You searched for: Proteins and Peptides

Supplier: Prosci

Wnts are lipid-modified morphogens that control many processes during development, stem cell maintenance and homeostasis and their aberrant regulation has been linked to diseases in man including diabetes, neurodegeneration and cancer. Three distinct receptor families mediate Wnt signaling: Fzs, the single-pass LRP5/6 co-receptors and the atypical tyrosine kinase receptors Ror2 and Ryk. Frizzled proteins can activate canonical Wnt/beta-catenin signaling as well as non-canonical pathways (Wnt/Ca2+ pathways and planar cell polarity). The cysteine-rich domain (CRD) of the frizzled receptors situated on the extracellular part of the receptor is sufficient to bind the Wnt ligands.

Supplier: Prosci

IL-23 is a proinflammatory heterodimeric protein composed of two subunits, a unique p19 subunit and a p40 subunit, which is shared with IL-12. IL-23 is secreted by activated dendritic cells and macrophages, and signals though a receptor comprised of IL-23R complexed with IL-12Rβ2. IL-23 has been shown to enhance proliferation of memory T cells. It also stimulates the production of IFN-gamma in NK cells, induces IL-17 production, and drives Th17 mediated responses. Recombinant IL-23 is a 53.5 kDa heterodimeric protein consisting of two subunits, p19 (170 amino acids) and p40 (306 amino acids).*Manufactured using BTI-Tn-5B1-4 cells under license from the Boyce Thompson Institute for Plant Research, Inc.

Supplier: Prosci

It is a single-pass type I membrane protein and contains 4 TNFR-Cys repeats. The protein is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein is the receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. It promotes apoptosis via TRAF3 and TRAF5 and may play a role in the development of lymphoid organs. The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis. Not only does the TNFRSF3 help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of TNFRSF3 in Human Cells cells increases IL-8 promoter activity and leads to IL-8 release. TNFRSF3 is also essential for development and organization of the secondary lymphoid organs and chemokine release.

Supplier: Prosci

The tetrameric receptor complex for IFN gamma consists of two subunits, IFNGR1 (IFN gamma R alpha) and IFNGR2 (IFN gamma R beta ), through which the dimeric IFN- gamma exerts its biological functions, including antiviral, antiproliferation and immune-modulatory activity in mammals. Both IFNGR1 and IFNGR2 are single transmembrane proteins belonging to the class II cytokine family. FNGR1, widely expressed in most host cells, is essential for IFN gamma binding, receptor trafficking, and signal transduction. IFNGR1 possesses an intracellular Janus tyrosine kinase (JAK) 1 binding site, a signal transducer and activator of transcription 1 (STAT1) binding site. The resulting STAT1 homodimers translocate from the cytoplasm to the nucleus and bind to the interferon-gamma activated sequence (GAS) promoter to induce expression of downstream interferon stimulated genes (ISGs).

Supplier: Prosci

CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.

Supplier: Prosci

CD19 is a single-pass type I membrane protein containing 2 Ig-like C2-type (immunoglobulin-like) domains. CD19 is expressed on follicular dendritic cells and B cells. In fact, it is present on B cells from earliest recognizable B-lineage cells during development to B-cell blasts but is lost on maturation to plasma cells. CD19 primarily acts as a B cell co-receptor in conjunction with CD21 and CD81. Upon activation, the cytoplasmic tail of CD19 becomes phosphorylated, which leads to binding by Src-family kinases and recruitment of PI-3 kinase. CD19 Assembles with the antigen receptor of B lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation. Defects in CD19 are the cause of immunodeficiency common variable type 3 (CVID3) which is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen.

Supplier: Prosci

Human beta -Nerve Growth Factor ( beta -NGF) was initially isolated in the mouse submandibular gland. It is composed of three non-covalently linked subunits alpha, beta , and gamma ; it exhibits all the biological activities ascribed to NGF. It is structurally related to BDNF, NT-3 and NT-4 and belongs to the cysteine-knot family of growth factors that assume stable dimeric structures. beta -NGF is a neurotrophic factor that signals through its receptor beta -NGF, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. beta -NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. These results suggest that beta -NGF is a pleiotropic cytokine, which in addition to its neurotropic activities may have an important role in the regulation of the immune system. Human beta -NGF shares 90% sequence similarity with mouse protein and shows cross-species reactivity.

Supplier: Prosci

SLAM Family Member 6 (SLAMF6) is a 60 kD single-pass type I membrane protein that belongs to the SLAM subgroup of the CD2 family. Human SLAMF6/ NTB-A contains a 205 amino acid extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain, a 21 amino acid transmembrane segment and an 84 amino acid cytoplasmic domain, with two immunoreceptor tyrosine-based switch motifs. SLAMF6 is a homodimer. SLAMF6 can interact with PTN6 and, upon phosphorylation, with PTN11 and SH2D1A/SAP. Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN- gamma by NK cells and independent of EAT-2 binding. It Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. On B cells, NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity.

Supplier: Prosci

Ephrin-B1, also named EFL-3, ELK ligand, EPH-related receptor tyrosine kinase ligand 2, is a single-pass type I membrane protein. It contains 1 ephrin RBD (ephrin receptor-binding) domain and belongs to the ephrin family. Ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. All ephrins share a conserved extracellular sequence, which most likely corresponds to the receptor-binding domain. Ephrin-B1 has been shown to bind EphA3, EphB1, EphB2, EphB3, and EphB4. The extracellular domains of human and mouse ephrin-B1 share 94% amino acid identity.

Supplier: Rockland Immunochemical

Sepharose™ protein A/G is a suspension of sepharose beads containing binding domains from both protein A (from Staphylococcus aureaus) and protein G (from Streptococcus sp.) which is used for immunoprecipitation and purification of monoclonal antibodies.

Supplier: Prosci

Annexin A13 (ANXA13) belongs to the annexin family which plays a role in phospholipase inhibition, cytoskeletal interactions, intracellular signal transduction pathways and regulation of cellular growth. ANXA13 contains four annexin repeats and a pair of annexin repeats may form one binding site for calcium and phospholipid. ANXA13 is highly expressed in intestinal and kidney epithelial cells. The specific function of ANXA13 has not yet been determined; however it is associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes.

Supplier: Prosci

Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.

Supplier: Thermo Scientific

Purified (unconjugated) Thermo Scientific Pierce Recombinant Protein L is useful as the basis for preparing various kinds of probes or affinity media for detection or purification of mouse and human antibodies in immunoassays and antibody purification protocols.

Supplier: Prosci

E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.

Supplier: Prosci

CD112 is a type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. It comprises one Ig-like V-type domain and two Ig-like C2-type domains in the extracellular region. The V domain is believed to mediate nectin binding to its ligands. Nectin2 is known to bind the pseudorabies virus, and herpes simplex virus2 (HSV2), involving in cell to cell spreading of these viruses. It does not bind poliovirus. As a homophilic adhesion molecule, CD112 is found concentrated in adherens junctions, and exists on neurons, endothelial cells,epithelial cells and fibroblasts. CD112 has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226/CD112 mediates cytotoxicity and cytokine secretion by T and NK cells. The costimulatory responses may be a critical component in allergic reactions and may therefore become targets for anti-allergic therapy.

Supplier: Prosci

Interleukin 6 (IL-6) is also known as HGF, BSF2,HSF, IFNB2 and IL-6, originally identified as a B cell differentiation factor, is a multifunctional cytokine that regulates immune responses, hematopoiesis, acute phase responses, and inflammatory reactions.It is secreted by T cells, macrophages , monocytes, fibroblasts,endothelial cells,et.al. to stimulate immune response to trauma, especially burns or other tissue damage leading to inflammation. Interleukin 6 has been shown to interact with interleukin-6 receptor and glycoprotein. IL-6 is relevant to many disease processes such as diabetes,atherosclerosis, depression,Alzheimer's Disease,systemic,lupus erythematosus,prostate cancer and rheumatoid arthritis. Advanced/metastatic cancer patients have higher levels of IL-6 in their blood.Hence there is an interest in developing anti-IL-6 agents as therapy against many of these diseases.

Supplier: Prosci

CD85 antigen-like family member J (CD85J) is also known as Leukocyte immunoglobulin-like receptor subfamily B member 1 (LILRB1 or LIR-1), Immunoglobulin-like transcript 2 (ILT-2), Monocyte/macrophage immunoglobulin-like receptor 7 (MIR7), which belongs to leukocyte immunoglobulin-like receptor (LIR) family. CD85J / LILRB1 Contains 4 Ig-like C2-type (immunoglobulin-like) domains. CD85J / LIR-1 is expressed predominantly on B-cells and monocytes. CD85J is receptor for class I MHC antigens and recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles and is also receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. CD85J / LILRB1 interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. CD85J / LILRB1 inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.

Supplier: Prosci

Interleukin 1 receptor-like 1 (IL1RL1) is also known as ST2, DER4, FIT-1, IL33R, ST2L, ST2V, which belongs to the interleukin-1 receptor family. IL1RL1 contains three Ig-like C2-type (immunoglobulin-like) domains and one TIR domain. IL1RL1 is receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 possibly involved in helper T-cell function. IL1RL1 can interact with MYD88, IRAK1, IRAK4, and TRAF6.

Supplier: Prosci

Fibronectin Leucine Rich Transmembrane protein 2 (FLRT2) is a member of the fibronectin leucine rich transmembrane protein (FLRT) family. The three fibronectin leucine-rich repeat transmembrane (FLRT) proteins: FLRT1, FLRT2 and FLRT3, all contain 10 leucine-rich repeats (LRR), a type III fibronectin (FN) domain, followed by the transmembrane region, and a short cytoplasmic tail. FLRT proteins have dual properties as regulators of cell adhesion and potentiators of fibroblast growth factor (FGF) mediated signalling. The fibronectin domain of all three FLRTs can bind FGF receptors. This binding is thought to regulate FGF signaling during development. The LRR domains are responsible for both the localization of FLRTs in areas of cell contact and homotypic cell cell association. FLRT2 is expressed in a subset of the sclerotome, adjacent to the region that forms the syndetome, suggesting its involvement in the FGF signalling pathway.

Supplier: Prosci

Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

Supplier: Prosci

Transforming growth factor beta 2 (TGF- beta 2) is a member of TGF-beta superfamily that shares a characteristic cysteine knot structure. Mice with TGF- beta 2 gene deletion show defects in development of cardiac, lung, craniofacial, limb, spinal column, eye, inner ear and urogenital systems. All TGF- beta isoforms signal via the same heteromeric receptor complex, consisting of a ligand binding TGF- beta receptor type II (T beta R-II), and a TGF- beta receptor type I (T beta R-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF- beta expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

Supplier: Prosci

Fibroblast growth factors (FGFs) constitute a family of heparin-binding polypeptides involved in the regulation of biological responses such as growth, differentiation and angiogenesis. The biological effects of FGFs are mediated by four structurally related receptor tyrosine kinases denoted FGFR1, FGFR2, FGFR3 and FGFR4. FGF-1 [FGF-acidic; ECGF; HBGF-1] is a powerful mitogen of cells of mesodermal, ectodermal and endodermal origin. FGF-1 association with heparan sulfate is a prerequisite for activation of FGF receptors. FGF-1 plays a role in various stages of development and morphogenesis as well as in angiogenesis and wound healing processes. Recent data indicate a role of FGF-1 in inflammation and obesity. FGF-1 is selectively induced in fat cells by high-fat diet feeding and established the PPARgamma-FGF-1 axis as a critical pathway that regulates adipose tissue remodeling.

Supplier: Prosci

Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is produced by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, GM-CSF is also a growth factor for erythroid, megakaryocyte and eosinophil progenitors. On mature hematopoietic, monocytes/ macrophages and eosinophils. GM-CSF has a functional role on non-hematopoitic cells. It can induce human endothelial cells to migrate and proliferate. Additionally, GM-CSF can also stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines.

Supplier: Prosci

Cytotoxic and Regulatory T-Cell Molecule (CRTAM) is a member of Nectin family under the immunoglobulin superfamily that is expressed by activated CD8+ and NK T cells. CRTAM is found in spleen, thymus, small intestine, peripheral blood, and it is highly expressed by Purkinje cells of the cerebellum. CRTAM is a type I transmembrane glycoprotein containing one Ig-like C2-type domain and one Ig-like V-type domain in its extracellular domain, while its cytoplasmic region shows a potential class I PDZ domain. CRTAM is expressed as a homodimer on the cell surface but does not show homotypic binding in trans. The high affinity of CRTAM/IGSF4 adhesion allows CRTAM to disrupt IGSF4 homotypic interactions. IGSF4 and T cell receptor coengagement of CD8+ cells expressiong CRTAM induces increased IFN gamma or IL-22 production.

Supplier: Prosci

The most prominent members of the interleukin-1 (IL-1) superfamily are IL-1alpha and IL-1beta. They lack a signal peptide and are secreted by an unconventional, endoplasmic reticulum-Golgi-independent mechanism. IL-1alpha was reported to be more widely and constitutively expressed and has intracellular functions, but also acts locally in a membrane-bound form by activating IL-1R1. Additionally, passive release of IL-1alpha upon cell death can trigger a sterile inflammatory response to dying cells. The cleavage of IL-1alpha is not mediated by caspase-1 and is not required for binding to IL-1R1. Recently it has been observed that all activators of the inflammasome NLRP3/NALP3 induce the simultaneous secretion of IL-1alpha and IL-1beta. Although most activators fully rely on the inflammasome for IL-1alpha secretion, some induce the processing and secretion of IL-1alpha in an inflammasome-independent manner.

Supplier: Prosci

Glial Cell Line-Derived Neurotrophic Factor Family Receptor alpha-1 (GDNFR alpha1) is a glycosylphosphatidylinositol (GPI) linked cell surface protein belonging to GDNF-family receptor alpha subtype which consists of at least four members. GFR alpha1and GFR alpha2 are the cognate co-receptor for the neurotrophic factor neurturin mediating the NRTN-induced autophosphorylation and activation of the RET tyrosine kinase receptor. Soluble GFR alphas released enzymatically from the cell surface by phosphatidylinositol phospholipase C, as well as recombinantly produced soluble GFR alpha1, can also bind with high affinity to GDNF and trigger the activation of Ret tyrosine kinase. Human GFR alpha1 shares 93% amino acid identity with mouse GFR alpha1.The expression of the various GFR alphas are differentially regulated in the central and peripheral nervous system, suggesting complementary roles for the GFR alphas in mediating the activities of the GDNF family of neurotrophic factors.

Supplier: Rockland Immunochemical

Supplier: Prosci

Tumor necrosis factor receptor superfamily member 1A (Tnfrsf1a) is a member of the tumor necrosis factor receptor superfamily. Tnfrsf1a is one of the major receptors for the tumor necrosis factor-alpha. It can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome

Supplier: Prosci

Interleukin-18 is a secreted protein and it belongs to the IL-1 family. IL-18 is a proinflammatory cytokine and produced by macrophages and other cells. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL-4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity. After stimulation with IL-18, natural killer (NK) cells and certain T cells release another important cytokine called interferon- gamma (IFN- gamma ) or type II interferon that plays an important role in activating the macrophages or other cells.

Supplier: Prosci

The Galectin family of proteins (with specificity for Nacetyllactosamine containing glycoproteins) consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members that share structural similarities in their carbohydrate recognition domains (CRD) have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins (1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain, and the tandem repeat Galectins (4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.