You searched for: Proteins and Peptides

Supplier: Prosci

R-spondin-1 is also known as Roof plate-specific Spondin 1 (RSPO1) and cysteinerich and single thrombospondin domain containing protein 3 (Cristin 3), is a secreted protein which belongs to the R-Spondin family and encodes a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. All Rspondins regulate Wnt/?-catenin signaling, but have distinct expression patterns. Like other R-Spondins, R-Spondin-1 contains two adjacent cysteinerich furinlike domains (aa 34-135) with one potential N-glycosylation site, followed by a thrombospondin (TSP1) motif (aa 147-207) and a region rich in basic residues (aa 211-263). Only the furinlike domains are needed for ?-catenin stabilization. A putative nuclear localization signal at the C-terminus may allow some expression in the nucleus. Potential isoforms of 200 and 236 aa have an alternate, shorter N-terminus or are missing aa 146-208, respectively. R-Spondin-1 is expressed in early development at the roof plate boundary and is thought to contribute to dorsal neural tube development. Human RSPO1 disruption results in a recessive syndrome characterized by XX sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin. It has been shown that the complete female-to-male sex reversal is due to the absence of the testis-determining gene, SRY. R-Spondin-1 regulates Wnt/?-catenin by competing with the Wnt antagonist DKK1 for binding to the Wnt co receptors, Kremen and LRP6, reducing their DKK1 mediated internalization. Reports differ on whether R-spondin 1 binds LRP6 directly.

Supplier: Rockland Immunochemical

1mg. Antibody Concentration: 1 mg/mL. Biotin/Protein Ratio: 10-20 BAC molecules per Human Albumin molecule. Buffer: 0.02M potassium phosphate, 0.15M sodium chloride, pH 7.2. Stabilizer: 10 mg/mL Bovine Serum Albumin IgG and protease free. Lyophilized.

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: MilliporeSigma

A highly selective, competitive, and irreversible inhibitor of caspase-1 and caspase-4

Supplier: Prosci

Mouse Cxcl12 is a secreted and highly conserved protein which belongs to the intercrine alpha (chemokine CxC) family.CXCL12 is widely expressed in various organs including brain, kidney, skeletal muscle, heart, liver, and lymphoid organs. Cxcl12 activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. It also binds to atypical chemokine receptor ACKR3 which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Cxcl12 has several critical functions during embryonic development such as B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Cxcl12 plays an important role in acting as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. It stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. It also plays a protective role after myocardial infarction, induces down-regulation and internalization of ACKR3 expressed in various cells and stimulates the proliferation of bone marrow-derived b progenitor cells in the presence of IL-7 as well as growth of the stromal cell-dependent B-cell clone DW34 cells.

Supplier: Prosci

T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.

Supplier: Prosci

CD152 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

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: Prosci

Human VEGF121, also known as Vascular endothelial growth factor A, VEGFA, Vascular permeability factor, VPF and VEGF, is a homodimeric, heparin-binding glycoprotein which belongs to the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family. VEGF-A is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis, permeabilization of blood vessels and endothelial cell growth, increasing microvascular permeability, promoting cell migration and inhibiting apoptosis. Alternatively spliced transcript variants of VEGF-A encod either secreted or cell-associated isoforms. The lymphangiogenesis may be promoted by upregulation of VEGF121, which may in turn act in part via induction of VEGF-C. It binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.

Supplier: Prosci

Interleukin-21 (IL-21) is a key factor in the transition between innate and adaptive immune responses secreted by activated T cells. The IL-21 receptor (IL-21R) is expressed in lymphoid tissue, in particular by NK, B, T and dendritic cells, macrophages and endothelial cells. Recent evidence suggests that IL-21 plays a supportive role in the proliferation of T and B cells and influences the cytolytic activity of natural killer cells. IL-21 has been shown to up-regulate genes associated with innate immunity and to inhibit the differentiation of naive T helper cells. IL-21 specifically inhibits IFN-gamma production from developing TH1 cells and is preferentially expressed by TH2 cells. Furthermore IL-21 has been identified as a growth and survival factor for human myeloma cells. IL-21/IL-21R interactions have a unique role in sequentially activating both innate and adaptive immune responses against poorly immunogenic tumors, leading to tumor rejection that is perforin dependent but IFN-gamma independent.

Supplier: Prosci

Transforming growth factor beta 1 ( TGFB1) is also known as TGF-?1, CED, DPD1, TGFB. is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation and apoptosis. The TGFB1 protein helps control the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis). The TGFB1 protein is found throughout the body and plays a role in development before birth, the formation of blood vessels, the regulation of muscle tissue and body fat development, wound healing, and immune system function. TGFB1 is particularly abundant in tissues that make up the skeleton, where it helps regulate bone growth, and in the intricate lattice that forms in the spaces between cells (the extracellular matrix). Within cells, this protein is turned off (inactive) until it receives a chemical signal to become active. TGFB1 plays an important role in controlling the immune system, and shows different activities on different types of cell, or cells at different developmental stages. Most immune cells (or leukocytes) secrete TGFB1. TGFB1 has been shown to interact with TGF beta receptor 1, LTBP1, YWHAE, EIF3I and Decorin.

Supplier: New England Biolabs (NEB)

Recombinant Albumin, Molecular Biology Grade, is a non-bovine derived albumin that can serve as an alternative to Bovine Serum Albumin (BSA).

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: Prosci

Leukocyte-Associated Immunoglobulin-Like Receptor 1 (LAIR1) is a single-pass type I membrane protein. LAIR1 expressed on the majority of peripheral mononuclear cells, including natural killer (NK) cells, T-cells, B-cells, monocytes, and dendritic cells, highly in naive T-cells and B-cells. As an inhibitory receptor, LAIR1 plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. LAIR1 plays inhibitory role independently of SH2-containing phosphatases and modulates cytokine production in CD4+ T-cells. It down-regulates IL2 and IFNG production while inducing secretion of transforming growth factor beta, also down-regulates IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. LAIR1 inhibits the differentiation of peripheral blood precursors towards dendritic cells. It also restrains proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells.

Supplier: MilliporeSigma

Fully-functional ubiquitin with an N-terminal glutathione S-transferase (GST) tag. Useful for ubiquitination of protein substrates and subsequent glutathione affinity purification of ubiquitinated molecules. Can also be used for immunodetection of conjugates using GST antibodies. Facilitates the visualization of polyUb chains due to larger ladder intervals.

Supplier: MilliporeSigma

Activates a variety of immune defense mechanisms by interactions with polymorphonuclear leukocytes, T cells, antibody-producing B lymphocytes, fibroblasts, and hematopoietic bone marrow cells. Activity is not species-specific. Induces apoptosis in human blood and bone marrow neutrophils and in endothelial cells. Increases iNOS levels in vascular smooth muscle cells. Involved in pathophysiological processes of several chronic and acute diseases. Stimulates stress activated protein (SAP) kinase. Biological activity: ED50=20–50pg/mL as measured in a cytotoxicity assay with the TNF-[alpha]-susceptible murine L-929 cells line in the presence of Actinomycin D (80055-066).

Supplier: Thermo Scientific Chemicals

CAS No.: 71977-09-8
Molecular Formula: C63H97N17O14S
Formula Weight: 1348.63
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
MDL No.: MFCD00076781

Supplier: Thermo Scientific Chemicals

CAS No.: 9076-44-2
Molecular Formula: C31H41N7O6
Formula Weight: 604.90
Physical Form: Powder
Appearance: White to off-white
Melting Point: 276-278°
MDL No.: MFCD00071059

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: MilliporeSigma

A potent, cell-permeable and irreversible inhibitor of caspase-5 (ICErel-III, TY) as well as caspase-1 and caspase-4.

Supplier: Prosci

Human Interleukin 15 (IL-15) is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL15 receptor (IL-15RA) with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each other's activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs. Mature Human IL-15 shares 70% amino acid sequence identity with Mouse and Rat IL-15.

Supplier: Thermo Scientific Chemicals

CAS No.: 154674-81-4
Molecular Formula: C33H42N4O10
Formula Weight: 654.71
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
Solubility: Soluble in DMSO
MDL No.: MFCD00798794

Supplier: Thermo Scientific Chemicals

CAS No.: 80448-90-4
Molecular Formula: C99H156N32O22
Formula Weight: 2146.49
Storage Temperature: -30°C to -10°C
Physical Form: Solid
Appearance: White to off-white
MDL No.: MFCD00076351

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: 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

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

Supplier: Prosci

Mouse Programmed cell death 1 ligand 1(Cd274，PD-L1), is a member of the growing B7 family of immune proteins.It involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.B7-H1 has been identified as one of two ligands for programmed death1 (PD1), a member of the CD28 family of immunoreceptors. B7-H1 is constitutively expressed in several organs such as heart, skeletal muscle B7-H1 expression is upregulated in a small fraction of activated T and B cells and a much larger fraction of activated monocytes. The costimulatory function of B7-H1 is critical for enhancing maturation and differentiation of T-cells in lymphoid organs.B7-H1 expression is also induced in dendritic cells and keratinocytes after IFN gamma stimulation. Interaction of B7-H1 with PD1 results in inhibition of TCR-mediated proliferation and cytokine production. The B7-H1:PD1 pathway is involved in the negative regulation of some immune responses and may play an important role in the regulation of peripheral tolerance.

Supplier: MilliporeSigma

Principal pigment of bile and one of the major end products of hemoglobin decomposition. Contains conjugated double bonds and reactive hydrogen atoms. Proposed to serve as a physiological antioxidant. Reported to pass through the blood-brain barrier and exert significant antioxidant effects in the brain. Extinction coefficient (454nm, trichloromethane): 59,100–62,300 M-1cm-1.