Supplier: Prosci

Description: Persephin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, Artemin, and Neurturin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR alpha (alpha1-alpha4) receptors. The GFRalpha4 was first identified in chicken and was later shown to be the preferential binding subunit for Persephin. Persephin promotes the survival of ventral midbrain dompaminergic neurons and motor neurons after sciatic nerve oxotomy, and like GNDF, promotes ureteric bud branching. However, in contrast to GDNF and Neurturin, Persephin does not support survival of peripheral neurons. Recombinant human Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 63) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Human Recombinant protein manufactured under license from the University of Washington patent# US 6,716,600; US 6,692,943; US 6,645,937; US 6,403,335; US 6,232,449; US 6,222,022.

Catalog Number: (10339-142)

Supplier: Bioss

Description: This gene encodes an epididymal protease inhibitor, which contains both kunitz-type and WAP-type four-disulfide core (WFDC) protease inhibitor consensus sequences. Most WFDC genes are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. This gene is a member of the WFDC gene family and belongs to the telomeric cluster. The protein can inhibit human sperm motility, and polymorphisms in this gene are associated with male infertility. Read-through transcription also exists between this gene and the downstream WFDC6 (WAP four-disulfide core domain 6) gene. [provided by RefSeq].

Catalog Number: (10459-182)

Supplier: Bioss

Description: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Catalog Number: (10459-184)

Supplier: Bioss

Description: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Catalog Number: (76079-766)

Supplier: Bioss

Description: This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms.

Catalog Number: (10408-936)

Supplier: Bioss

Description: This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].

Supplier: Prosci

Description: PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs; PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant human PDGF-AA is a 28.5 kDa disulfide-linked homodimer of two A chains (250 total amino acids). Recombinant murine PDGF-AA is a 28.7 kDa disulfide-linked homodimer of two A chains (250 total amino acids).

Catalog Number: (10072-650)

Supplier: Prosci

Description: Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins which include NP-1, NP-2 and NP-3, are distinguished from the β-defensins by the pairing of their three disulfide bonds. In addition to antimicrobial activity, NP-1 exhibits chemotactic activity on dendritic cells. NP-1 is expressed as the C-terminal portion of an inactive precursor protein, which also contains a 19 amino acid N-terminal signal sequence and a 45 amino acid polypeptide. NP-1 contains a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant human NP-1 is a 3.4 kDa protein containing 30 amino acid residues.

Catalog Number: (10408-938)

Supplier: Bioss

Description: This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].

Catalog Number: (10408-942)

Supplier: Bioss

Description: This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].

Supplier: Peprotech

Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Rat Resistin is a 20.0 kDa, disulfide-linked, homodimeric protein composed of two 94 identical amino acid chains linked by a single disulfide bond.

Supplier: Peprotech

Description: IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate proliferation and activation of T-cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. Recombinant Murine IL-17F is a 30.0 kDa, disulfide-linked homodimer consisting of two 134 amino acid residue chains.

Catalog Number: (10072-856)

Supplier: Prosci

Description: IL-17B is a disulfide-linked homodimer of two 161 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17B is expressed by T-cells and has been shown to stimulate release of TNF-α and IL-1β from cells of the monocyte lineage. Recombinant human IL-17B is a 36.6 kDa non-disulfide-linked homodimer of two 161 amino acid polypeptide chains.

Supplier: Peprotech

Description: GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 354 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease. Recombinant Human GDF-5 (BMP-14/CDMP-1) is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.

Supplier: Peprotech

Description: The Insulin/Relaxin structural family of proteins consists of at least seven members, each containing an insulin-like heterodimeric structure of two polypeptide chains held together by two inter-chain disulfide bonds. The INSL5/INSL7 hybrid contains the β-chain of INSL7 (Relaxin-3), linked to the α-chain of INSL5. The INSL5/INSL7 hybrid protein can specifically activate the G protein-coupled receptors, GPCR135 and GPCR142, but unlike Relaxin-3, does not induce significant activation of the LGR7 receptor. Recombinant Human INSL5/INSL7 Hybrid is a heterodimeric, 5.2 kDa protein consisting of a 27 amino acid β-chain linked to a 21 amino acid α-chain by two disulfide bonds.

Supplier: Peprotech

Description: PlGF-1 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-1 is expressed in placental tissues, the colon and mammary carcinomas. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. Recombinant Human PlGF-1 is a 29.7 kDa disulfide-linked homodimeric protein of two 132 amino acid polypeptide chains.Manufactured using all Animal-Free reagents.