provided herein. The compositions can be used to produce pharmaceutical compositions and can be used in methods of treating a variety of diseases or disorders. The compositions are especially suitable for localized delivery and may allow for intratamoral delivery and treatment of cancers or stimulation of an immune response to a co-administered antigen.

Abstract: In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine.

Abstract: In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine.