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Proteins are used in routine laboratory procedures such as binding enzymes or coupling peptides to carrier proteins. These kits, mixture solutions, and collagen matrices fulfill a myriad of essential laboratory functions for developing relationships between proteins and other cellular components. The stimulating proteins offered have various amino acid arrangements and functions to fulfill any sample manipulation for testing purposes in any field.
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Description:
ESM-1, short from Endothelial cell-specific molecule 1, is expressed in lung, on the vascular capillary network within alveolar walls, and also at lower level in kidney. It is a secretory protein, and can be inducted by TNF and IL1B/interleukin-1beta, but not IL4/interleukin-4. This protein plays great roles in angiogenesis, sprouting, and may have potent implications in lung endothelial cell-leukocyte interactions.
Description:
Dectin-1 and dectin-2 are type II transmembrane proteins of the C-type lectin family. They contain single carbohydrate recognition domains (CRDs) in their extracellular region. Dectin-1 and dectin-2 are expressed in macrophages and dendritic cells. Dectin-1 recognises beta-glucans with its CRD and signals through its immunoreceptor tyrosine-based activation motif (ITAM)-like motif in the cytoplasmic domain, whereas dectin-2 recognises alpha-mannans and transduces its signal through association with the ITAM-containing Fc receptor gamma-chain.
Description:
Biglycan is a 200-350 kD proteoglycan consisting of a 45 kD core protein and two chrondroitin/dermatan sulfate glycosaminoglycan chains. Biglycan binds to TGF-ß. It also binds to collagen type I in low ionic strength (less than 3 mM phosphate) buffer. At higher ionic strengths, Biglycan does not bind to collagen type I. It enhances the inhibition effect of TGF-ß on osteoclast proliferation at a concentration of 4-20 mg/ml. It also prevents the attachment of CHO cells to fibronectin, with a 50% inhibition at 17-21 mg/ml.
Description:
NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappaB p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3.
Description:
The human Polymeric Immunoglobulin Receptor (pIgR) is a 100 kDa type I transmembrane glycoprotein. Its precursor is 764 amino acids. It contains an 18 amino acid signal sequence, a 620 amino acid extracellular region, a 23 amino acid transmembrane fragment, and a 103 amino acid cytoplasmic domain. pIgR is synthesized by secretory epithelial cells with five Ig-like domains in extracellular region, and transfer to the basolateral plasma membrane. For IgA and IgM polymers, in addition to alpha-heavy chains and light Ig chains, a short polypeptide named joining chain (J chain) is also contained and required. pIgR can bind larger polymers of IgA (pIgA) and pentameric IgM as a carrier that transports IgA and IgM across epithelium. The receptor-ligand complexes are endocytosed and transcytosed to the apical surface, then proteolytic cleavage of the sixth extracellular domain of pIgR and generate secretory IgA (SIgA), the pIgR fragment is referred to as secretory component (SC). SIgA is a important component of the mucosal immune system. SC is anti-microbial properties and protects SIgA from proteolytic degradation
Description:
Interleukin-2(IL-2) is an interleukin, a type of cytokine signaling molecule in the immune system，belongs to the IL-2 family. It is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes.
Description:
C1q R1 is also known as CD93, collectin receptor, and AA4 antigen, belongs to the Group XIV C-Type lectin family which play a role not only in cell–cell adhesion processes but also in host defence. All of them contain a C-type lectin domain, a series of epidermal growth factor like domains (EGF), a highly glycosylated mucin-like domain, a unique transmembrane domain and a short cytoplasmic tail. C1q R1 has also been identified as a hematopoietic stem cell marker.
Description:
Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many Kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen Kallikrein subfamily members located in a cluster on chromosome 19. Its encoded protein is secreted and may play a role in suppression of tumorigenesis in breast and prostate cancers. Alternate splicing of this gene results in multiple transcript variants encoding the same protein.
Description:
Cystatin-D is a protein that in humans is encoded by the CST5 gene. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a protein found in saliva and tears. The encoded protein may play a protective role against proteinases present in the oral cavity.
Description:
Mouse interleukin-16(IL-16) is a single chain non-glycosylated polypeptide. IL-16 is widely expressed in human tissues including spleen, thymus, lymph nodes, peripheral leukocytes, bone marrow and cerebellum. IL-16 plays an important role instimulating a migratory response in CD4+ lymphocytes, monocytes, and eosinophils,inducing T-lymphocyte expression of interleukin 2 receptor.It was originally identified as a CD8+ T cell-derived chemoattractant for CD4+ cells. In addition to its chemotactic properties, IL-16 has also been shown to suppress HIV-1 replication in vitro and appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. It may act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Description:
Mouse interleukin 13 (mIL-13) is a pleiotropic cytokine produced by activated Th2 cells. IL-13 induces B cell proliferation and immunoglobin production. It contains a four helical bundle with two internal disulfide bonds. Mouse IL13 shares 58% sequence identity with human protein and exhibits cross-species activity. IL13 signals via receptor IL13R (type2, IL4R) and activates STAT-6. IL13 initially binds IL-13R alpha1 with low affinity and triggers association of IL4R alpha, generating a high affinity heterodimeric receptor IL13R and eliciting downstream signals. IL13 also binds IL-13R alpha2 with high affinity, which plays a role in a negative feedback system of IL13 signaling. IL13 is an important mediator of allergic inflammation and disease.
Description:
Granulocyte-macrophage colony-stimulating factor is an enzyme that in mouse is encoded by the Csf2 gene, belongs to the GM-CSF family.CSF2 is a Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes
Description:
Mouse Interleukin-4(IL-4) is a monomeric, Th2 cytokine that shows pleiotropic effects during immune responses. It is a glycosylated polypeptide that contains three intrachain disulfide bridges and adopts a bundled four alphahelix structure. IL4 exerts its effects through two receptor complexes, Participates in at least several B-cell activation processes as well as of other cell types. IL4 is primarily expressed by Th2biased CD4+T cells, mast cells, basophils, and eosinophils. It promotes cell proliferation, survival, and immunoglobulin class switch to IgG1 and IgE in mouse B cells, acquisition of the Th2 phenotype by naïve CD4+T cells, priming and chemotaxis of mast cells, eosinophils, and basophils, and the proliferation and activation of epithelial cells. IL4 plays a dominant role in the development of allergic inflammation and asthma. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes.
Description:
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 signalling pathways in target cells linked to a pro-inflammatory response. IL-36B is synthesised 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 signalling 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.
Description:
Interleukin12 receptor subunit beta 1 (IL12RB1) is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. IL12RB1 can spontaneously form homodimers and -oligomers, which are able to bind IL12 with only low affinity. IL12 high affinity receptor complex is composed of two subunits designated IL12RB1 and IL12RB2. While IL12RB1 interacts with the IL-12p40 subunit, IL-12p35 is mainly connecting with IL12RB2. This receptor chain is also responsible for transmitting the IL12 signal into the cell. IL12RB1, to the contrary, is also part of the IL23R, where it interacts with the p40 subunit of IL23. IL12RB1 is expressed in activated T cells, NK cells and B cells.
Description:
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.
UOM:
1 * 50 µG
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,PRSI91-949EA
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