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Supplier: Prosci

CD152 (CTLA-4) and CD28, together with their ligands B7-1 and B7-2, constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD152 and CD28 are structurally
homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD152 and CD28 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an
intracellular domain. CD152 and CD28 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. CD152 was originally identified as a gene that was specifically expressed by
cytotoxic T lymphocytes. However, CD152 transcripts have since been found in both Th1 and Th2, and CD4+ and CD8+ T cell clones. Whereas, CD28 expression is constitutive on the surfaces of 95% of CD4+
T cells and 50% of CD8+ T cells and is down regulated upon T cell activation, CD152 expression is upregulated rapidly following T cell activation and peaks approximately 24 hours following activation.
Although both CD152 and CD28 can bind to the same ligands, CD152 binds to B71 and B72 with 20-100-fold higher affinity than CD28.

Supplier: Thermo Scientific Chemicals

Molecular Formula: C63H83N17O14
Formula Weight: 1302.44
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White to off-white
Solubility: Soluble in water at 1mg/ml
MDL No.: MFCD03452696

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-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant human PDGF-BB is a 24.3 kDa disulfide-linked homodimer of two B chains (218 total amino acids). Recombinant murine PDGF-BB is a 24.4 kDa disulfide-linked homodimer of two B chains (218 total amino acids).

Supplier: New England Biolabs (NEB)

Fetuin is a glycoprotein containing sialylated N-linked and O-linked glycans that can be used as a positive control for endoglycosidase enzymes.

Supplier: Prosci

Oxidized Low-Density Lipoprotein Receptor 1 (Ox-LDL Receptor 1) is a secreted, single-pass type II membrane protein which belongs to the C-type lectin superfamily. Ox-LDL Receptor 1 is expressed at high levels in endothelial cells and vascular-rich organs such as placenta, lung, liver, brain, aortic intima, bone marrow, spinal cord and substantia nigra. The expression of Ox-LDL Receptor 1 is induced by inflammatory cytokines such as TNF, IFNG and IL6 by pathological conditions, such as hyperlipidemia, hypertension and diabetes mellitus. Ox-LDL Receptor 1 mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (OxLDL) by vascular endothelial cells. Ox-LDL Receptor 1 association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. Ox-LDL Receptor 1 also binds to oxLDL, which acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. It also participates in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation.

Supplier: Prosci

Interleukin-21 receptor (IL-21R) is a type I transmembrane glycoprotein within the class I cytokine receptor family, type 4 subfamily. Complex formation between IL-21R and the common gamma chain (gammac) is required for signaling. IL-21R is expressed mainly on B cells (highest on mature, activated, follicular and germinal center B cells), NK cells and activated T cells, but is also found on dendritic cells, alternatively activated macrophages, intestinal lamina propria fibroblasts and epithelial cells and keratinocytes. B cell IL-21R engagement induces Blimp1 (which mediates plasma cell differentiation) and is important for memory responses. IL-21R engagement on mouse NK cells enhances their cytotoxic activity and IFN-gamma production. IL-21R engagement on CD8+ T cells aids control of viral infection and tumor growth; IL-21R is also necessary for sufficient numbers of regulatory T cells to combat chronic inflammation. IL-21R expression is often upregulated in allergic skin inflammation, systemic lupus erythematosus and diffuse large B cell lymphoma (DLBCL).

Supplier: Thermo Scientific Chemicals

CAS No.: 169332-60-9
Molecular Formula: C20H30N4O11
Formula Weight: 502.47
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
MDL No.: MFCD00671412

Supplier: MilliporeSigma

Cell-permeable derivative of glutathione (GSH) that undergoes hydrolysis by intracellular esterases thereby increasing intracellular GSH concentration in many tissues and cell types. Effective transport of GSH-MEE has been used to protect cells against radiation damage, oxidants, and various toxic compounds including heavy metals. A protective agent against cellular damage such as in cataracts and mitochondrial degeneration.

Supplier: Prosci

C-X-C chemokine receptor type 4 is also known as fusin or CD184 (cluster of differentiation 184), CXCR4, CD184, D2S201E, FB22, HM89, HSY3RR, LAP3, LCR1, LESTR, NPY3R, NPYR, NPYRL, NPYY3R or WHIM. CXCR-4 is an alpha-chemokine receptor specific for stromal-derived-factor-1 (SDF-1 also called CXCL12), a molecule endowed with potent chemotactic activity for lymphocytes. This receptor is one of several chemokine receptors that HIV isolates can use to infect CD4+ T cells. HIV isolates that use CXCR4 are traditionally known as T-cell tropic isolates. Typically, these viruses are found late in infection. It is unclear as to whether the emergence of CXCR4 using HIV is a consequence or a cause of immunodeficiency.CXCR4 is upregulated during the implantation window in natural and hormone replacement therapy cycles in the endometrium, producing, in presence of a human blastocyst, a surface polarization of the CXCR4 receptors suggesting that this receptor is implicated in the adhesion phase of human implantation. SDF-1 and CXCR4 were believed to be a relatively "monogamous" ligand-receptor pair (other chemokines tend to use several different chemokine receptors in a fairly "promiscuous" manner). Recent evidence demonstrates ubiquitin is also a natural ligand of CXCR4. Chronic exposure to THC increased T lymphocyte CXCR4 expression on both CD4+ and CD8+ T lymphocytes. Drugs that block the CXCR4 receptor appear to be capable of "mobilizing" hematopoietic stem cells into the bloodstream as peripheral blood stem cells.

Supplier: Prosci

Insulin-like growth factor 1 (IGF-1) is also known as somatomedin C, IGF1A, IGFI, sulfation factor, and is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons. IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. IGF-1 binds to at least two cell surface receptors: the Insulin-like growth factor 1 receptor, abbreviated as "IGF1R", and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. Its primary action is mediated by binding to its specific receptor IGF1R, present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death. Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6). Specific references are provided for interactions with IGFBP3, IGFBP4 and IGFBP7.

Supplier: MilliporeSigma

Native α1-acid glycoprotein from human plasma. Glycoprotein used for the study of the structure of oligosaccharide units. Consists of 40 - 45% carbohydrate. Present in human plasma at concentrations of 55 - 140 mg/100 mL. Clinically, α1-AG is an acute-phase reactant that, together with haptoglobin, indicates acute inflammation. Selectively suppresses the augmentation of NK cell activity by IFN-α and IFN-ɣ.

Supplier: Prosci

CD28 and CTLA-4 together with their ligands, CD80 (B7-1) and CD86 (B7-2), constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD28 and CTLA-4 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD28 and CTLA-4 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. The genes encoding these two molecules are closely linked on human chromosome 2 and mouse chromosome 1. Mouse CD28 is expressed constitutively on virtually 100% of mouse T cells and on developing thymocytes. Cell surface expression of mouse CD28 is downregulated upon ligation of CD28 in the presence of PMA or PHA. In contrast, CTLA-4 is not expressed constitutively but is upregulated rapidly following T cell activation and CD28 ligation. Cell surface expression of mouse CTLA-4 peaks approx.y 48 hours after activation. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28. CD28/B7 interaction has been shown to prevent apoptosis of activated T cells via the upregulation of bcl-XL. CD28 ligation has also been shown to regulate Th1/Th2 differentiation.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

Interleukin-20 (IL-20) is a member of the IL-10 family of regulatory cytokines that includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences but they are dissimilar in their biological functions. IL-20 exhibits approximately 28% amino acid identity with IL-10 and 76% amino acid identity with mouse IL-20. There are two heterodimeric receptor complexes for IL-20. The first is composed of IL-20 R alpha and IL-20 R beta . The second is composed of IL-22 R and IL-20 R beta . Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24, the IL-20 R alpha/IL-20 R beta complex is shared with both IL-19 and IL-24. IL-20 has been shown to initiate transduction cascades involving STAT3 and stimulates the induction of pro-inflammatory genes including TNF- alpha and MCP-1. Initial functional studies using transgenic mice suggest that IL-20 has the ability to regulate skin development. The over-expression of both human and mouse forms of IL-20 results in keratinocyte hyper-proliferation, abnormal epidermal differentiation, and neonatal lethality. In humans, IL-20 and its receptors are up-regulated in psoriatic skin, and polymorphisms in the IL-20 gene have been associated with plaque-type psoriasis. IL-20 may also have a role in hematopoiesis. It enhances the proliferation of multi-potential progenitors in vitro and increases their numbers and cell cycling status in IL-20 transgenic mice. IL-20 is also shown to suppress COX-2 and PGE2 and acts as an inhibitor of angiogenesis in model systems.

Supplier: Prosci

The Fas is also known as FAS receptor (FasR), apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs) are found in most mammals. Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor. This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain. Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.

Supplier: Thermo Scientific

HRP-Conjugated Streptavidin consists of streptavidin protein that is covalently conjugated to horseradish peroxidase (HRP) enzyme (RZ > 3.0). Streptavidin binds to biotin and the conjugated HRP provides enzyme activity for detection using an appropriate substrate system. This particular product has been used primarily in sandwich ELISA applications to provide consistent measurement of biotinylated detection antibodies.

Formulation: Provided in a conjugate stabilizer containing 0.1% ProClin Compound as a preservative.
Shipped on cold packs.
Application: ELISA: to be used with biotin-labeled detection antibodies. Recommended dilution range is from 1:4,000 to 1:20,000. The optimal dilution must be determined empirically for each specific application. Prepare dilutions immediately before use.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

Receptors for the Fc region of immunoglobin G (Fc gamma R) are divided into three classes and Fc gamma RIII is a multifunctional, low/intermediate affinity receptor. In humans, Fc gamma RIII is expressed as two distinct forms (Fc gamma RIIIA and Fc gamma RIIIB) that are encoded by two different but highly homologous genes in a cell type-specific manner. Fc gamma RIIIB is a low-affinity, GPI-linked receptor expressed by neutrophils and eosinophils, whereas Fc gamma RIIIA is an intermediate affinity polypeptide-anchored transmembrane glycoprotein expressed by a subset of T lymphocytes, natural killer (NK) cells, monocytes, and macrophages. The Fc gamma RIIIA receptor is involved in phagocytosis, secretion of enzymes, inflammatory mediators, antibody-dependent cellular cytotoxicity (ADCC), mast cell degranulation, and clearance of immune complexes. Fc gamma RIIIA has an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain and delivers an activation signal in the immune responses. Aberrant expression or mutations in this gene is implicated in susceptibility to recurrent viral infections, systemic lupus erythematosus, and alloimmune neonatal neutropenia. In humans, it is a 50 -70 kD type I transmembrane activating receptor. The Fc gamma RIIIA cDNA encodes 254 amino acid including a 16aa signal sequence, 191 amino acid ECD with two C2-type Ig-like domains, five potential N-glycosylation sites, a 22 amino acid transmembrane sequence and a 25 amino acid cytoplasmic domain.

Supplier: Prosci

Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Human Fc gamma Rs are divided into three classes designated Fc gamma RI (CD64), Fc gamma RII (CD32), and Fc gamma RIII (CD16), which generate multiple isoforms, are recognized. The activating­ type receptor either has or associates non­covalently with an accessory subunit that has an immunoreceptor tyrosine­based activation motif (ITAM) in its cytoplasmic domain. Fc gamma RI binds IgG with high affinity and functions during early immune responses, whereas Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. Three genes for human Fc gamma RII (A, B, and C) and one for mouse (Fc gamma RIIB), encoding type I transmembrane proteins with ITAM motifs (Fc gamma RII A and C) or ITIM motifs (Fc gamma RIIB) in their cytoplasmic domains, have been identified. Human CD32, also known as Low affinity immunoglobulin gamma Fc region receptor II-a (IgG Fc receptor II-a), Fc gamma RII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcR gamma , CD32a (Fc gamma RII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fc gamma RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors.

Supplier: Abnova

The Recombinant Human HIST2H3A Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human HIST2H3A Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: Abnova

The Recombinant Human PKN3 Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human PKN3 Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: Abnova

Human ADAM5P full-length ORF (AAH67864.2, 1 a.a. to 412 a.a.) recombinant protein with GST-tag at N-terminal.

Supplier: Abnova

The Recombinant Human MTF2 Protein from Novus Biologicals is derived from Wheat germ. The Recombinant Human MTF2 Protein has been validated for the following applications: Western Blot, ELISA, SDS-Page, Protein Array, Immunoaffinity Purification.

Supplier: New England Biolabs (NEB)

NEBExpress GamS nuclease inhibitor is a recombinant protein that inhibits Exonuclease V (RecBCD) activity and stabilizes linear DNA templates in E. coli based in vitro protein synthesis reactions.