
Katalognummer: 209 - 200-002S-AF
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 2 µg
200-002-AF
Human Bone Morphogenetic Protein-2 (BMP-2) is a disulfide-bonded homodimeric protein with an apparent molecular weight of 26 kDa. BMP-2 regulates similarly to its nearest homologue BMP-4 diverse fundamental processes during embryonic development: BMP-2 and other BMP proteins have great potential for medical therapeutic applications, in particular because they allow or at least accelerate the ossification of extensive bone lesions. The amino acid sequence of recombinant human BMP-2 starts with MQAKHKQ (position 283) containing the Met from the E. coli expression vector. BMP-2 is a heparin binding protein.
200-002S-AF
Human Bone Morphogenetic Protein-2 (BMP-2) is a disulfide-bonded homodimeric protein with an apparent molecular weight of 26 kDa. BMP-2 regulates similarly to its nearest homologue BMP-4 diverse fundamental processes during embryonic development: BMP-2 and other BMP proteins have great potential for medical therapeutic applications, in particular because they allow or at least accelerate the ossification of extensive bone lesions. The amino acid sequence of recombinant human BMP-2 starts with MQAKHKQ (position 283) containing the Met from the E. coli expression vector. BMP-2 is a heparin binding protein.
40-722
BMPs (Bone Morphogenetic Proteins) belong to the TGF-β superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human/Murine/Rat BMP-2 is a 26.0 kDa homodimeric protein consisting of two 115 amino acid polypeptide chains.
100-087S-AF
NT-4 is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-3. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. NT-4 is expressed in the prostate, thymus, placenta, and skeletal muscle. NT-4 can signal through the LNGFR and trkB receptors, and promotes the survival of peripheral sensory sympathetic neurons. Recombinant Human NT-4 is a noncovalently linked homodimer of two 14.0 kDa polypeptide monomers (260 total amino acid residues).
100-019-AF
FGF-6 is a secreted, heparin-binding growth factor that is a member of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-6 is expressed in leukemia cell lines with platelet megakaryocytic differentiation potential. It signals through FGFR 1c, 2c, and 4. Recombinant Human FGF-6 is an 18.7 kDa protein consisting of 168 amino acid residues.
100-019S-AF
FGF-6 is a secreted, heparin-binding growth factor that is a member of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-6 is expressed in leukemia cell lines with platelet megakaryocytic differentiation potential. It signals through FGFR 1c, 2c, and 4. Recombinant Human FGF-6 is an 18.7 kDa protein consisting of 168 amino acid residues.

By: Author , 2 Comment
23 August 2025

By: Author , 2 Comment
16 August 2025

By: Author , 2 Comment
1 August 2025

By: Author , 2 Comment
22 July 2025

