You searched for: Proteins and Peptides

Supplier: Prosci

The prolactin receptor (PRLR) is a member of the class I cytokine/lactogen receptor family which mediates the diverse cellular actions of prolactin in several tissues. PRLRs are expressed in normal and neoplastic human breast tissue, and in most breast cancer cells. PRLR contains an extracellular region that binds prolactin, a transmembrane region, and a cytoplasmatic region required for the activation of the Jak2–Stat5 signal transduction pathway by Prl which is essential for transcriptional activation of all known prolactin regulated genes. PRLRs have also been observed in ovarian follicular cells of mice, pigs, sheep, deer, and humans, as well as in luteal tissue in cow and horse ovaries. Furthermore, PRLR knockout mice exhibit failure of embryonic implantation, reduced number of mature oocytes, and low fertilization rates. Knockout females also display a reduced number of primary follicles.

Supplier: BioVendor

Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies.

Supplier: Prosci

Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumor cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.

Supplier: Prosci

Interleukin-22(IL-22) is a member of a group of the IL-10 family, a class of potent mediators of cellular inflammatory responses. IL-22 is produced by activated DC and T cells. IL-22 and IL-10 receptor chains play a role in cellular targeting and signal transduction. It can initiate and regulate innate immune responses against bacterial pathogens especially in epithelial cells such as respiratory and gut epithelial cells. IL-22 along with IL-17 likely plays a role in the coordinated response of both adaptive and innate immune systems. IL-22 also promotes hepatocyte survival in the liver and epithelial cells in the lung and gut similar to IL-10. Biological activity of IL-22 is initiated by binding to a cell-surface complex consisting of IL-22R1 and IL-10R2 receptor chains. IL-22 biological activity is further regulated by interactions with a soluble binding protein, IL-22BP. IL-22BP and an extracellular region of IL-22R1 share sequence similarity. In some cases, the pro-inflammatory versus tissue-protective functions of IL-22 are regulated by cytokine IL-17A.

Supplier: Thermo Scientific Chemicals

Highly active luteinizing hormone releasing hormone (LHRH) agonist

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Prosci

ENA-78 is a CXC chemokine that signals through the CXCR2 receptor. It is expressed in monocytes, platelets, endothelial cells, and mast cells. ENA-78 is a chemoattractant for neutrophils. The murine homolog of ENA-78 is called LIX. Three N-terminal truncated variants of human ENA-78; ENA 5-78, ENA 8-78, ENA 9-78, contain 74, 71, and 70 amino acid residues, respectively, possess increased biological activity. ENA-78 contains the four conserved cysteine residues present in CXC chemokines, and also contains the ‘ELR’ motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors. Recombinant human ENA-78 is a 7.8 kDa protein consisting of 71 amino acid residues.

Supplier: Prosci

Intelectin-1(ITLN1) is a secreted protein and contains 1 fibrinogen C-terminal domain. Intelectin-1 is a 40 kDa Ca-dependent galactofuranose-binding lectin that is not a C-type lectin. It is expressed on multiple cell types and appears to participate in insulin signaling and microbe recognition. The protein has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. It increases AKT phosphorylation in the absence and presence of insulin and it may play a role in the defense systemagainst microorganisms. It also may specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosy l residues, in a calcium-dependent manner.

Supplier: Prosci

IL-2R is a heterotrimeric protein binds and responds to the cytokine IL-2. Three distinct chains of IL-2R, termed as ?, ? and ?, which are non-covalently associated are identified. The ? and ? chains are involved in binding IL-2, while signal transduction following cytokine interaction is carried out by the ? chain, along with the ? subunit. The ? chain of the IL-2R can bind to the ? chain before receptor interaction with IL-2. The ? chain alone has a very weak affinity for IL-2, but after the ligand is bound to the ?/? heterodimer, the ? chain becomes recruited to the complex to form a very stable macromolecular quaternary ligand/receptor complex.
Interleukin-2 receptor subunit gamma (IL2RG), also known as cytokine receptor common subunit gamma, CD antigen CD132, gammaC, p64, which belongs to the type I cytokine receptor family or type 5 subfamily. IL2RG is located on the surface of immature blood-forming cells in bone marrow. Defects in IL2RG are the cause of severe combined immunodeficiency X-linked T-cell-negative/B-cell-positive/NK-cell-negative (XSCID).

Supplier: Prosci

Inter-Cellular Adhesion Molecule 1 (ICAM-1) is also known as Cluster of Differentiation 54 (CD54), is a member of the immunoglobulin superfamily, and is a cell surface glycoprotein which is typically expressed in low concentrations on endothelial cells and cells of the immune system. The protein encoded by this gene is a type of intercellular adhesion molecule continuously present in low concentrations in the membranes of leukocytes and endothelial cells. Upon cytokine stimulation, the concentrations greatly increase. ICAM-1 can be induced by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNF?) and is expressed by the vascular endothelium, macrophages, and lymphocytes. ICAM-1 is a ligand for LFA-1 (integrin), a receptor found on leukocytes. When activated, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues. ICAM-1 has been implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be significantly elevated in patients with SAH over control subjects in many studies. ICAM-1 expressed by respiratory epithelial cells is also the binding site for rhinovirus, the causative agent of most common colds.

Supplier: Prosci

RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant human sRANKL is a 20.0 kDa polypeptide comprising the TNF homologous region of RANKL (176 amino acid residues).

Supplier: Prosci

RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic-cell-membrane protein, which by interacting with RANKL augments the ability of dendritic cells to stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, to promote the survival of RANK + T cells, and to regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. Recombinant murine sRANKL is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Supplier: Prosci

Programmed death ligand 1 (PD-L1, B7-H1 or CD274) is a member of the growing B7 family of immune proteins that provide signals for both stimulating and inhibiting T cell activation. CD274 has been identified as one of two ligands for programmed death 1 (PD-1), a member of the CD28 family of immunoreceptors. CD274 is widely expressed in several organs such as heart, skeletal muscle, placenta and lung, and in lower amounts in thymus, spleen, kidney and liver. CD274 expression is upregulated in a small fraction of activated T and B cells and a much larger fraction of activated monocytes. CD274 expression is also induced in dendritic cells and keratinocytes after IFN-gamma stimulation. CD274 expression is also upregulated in a variety of tumor cell lines. Interaction of CD274 with PD-1 results in inhibition of TCR mediated proliferation and cytokine production, suggesting an inhibitory role in regulating immune responses. The CD274 - PD-1 pathway is involved in the negative regulation of some immune responses and may play an important role in the regulation of peripheral tolerance.

Supplier: Thermo Scientific Chemicals

Molecular Formula: C32H43FN6O10.xC2HF3O2.yH2O
Formula Weight: 690.71(anhy)
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: Off-white to pale brown
Solubility: Soluble in DMSO.
MDL No.: MFCD01862609

Supplier: Prosci

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-B. PDGFR-a is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-B interacts with only PDGF-BB and PDGF-AB. Recombinant human PDGF-AB is a 25.5 kDa disulfide-linked dimer, consisting of one A chain and one B chains (234 total amino acids).

Supplier: Prosci

Bone Marrow Stromal Antigen 2 (BST2) is a single-pass type II membrane protein that belongs to the tetherin family. BST2 is predominantly expressed in the liver, lung, heart and placenta. BST2 is involved in the sorting of secreted proteins. BST2 is a human cellular protein which inhibits retrovirus infection by preventing the diffusion of virus particles after budding from infected cells. BST2 is initially discovered as an inhibitor to HIV-1 infection in the absence of Vpu, it has also been shown to inhibit the release of other viruses such as retroviruses, filoviruses, arenaviruses, and herpes viruses. BST2 may play a role in B-cell activation in rheumatoid arthritis.

Supplier: Prosci

Cryptic (CFC1) is a member of the epidermal growth factor (EGF)- Cripto, Frl-1, and Cryptic (CFC) family. It contains an EGF-like domain, and is glycosylated on its N-terminal during post-translational modification. Cryptic is identified as a NODAL coreceptor involved in the correct establishment of the left-right axis. It may play a role in mesoderm and/or neural patterning during gastrulation. The unnormal expression of this gene may causes a series of diseases such as HTX2, Transposition of the great arteries dextro-looped 2, and Conotruncal heart malformations.

Supplier: MilliporeSigma

A reversible inhibitor of trypsin-like proteases and cysteine proteases

Supplier: Prosci

CD33 is a type I Lectin belonging to the Ig superfamily. CD33 contains an N terminal Ig like V type domain, which mediates sialic acid binding, followed by one Ig like C2 type domain, a transmembrane region and a cytoplasmic tail containing two conserved immunoreceptor tyrosine based inhibition motifs (ITIMs). Eleven human Siglecs have been characterized. Siglecs 5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. They are collectively referred to as CD33 related Siglecs. CD33 related Siglecs have differential expression pattern within the hematopoietic system. They are involved in the regulation of cellular activation within the immune system. Siglec 3 expression is restricted to cells of myelomonocytic lineage. Siglec3 recruits SHP1 and SHP2 to its ITIMs upon phosphorylation.

Supplier: Prosci

Interleukin-1 receptor type 2 (IL1R2) belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1 receptor type II is a 68 kDa transmembrane protein found on B lymphocytes, neutrophils, monocytes, large granular leukocytes and endothelial cells. IL1R2 is non-signaling receptor forIL1A, IL1B and IL1RN, reduces IL1B activities. IL1R2 serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.

Supplier: Prosci

IL-3 is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T cells, mast cells and eosinophils, IL-3 enhances thrombopoieses, phagocytosis, and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL-3 may have additional immunoregulatory roles. Many of the IL-3 activities depend upon co-stimulation with other cytokines. IL-3 is species-specific, variably glycosylated cytokine. Recombinant rat IL-3beta is a 16.3 kDa globular protein containing 144 amino acid residues.

Supplier: Prosci

Human DUSP3 belongs to the dual specificity protein phosphatase subfamily. DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSPs are major modulators of critical signalling pathways that are dysregulated in various diseases. They negatively regulate members of the mitogen-activated protein kinase superfamily, which are associated with cellular proliferation and differentiation. DUSP3 is expressed in human tissues including breast and ovarian.DUSP3 shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Human DUSP3 specifically dephosphorylates and inactivates ERK1 and ERK2.

Supplier: Thermo Scientific Chemicals

Molecular Formula: C16H28N6O4
Formula Weight: 368.40
Physical Form: Powder
Appearance: White
MDL No.: MFCD00081011

Supplier: Shenandoah Biotechnology

Fibroblast growth factor 4 (FGF4) is a secreted growth factor that is predominantly expressed during bone morphogenesis and embryonic limb development. FGF4 is an important growth regulator for stem cells, fibroblasts, and endothelial cells. FGF4 contains a single N-linked glycosylation signal. However, in-vitro studies suggest that unglycosylated FGF4 is cleaved into 13 kDa and 15 kDa truncated proteins that have greater biological activity than the wild type 19 kDa FGF4 protein. Human FGF4 shares high homology and is cross-reactive with mouse FGF4.

Supplier: Prosci

Angiopoietin-related protein 4（ANGPTL4）is a secreted protein and contains 1 fibrinogen C-terminal domain. The protein may act as a regulator of angiogenesis and modulate tumorigenesis. It inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 may exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity (By similarity). In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation.

Supplier: Rockland Immunochemical

1mg. Antibody Concentration: 1 mg/mL. Fluorochrome/Protein: 3.4 moles Texas Red per mole of Human Transferrin. Buffer: 0.02M potassium phosphate, 0.15M sodium chloride, pH 7.2. Stabilizer: 10 mg/mL BSA IgG and protease free. For research. Lyophilized.

Supplier: Prosci

IL-12 is a potent regulator of cell mediated immune responses and it induces IFN-gamma production by NK and T cells. It is produced by activated monocytes/macrophage cells, B lymphocytes and connective tissue type mast cells. Among its biological activities IL-12 promotes the growth and activity of activated NK, CD4+ and CD8+ cells and induces the development of IFN-gamma producing Th1 cells. Recombinant murine IL-12 is a 75.0 kDa heterodimeric glycoprotein consisting of disulfide-linked 35 kDa (p35) and 40 kDa (p40) subunits (506 total amino acid residues). Recombinant Human IL-12 is a 75.0 kDa heterodimeric glycoprotein consisting of disulfide-linked 35 kDa (p35) and 40 kDa (p40) subunits (503 total amino acid residues).

Supplier: Prosci

The TNF family ligand ectodysplasin A (EDA) and its receptor EDAR are required for proper development of skin appendages such as hair, teeth and eccrine sweat glands. Loss of function mutations in the Eda gene cause X-linked hypohidrotic ectodermal dysplasia (XLHED), a condition that can be ameliorated in mice and dogs by timely administration of recombinant EDA. The Eda gene on the X chromosome is transcribed as multiple splice variants, only two of which code for the receptor-binding C-terminal TNF homology domain. These two variants code for 391- and 389-amino acid-long proteins called EDA1 and EDA2. EDA1 binds EDAR, whereas EDA2 binds to another receptor, XEDAR. The biology of EDA2 and XEDAR is distinct from that of EDA1. Indeed, XEDAR-deficient mice have no obvious ectodermal dysplasia phenotype, whereas mice deficient in EDA, EDAR, or the signaling adaptor protein EDARADD all display virtually indistinguishable ectodermal dysplasia phenotypes, indicating the predominance of the EDA1-EDAR axis in the development of skin-derived appendages.

Supplier: Prosci

GDF-2 belongs to the TGF-B cytokine family whose members play an important role during prenatal development and postnatal growth, remodeling and maintenance of a variety of tissues and organs. GDF-2 is expressed mainly in nonparenchymal cells of the liver, but is also found in other various cells and tissues. GDF-2 can signal through the ALK1 receptor and has been implicated in a number of physiologic events. These include regulation of the hepatic reticuloendothelial system, glucose homeostasis, and iron homeostasis, as well as the inhibition of angiogenesis. Recombinant human GDF-2 is a 24.1 kDa disulfide linked homodimeric protein consisting of two 110 amino acid polypeptide chains.

Supplier: Prosci

Follistatin-like 1 (FSTL1) is a secreted glycoprotein that has been grouped into the follistatin family of proteins. FSTL1 is composed of a follistatin domain and two non-functional calcium-binding motifs. It was originally cloned as a TGF beta 1 inducible factor but subsequently shown to regulate diverse developmental pathways and tissue homeostasis. Ablation of the FSTL1 gene in the mouse results in several structural developmental defects and neonatal lethality due to respiratory failure. FSTL1 suppresses BMP signaling, but the precise mechanism of its action has not been elucidated. FSTL1 is expressed in the human placenta, mainly in extravillous trophoblasts.