You searched for: Proteins and Peptides

Supplier: G-Biosciences

A selection of individual protease inhibitors are offered for researchers who wish to design their own cocktails, supplement existing cocktails, or screen for specific proteases

Supplier: Thermo Scientific Chemicals

CAS No.: 86073-88-3
Molecular Formula: C60H73N15O13
Formula Weight: 1212.31
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
MDL No.: MFCD00133497

Supplier: MilliporeSigma

A potent, specific, and reversible inhibitor of caspase-1 (Ki=200pM for human recombinant caspase-1) and caspase-4

Supplier: MilliporeSigma

In 100mM NaCl, 50mM HEPES, 10mM DTT, 1mM EDTA, 10% glycerol, 0.1% CHAPS, pH 7.4

Supplier: New England Biolabs (NEB)

ET SSB (Extreme Thermostable Single-Stranded DNA Binding Protein) is a single-stranded DNA binding protein isolated from a hyperthermophilic microorganism, which remains fully active after incubation at 95°C for 60 minutes. Due to the extreme thermostability, ET SSB can be used in applications that require extremely high temperature conditions, such as nucleic acid amplification and sequencing.

Supplier: Prosci

Epidermal growth factor (EGF) is a growth factor and the founding member of the EGF family. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. These receptors undergo a complex pattern of ligand induced homo or heterodimerization to transduce EGF family signals. EGF binds to the receptor EGFR stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity initiates a signal transduction cascade that results in a variety of biochemical changes within the cell, including a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR, which lead to DNA synthesis, cell growth, proliferation and differentiation. Other biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.

Supplier: Prosci

Interleukin-15 receptor subunit alpha, also known as Il15ra, is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits (Common gamma chain, or gamma c) to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells. Human Il15ra shares 45% amino acid sequence homology with the mouse form of the receptor. Eight isoforms of IL-15 R alpha mRNA have been identified, resulting from alternative splicing events involving different exons.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.

Supplier: MilliporeSigma

Trypsin inhibitor, soybean (CAS 9035-81-8) is a reversible inhibitor of trypsin that binds to trypsin in a stoichiometric, pH-dependent manner (Kd = 500 nM at pH 7.8).

Supplier: Thermo Scientific Chemicals

Molecular Formula: C152H243N47O44S4
Formula Weight: 3561.09
Storage Temperature: -30°C to -10°C
Physical Form: Solid
Appearance: White to off-white
Solubility: Soluble in water at 1mg/ml
MDL No.: MFCD07369024

Supplier: Prosci

Interleukin-12 (IL12) is also known as natural killer cell stimulatory factor (NKSF), cytotoxic lymphocyte maturation factor (CLMF) , is a heterodimeric cytokine encoded by two separate genes, IL-12A (p35) and IL-12B (p40). IL12 is naturally produced by dendritic cells, macrophages and human B-lymphoblastoid cells (NC-37) in response to antigenic stimulation. IL-12 is involved in the differentiation of naive T cells into Th0 cells and plays an important role in the activities of natural killer cells and T lymphocytes.IL-12 also has anti-angiogenic activity, which means it can block the formation of new blood vessels.
Interleukin-12 subunit beta (IL12B) also known as NKSF2, CLMF2 and P40. Interleukin-12 subunit beta has been shown to interact with IL23. A large excess of monomeric IL12B is also secreted by the cells producing IL12, and exhibits no demonstrable biological activity. Overexpression of IL12B gene has been shown to be associated with the pathogenesis of multiple sclerosis. In addition, studies have revealed that the promoter polymorphism of this gene is implicated in the severity of atopic and non-atopic asthma in children.

Supplier: Prosci

Interleukin-15 (IL-15) has a broad spectrum of biological activities. It is crucial for the development, proliferation, survival and differentiation of multiple cells from both innate and adaptive immune systems. IL-15 up-regulation has a central role in the development of several autoimmune or chronic inflammatory disorders. Targeting IL-15 or its receptor may have a valuable impact on the treatment of immune-mediated diseases. IL-15 participates in the development of important immune antitumor mechanisms. It activates CD8(+) T cells, natural killer (NK) cells, NK T cells, and can promote the formation of antitumor antibodies. IL-15 can also protect T effector cells from the action of T regulatory cells and reverse tolerance to tumor-associated antigens. In pre-clinical studies IL-15 has been found to demonstrate potentiated antitumor effects following pre-association with IL-15Ralpha, or when used in combination with chemotherapy, adoptive therapy, monoclonal antibodies, and tumor vaccines.
Application: Useful for immunofluorescent staining and flow cytometric analysis to identify and enumerate IL-15Ralpha expressing cells within mixed cell populations.

Supplier: LONZA PHARMA - BIOSCIENCE CA

Human Transferrin are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Human transferrin is encoded by the TF gene. Human Transferrin glycoproteins bind iron very tightly, but reversibly and are the most important iron pool, with the highest rate of turnover (25 mg/24 h).

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: 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

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: Prosci

Interleukin-27 (IL-27) is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines. It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the cloned 28 kDa glycoprotein that is related to the p35 chain of IL-12. IL-27 is expressed by monocytes, endothelial cells and dendritic cells. IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1. IL-27 has both anti- and proinflammatory properties. As an antiinflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity. At the onset of infection, IL-27 induces an IL-12 receptor on naie CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development). Notably, IL-12 family cytokines are both induced and inhibited by bacterial products. Microbes promote IL-27 secretion through TLR4, and also block IL-27 production via C5a induction.

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: 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: 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

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 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: Abnova

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

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.