You searched for: Proteins and Peptides

Supplier: Thermo Scientific Chemicals

Useful in the prophylaxis and treatment of LPS-mediated diseases; binds to and neutralizes endotoxin from gram-negative bacteria

Supplier: Prosci

NKG2D ligand 1, also called ULBP1, is a member of UL16-binding protein (ULBP) family which has also been termed the retinoic acid early transcript 1 (RAET1) family. Unlike the classical MHC class I molecules and the MIC molecules possess alpha1, alpha2 and alpha3 domains, ULBP/RAET1 family members lack alpha3 domain. ULBP1 is recognized by the activating receptor NKG2D on the surface of cytotoxic natural killer (NK) and T cells, and then promotes the lysis of cells expressing ULBP1 which is important for the immune surveillance. ULBP1 and several other family members, ULBP2 and ULBP5, own the ability to bind the human cytomegalovirus (CMV) UL16 glycoprotein. The human CMV glycoprotein UL16 binds to intracellular ULBP1 and so inhibits its expression at the cell surface, which reduces the susceptibility of the virus-infected cell to cytotoxic destruction by NK cells. The expression of ULBP1 has been found on some tumor cells and is implicated in tumor surveillance.

Supplier: Prosci

T-cell-specific surface glycoprotein CD28(CD28) is a single-pass typeI membrane protein which contains one Ig-likeV-type (immunoglobulin-like) domain. It belongs to the immunoglobulin(Ig) superfamily. CD28 is one of the molecules expressed on T cells that provide co-stimulatory signals, which are required for T cell activation.CD28 co-stimulation is necessary for CD4 positive T-cell proliferation and survival, interleukin-2 production, and T-helper type-2 development. Human post-thymic regulatory T cells require CD28 co-stimulation to expand and maintain potent suppressive function in vivo. Apoptosis plays a key role in the age-related decline of CD28 expression and in immunosenescence. CD28 is the receptor for CD80 (B7.1) and CD86 (B7.2). When activated by Toll-like receptor ligands, the CD80 expression is upregulated in antigen presenting cells (APCs). The CD86 expression on antigen presenting cells is constitutive. CD28 is the only B7 receptor constitutively expressed on naive T cells.

Supplier: Prosci

Ectodysplasin A receptor (EDAR) is a type I transmembrane protein of the TNF- alpha receptor superfamily which plays a key role in ectodermal differentiation. EDAR was encoded by the mouse downless gene and defective in human dominant and recessive forms of autosomal hypohidrotic ectodermal dysplasia (EDA) syndrome. The extracellular domain of EDAR contains 14 cysteine residues, six of which approximate the TNFRSF cysteine-rich region, the cytoplasmic domain contains a region with homology to the death domains found in other TNFRSF members. EDAR has been suggested to be an early and important promoter of placode development in all ectodermal organs, such as uch as hair follicles, teeth and sweat glands. EDA-A1, the A1 isoform of EDA, is the EDAR ligand. EDA and EDA are implicated in appendage development by the cloning of a gene underlying hypohidrotic ectodermal dysplasia (HED) in mouse and human. HED is characterized by agenesis or malformation of ectoderm-derived appendages, such as teeth, sweat glands and hair follicles, while the skin itself develops normally.

Supplier: Prosci

The pro-inflammatory cytokine IL-1 induced cellular response requires IL-1 receptor complex including IL-1RI and IL-1RAcP. MyD88 has been identified as an adapter molecule in the IL-1 signaling pathway (1). MyD88 associates with and recruits IRAK to the IL-1 receptor complex in response to IL-1 treatment and dominant negative form of MyD88 attenuates IL-1R-mediated NF-B activation. MyD88 is also employed as a regulator molecule by IL-18 receptor and human Toll receptor (2,3), which are members in the Toll/IL-1R family of receptors. Targeted disruption of the MyD88 gene results in lose of cellular responses to IL-1 and IL-18, and MyD88-deficient mice lack responses to bacterial product LPS that employs Toll-like receptors 2 and 4 (TLR2 and TLR4) as the signaling receptors. MyD88 is a general adapter protein for the Toll/IL-1R family of receptors and plays an important role in the inflammatory response induced by cytokines IL-1 and IL-18 and endotoxin. MyD88 gene is expressed in many tissues.

Supplier: Prosci

Interleukin-6 receptor subunit beta (IL6ST) is also known as IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130 (gp130), CD130, Oncostatin-M receptor subunit alpha and Il6st,which is single-pass type I membrane protein. IL6ST /gp130 /CD130 can be found in tissues such as brain, heart, thymus, spleen, kidney, lung and liver and found in all the cell lines tested except BaF-B03.The expression of IL-6ST /gp130 is not restricted to IL6-responsive cells. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. IL6ST /CD130 can bind to IL6 /IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduce the signal. IL6ST /GP130 does not bind IL6 and may have a role in embryonic development.

Supplier: Prosci

Colony stimulating factor 1 receptor (CSF1R) is also known as macrophage colony-stimulating factor receptor (M-CSFR), CD115 Cluster of Differentiation 115 (CD115), C-FMS, CSFR, FIM2, FMS, and is a member of the type? subfamily of receptor tyrosine kinases (RTKs). CSF1R is a receptor for a cytokine called colony stimulating factor 1, The protein encoded by the CSFR1 gene is the receptor for colony stimulating factor 1, a cytokine which controls the production, differentiation, and function of macrophages. This receptor mediates most, if not all, of the biological effects of this cytokine. Ligand binding activates CSFR1 through a process of oligomerization and transphosphorylation . Mutations in CSF1R are associated with chronic myelomonocytic leukemia and type M4 acute myeloblastic leukemia. Increased levels of CSF1R1 are found in microglia in Alzheimer's disease and after brain injuries. The increased receptor expression causes microglia to become more active. Both CSF1R, and its ligand colony stimulating factor 1 play an important role in the development of the mammary gland and may be involved in the process of mammary gland carcinogenesis.

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: Prosci

Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

Supplier: Prosci

Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

Supplier: New England Biolabs (NEB)

p-Nitrophenyl Phosphate (PNPP) is a non-proteinaceous, non-specific substrate used to assay protein, alkaline and acid phosphatases.

Supplier: Prosci

Tyrosine-protein phosphatase non-receptor type substrate 1 (SHPS1) is also known as CD172 antigen-like family member A (CD172a), Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha (SIRPA or SIRP alpha) or p84, is a member of the SIRP family, and also belongs to the immunoglobulin superfamily. SIRP alpha is Ubiquitous and highly expressed in brain. SIRPA / CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA / SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function By similarity. SIRPA / MyD1 involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin and mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells.

Supplier: Rockland Immunochemical

1mg. Antibody Concentration: 1 mg/mL. Biotin/Protein: 10-20 BAC molecules per Human Transferrin molecule. 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: Rockland Immunochemical

1mg. Antibody Concentration: 1 mg/mL. Fluorochrome/Protein: 4 moles TRITC per mole of Bovine Albumin. Buffer: 0.02M potassium phosphate, 0.15M sodium chloride, pH 7.2. Stabilizer: 10 mg/mL polyethylene glycol. For research. Lyophilized.

Supplier: Prosci

Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. 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 65-70 kDa glycoprotein containing 516 amino acid residues.

Supplier: Thermo Scientific Chemicals

CAS No.: 62568-57-4
Molecular Formula: C35H48N10O15
Formula Weight: 848.81
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
Solubility: Soluble in water at 0.5mg/ml
Merck Reference: 14,3458
MDL No.: MFCD00076883

Supplier: Thermo Scientific Chemicals

CAS No.: 16941-32-5
Molecular Formula: C153H225N43O49S
Formula Weight: 3482.74
Physical Form: Powder
Appearance: White

Supplier: MilliporeSigma

White solid. Excellent buffer above pH 8.0. Purity: >98% by TLC. pKa 8.4 at 20[degree] C. CAS 556-50-3, M.W. 132.1.

Supplier: Prosci

Programmed cell death protein 1 (PD-1) is also known as CD279 and PDCD1, is a type I membrane protein and is a member of the extended CD28/CTLA-4 family of T cell regulators. PDCD1 is expressed on the surface of activated T cells, B cells, macrophages, myeloid cells and a subset of thymocytes. PD-1 has two ligands, PD-L1 and PD-L2, which are members of the B7 family. PD-L1 is expressed on almost all murine tumor cell lines, including PA1 myeloma, P815 mastocytoma, and B16 melanoma upon treatment with IFN-?. PD-L2 expression is more restricted and is expressed mainly by DCs and a few tumor lines. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-? by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. In vitro, treatment of anti-CD3 stimulated T cells with PD-L1-Ig results in reduced T cell proliferation and IFN-? secretion. Monoclonal antibodies targeting PD-1 that boost the immune system are being developed for the treatment of cancer.

Supplier: Prosci

Cluster of differentiation 14 (CD14), is a cell surface glycoprotein, and is a is a component of the innate immune system. CD14 is a myelomonocytic differentiation antigen preferentially expressed on monocytes, macrophages, and activated granulocytes. CD14 exists in two forms. Either it is anchored into the membrane by a glycosylphosphatidylinositol tail (mCD14) or it appears in a soluble form (sCD14). Soluble CD14 either appears after shedding of mCD14 (48 kDa) or is directly secreted from intracellular vesicles (56 kDa). CD14 acts as a co-receptor (along with the Toll-like receptor TLR 4 and MD-2) for the detection of bacterial lipopolysaccharide (LPS). CD14 can bind LPS only in the presence of lipopolysaccharide-binding protein (LBP). CD14 has been proposed to be involved in various biological processes, including transportation of other lipids, cell-cell interaction during different immune responses, as well as recognition of apoptotic cells. Although LPS is considered its main ligand, CD14 also recognizes other pathogen-associated molecular patterns. CD14+ cells are monocytes that can differentiate into a host of different cells. CD14 has been shown to interact with Lipopolysaccharide-binding protein.

Supplier: Prosci

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerization of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

Supplier: Prosci

CD5 is a transmembrane glycoprotein of the conserved scavenger receptor cysteine-rich (SRCR) superfamily and expressed on thymocytes, peripheral T cells and a subset of B cells (B1-a). Moreover, CD5 also was found expressed in small lymphocytic lymphoma, hairy cell leukaemia and mantle cell lymphoma cells. The long cytoplasmic tail of CD5 has no intrinsic enzymatic activity, but contains four tyrosine phosphorylation sites, including an immunoreceptor tyrosine-based (ITAM)-like motif (pseudo-ITAM) and an immunoreceptor tyrosine-based inhibitory (ITIM)-like motif (pseudo-ITIM), as well as multiple potential serine and threonine phosphorylation sites. It physically associates with the T cell antigen receptor (TCR) and B cell antigen receptor (BCR), where it negatively modulates the activation and differentiation signals transduced by these receptors. CD5 also plays an important role in protection from activation-induced cell death and in the recognition of pathogen associated molecular patterns (PAMPS) present on fungal surfaces.

Supplier: Prosci

Human Vascular endothelial growth factor receptor 1(VEGFR-1, FLT-1) is a member of the the class III subfamily of receptor tyrosine kinases (RTKs) and Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR-1 is widely expressed in human tissues including normal lung, placenta, liver, kidney, heart and brain tissues. It is specifically expressed in most of the vascular endothelial cellsand peripheral blood monocytes. VEGFR-1 contains seven Ig-like C2-type domains and one protein kinase domain. VEGFR-1is an essential receptor tyrosine kinase and plays an important role in theregulation of VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. It is also mediators of neurotrophic activity and regulators of hematopoietic development. VEGFR-1 is a receptor for VEGF, VEGFB and PGF. It has a tyrosine-protein kinase activity. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF.It may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells and promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. VEGFR-1 can also promote PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro).

Supplier: MilliporeSigma

A potent, cell-permeable, and reversible inhibitor of caspase-4 (ICErel-II, TX, ICH-2).

Supplier: Prosci

Interleukin 1 receptor, type I (IL-1R1) is an interleukin receptor that belongs to the interleukin-1 receptor family. IL-1R1 is an 80 kDa transmembrane protein that is expressed predominantly by T cells, fibroblasts, and endothelial cells. This gene along with IL1R2, IL1RL2, and IL1RL1 form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. IL-1R1 is an important mediator involved in many cytokine induced immune and inflammatory responses. It binds to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. The signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. It also binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. An IL1 receptor accessory protein that can heterodimerize with the Type I receptor in the presence of IL1 alpha or IL1β but not IL1ra, was identified. Recombinant IL1 soluble receptor Type I is a potent antagonist of IL1 action.

Supplier: Prosci

Signal Transducer and Activator of Transcription 5b (STAT5B) is a member of the STAT family of transcription factors. They are responsible for an array of cellular activities including regulating growth, survival, differentiation, motility, and the immune response. STAT5B mediates the signal transduction triggered by various cell ligands, such as IL2, IL4, CSF1, and different growth hormones. It has been shown to be involved in diverse biological processes, such as TCR signaling, apoptosis, adult mammary gland development, and sexual dimorphism of liver gene expression. Signal transduction and activator of transcription 5 (STAT5) is a member of the Jak/STAT signal transduction pathway and is activated by a variety of cytokines (IL22, IL6). STAT5 has two isoforms (A and B) that share 93% amino acid identity and bind the DNA consensus site TTCN3GAA. STAT5 mediates cytokine signaling by acting as a signal transducer in the cytoplasm and, upon phosphorylation, translocates to the nucleus and activates transcription of specific genes. STAT5 is involved in a wide array of biological processes ranging from regulating apoptosis to adult mammary gland proliferation, differentiation and survival.

Supplier: Prosci

CD40 Ligand (CD40L), renamed TNFSF5 but now also known as CD154, TRAP and gp39, is a 34-39kDa type II transmembrane glycoprotein that belongs to the TNF superfamily. As with other TNF superfamily members, CD40L will exist as a trimer, both as a membrane bound and soluble form. Multiple mutations and alternate splice forms of CD40L exist, often associated with pathology and leading to truncated or nontrimerizable forms of CD40L. CD40L binds to both CD40 and to integrin alphaIIbbeta3 (CD41). In the cell membrane, it also associates with a unique splice variant of CD28 (CD28i) that may facilitate CD40L signal transduction. CD40L is expressed by monocytes, NK cells, mast cells, basophils, smooth muscle cells, endothelial cells, dendritic cells,activated and resting B cells, plus activated platelets and CD4+ T cells. CD40L ligation of CD40 on dendritic cells (DC) initiates DC maturation and differentiation. CD40L signaling into naive B cells promotes germinal center formation and isotope switching. CD40-CD40L seems to bridge innate and adaptive immune signals.

Supplier: Prosci

CCND2，also known as G1/S-specific cyclin-D2，is a member of the highly conserved cyclin family. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Cyclins function as regulators of CDK kinases. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition. CCND2 is involved in a number of fundamental biological processes such as phosphorylating and inhibiting members of the retinoblastoma (RB) protein family including RB1 and regulating the cell-cycle during G1/S transition. It is also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G1 phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Component of the ternary complex, cyclin D2/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.

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: Prosci

Mouse Interleukin 36 beta (IL-36B)is a member of the IL-1 family of proteins. It is a cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. IL-36B is synthesized in several cells including resting and activated monocytes, and B cells. The receptor for IL-36 beta is thought to be a combination of IL-1 Rrp2 and IL-1 RAcP. Interleukin 36 beta is one part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Interleukin 36 beta are involved in a number of fundamental biological processes such as stimulating production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes, inducing expression of a number of antimicrobial peptides including beta-defensin 4 and beta-defensin 103 as well as a number of matrix metalloproteases , inducing the production of proinflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23, and activating p38 MAPK phosphorylation in BMDCs.Moreover, interleukin 36 beta may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. It plays an important role in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II and inducing the production of IFN-gamma, IL-4 and IL-17 by T helper 1 (Th1) cells, cultured CD4+ T cells and splenocytes.