Supplier: PeproTech, Inc.

Description: Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b-9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL-8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive C5a activation has been linked to liver fibrosis, sepsis, adult respiratory distress syndrome, rheumatoid arthritis, Alzheimer’s disease, and ischemic heart disease. Human C5a shares 60% and 54% sequence identity to mouse and rat C5a, respectively. The human C5 gene encodes a 1,676 amino acid glycoprotein that is comprised of a disulfide-linked C5 alpha and a C5 beta chain, the former of which contains the active, 74 amino acid C5a anaphylatoxin chain. Recombinant Human C5a is an 8.28 kDa glycoprotein containing the 74 amino acid residues of the C5a anaphylatoxin chain.

Supplier: PeproTech, Inc.

Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible (“suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes, including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In humans, the serpins represent approximately 2% of total serum proteins, of which 70% is α1-antitrypsin. Vaspin exhibits 40.2% sequence identity with α1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines, including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant Human Vaspin is a 45.2 kDa protein containing 395 amino acid residues.

Supplier: PeproTech, Inc.

Description: The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potency Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.

Supplier: PeproTech, Inc.

Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in

Catalog Number: (10771-886)

Supplier: PeproTech, Inc.

Description: The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potency Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.

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Supplier: PeproTech, Inc.

Description: Human soluble DLL-1 comprises the extracellular signaling domain of DLL-1, a member of the Delta/Serrate/Lag-2 (DSL) family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. It is expressed primarily in the heart, pancreas and epidermis. DLL-1 functions to specifically activate the Notch-1 and Notch-2 receptors. Proteolytic cleavage of DLL-1 produces a secreted extracellular domain, sDLL-1, that interacts with Notch receptors expressed on adjacent cells. Notch signaling plays an essential role in controlling cell fate decisions during prenatal development and postnatal stem cell renewal, and differentiation in many tissues. Human sDLL-1 blocks monocyte differentiation into macrophages, but permits differentiation into dendritic cells. In hematopoietic progenitor cells, hsDLL-1, suppresses differentiation into B-cells, while promoting differentiation into T-cells and NK cell precursors. In cell culture, human sDLL-1 has been shown to promote expansion of hematopoietic progenitor cells and suppress apoptosis by inhibiting differentiation. Overexpression of Notch receptors appears to inhibit differentiation in several mammalian cell lines, and increasing evidence suggests that Notch signaling is frequently downregulated in human malignancies. The human DLL-1 gene consists of a 528 amino acid extracellular domain with one DSL domain, eight EGF-like repeats, a 23 amino acid transmembrane domain, and a 155 amino acid cytoplasmic domain. The calculated molecular weight of Recombinant Human sDLL-1 is 56.3 kDa.

Supplier: PeproTech, Inc.

Description: Angiopoietin-1 (ANG-1) is a secreted ligand for Tie-2, a tyrosine-kinase receptor expressed primarily on vascular endothelial cells and early hematopoietic cells. ANG-1/Tie-2 signaling promotes angiogenesis during the development, remodeling, and repair of the vascular system. Transgenic mice lacking expression of either ANG-1 or Tie-2 fail to develop a fully functional cardiovascular system and die before birth. Postnatally, the angiogenic activity of ANG-1/Tie-2 is required during normal tissue repair and remodeling of the female endometrium in the menstrual cycle. ANG-1/Tie-2 signaling appears to be regulated by Angiopoietin-2 (ANG-2), a natural antagonist for Tie-2 that exerts its effects through an internal autocrine loop mechanism. In addition to suppressing endothelial cell activation by inhibiting the expression of adhesion and inflammatory molecules, Ang-1 enhances endothelial cell survival and capillary morphogenesis, and lessens capillary permeability. As such, ANG-1 has potential to become an effective therapeutic agent for treating various endothelium disorders, including several severe human pulmonary diseases. The efficacy of cell-based Ang-1 gene therapy for acute lung injury (ALI) has recently been studied in a rat model of ALI. The results of this study show that such therapy can markedly improve lung condition and suggest that Ang-1 therapy may represent a potential new strategy for the treatment and/or prevention of acute respiratory distress injury (ARDI), a significant cause of morbidity and mortality in critically ill patients. Recombinant Human ANG-1, derived from

Catalog Number: (76304-086)

Supplier: PeproTech, Inc.

Description: Irisin is a proteolytic hormone released into circulation by skeletal muscle tissue during acute exercise, and is a derivative of the cleaved plasma membrane protein Fibronectin type III domain-containing protein 5 (FNDC5). Found in muscle tissue, FNDC5 is synthesized at increased levels during exercise as a result of the overexpression of the exercise-responsive transcriptional co-activator PGC-1alpha (peroxisome proliferator-activated receptor-gamma co-activator-1alpha). Like its parent polypeptide, Irisin can induce the browning of subcutaneous adipocytes, or the conversion of white adipose tissue (WAT or white fat) into brown (or beige) adipose tissue (BAT or brown fat). Given that brown fat can undergo thermogenesis, or the physiologic process of heat production, Irisin contributes to the metabolic process by increasing thermogenic function and glucose homeostasis. Irisin, thus, represents a link between exercise and "burning" of fats and/or sugars, and consequently may have relevance in the development of new treatments for diabetes and obesity. CHO cell-derived Recombinant Human/Murine/Rat Irisin is a glycosylated homodimer of 224 amino acid residues, whose monomer consists of 112 amino acid residues corresponding to the active portion of the 121-amino-acid length Irisin extracellular domain. Recombinant Human/Murine/Rat Irisin, appears to form a non-disulfide linked oligomeric structure in solution, has a calculated theoretical molecular weight of 25.2 kDa, but migrates at an apparent molecular weight of 28 kDa by SDS-PAGE analysis under reducing conditions due to glycosylation.

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Supplier: PeproTech, Inc.

Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. Human Klotho exists in both membrane bound and secreted forms, and is predominantly expressed in the kidney convoluted tubules, and, to a lesser extent, in the brain, reproductive organs, endocrine glands, urinary bladder, skeletal muscle, placenta, and colon. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively. The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease, which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone-derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant Human Klotho is a glycoprotein of 516 amino acid residues that migrates at an apparent molecular weight of 65-70 kDa by SDS-PAGE analysis under reducing conditions. Recombinant Human Klotho has a calculated molecular weight of 58.6 kDa.

Supplier: PeproTech, Inc.

Description: PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47 kDa, nonglycosylated, intracellular protein, which can be induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular, dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable, except during pregnancy and in some forms of monocytic leukemia. Secretion of PAI-2 from the placenta normally occurs during the third trimester of pregnancy, and accounts for the dramatic increase in PAI-2 levels (up to 250 ng/ml), which are maintained at these levels until postpartum, and then rapidly decline. In addition to its vital role in protecting the placenta from degradation by uPA and/or uPA-activated proteases, PAI-2 has been shown to be essential for the prevention of metastatic spread of neck, lung and breast cancers. The beneficial effect of PAI-2 seen in these studies is presumed to stem from its ability to inhibit uPA-dependent cell dissemination. PAI-2 has also been reported to inhibit keratinocyte proliferation, and to participate in the innate immune response during viral infection. Recombinant Human PAI-2 is a 46.5 kDa, nonglycosylated protein of 415 residues.

Supplier: PeproTech, Inc.

Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue.  Recently, visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity.  Like insulin, visfatin exerts hypoglycemic effects by interacting with the insulin receptor.  The binding affinity of visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites.  The circulating levels of visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of visfatin may not be of physiological importance.  The plasma visfatin levels, like those of leptin, correlate positively with the percent of body fat, and increase during the development of obesity. Receptors for both leptin (Ob-R) and visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism.  Although the metabolic function of visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat.  The PBEF gene encodes a polypeptide of 491 amino acid residues. The secreted form of this polypeptide, i.e. visfatin, contains 465 residues and lacks the first 26 N-terminal residues of the PBEF gene product. The 491-residue form has been shown to be a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. The amino acid sequence of visfatin is highly conserved across different species and shows no homology to any known protein. It contains 5 cysteine residues, of which only two of them appear to be involved in disulfide bridge formation. Recombinant human Visfatin is a 52.6 kDa protein containing 466 amino acid residues (isoform 1).

Catalog Number: (76470-378)

Supplier: PeproTech, Inc.

Description: RECOM CHOCELL IL-18BPFC HU >/= 95% 250UG

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Catalog Number: (76470-380)

Supplier: PeproTech, Inc.

Description: RECOM CHOCELL IL-18BPFC HU >/= 95% 500UG

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Catalog Number: (76470-372)

Supplier: PeproTech, Inc.

Description: RECOM CHOCELL IL-18BPFC HU >/= 95% 100UG

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Catalog Number: (76470-376)

Supplier: PeproTech, Inc.

Description: RECOM CHO CELL IL18BP FC HU >/= 95% 20UG

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Catalog Number: (76470-374)

Supplier: PeproTech, Inc.

Description: RECOM CHO CELL IL-18BP FC HU >/= 95% 1MG

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