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Supplier: Peprotech
Description: IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate the proliferation and activation of T-cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. The mature human IL-17F is a homodimeric protein with a total weight of 30.1 kDa, consisting of two 133 amino acid residue chains.

Supplier: Bachem Americas
Description: Vapreotide is a potent octapeptide analog of somatostatin with selectivity for the somatostatin receptor subtypes SSTR-2 and SSTR-5. It is under investigation in the management of various disorders, including esophageal variceal bleeding, gastrointestinal and pancreatic fistulas, acromegaly, carcinoid tumors, and for the prevention of postoperative complications following pancreatic surgery.

Supplier: FUJIFILM IRVINE SCIENTIFIC, INC
Description: Platelet-derived growth factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis.  PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β, and EGF signaling.  PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells.

Supplier: FUJIFILM IRVINE SCIENTIFIC, INC
Description: Platelet-derived growth factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells.

Supplier: Peprotech
Description: Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

Catalog Number: (76303-716)
Supplier: Peprotech
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex.


Catalog Number: (75794-258)
Supplier: Prosci
Description: 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.


Catalog Number: (75794-256)
Supplier: Prosci
Description: 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.


Catalog Number: (10072-758)
Supplier: Prosci
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.


Catalog Number: (H-4902.0001BA)
Supplier: Bachem Americas
Description: Anticoagulant and antithrombotic peptides. Please see also the product family 'Hirudin Fragments and Analogs', the inhibitors N-1065, N-1215, N-1260, N-1565, and N-1970, and the anticoagulant anisindione, Q-1085.


Supplier: Biotium
Description: This MAb recognizes proteins of 19-22 kDa (reducing) and 38 kDa-44 kDa (non-reducing), identified as various isoforms of Vascular Endothelial Growth Factor or Vascular Permeability Factor (VEGF/VPF). It is highly specific to VEGF, which is a homodimeric, disulfide-linked glycoprotein with a close homology to platelet derived growth factor (PDGF). There are multiple isoforms of VEGF containing 206-, 189-, 165-, and 121-amino acid residues. The smaller two isoforms, VEGF165 and VEGF121, are secreted proteins and act as diffusible agents, whereas the larger two remain cell associated. VEGF/VPF plays an important role in angiogenesis, which promotes tumor progression and metastasis.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.

Catalog Number: (75794-262)
Supplier: Prosci
Description: 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: Biotium
Description: CD98 exits as a heterodimer containing a disulphide-linked glycosylated heavy chain and a non-glycosylated light chain. It is a member of the solute carrier family and encodes a cell surface, transmembrane protein. The protein exists as the heavy chain of a heterodimer, covalently bound through disulfide bonds to one of several possible light chains. The encoded transporter plays a role in regulation of intracellular calcium levels and transports L-type amino acids. Alternatively spliced transcript variants, encoding different isoforms, have been characterized.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.

Catalog Number: (75794-252)
Supplier: Prosci
Description: 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.


Catalog Number: (89359-700)
Supplier: Genetex
Description: Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the endoplasmic reticulum (ER). Many resident ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multisubunit proteins. Studies indicate that calnexin associates with the major histocompatability complex (MHC) class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin, but not with completed receptor complexes. It has been shown that calnexin is a chaperone that retains incompletely or improperly folded proteins in the ER. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble ER resident proteins such as GRP 78 and GRP 94 and protein disulfide isomerase. Integral membrane ER resident proteins, like calnexin, often lack this KDEL sequence but contain positively charged cytosolic residues that ensure ER retention. Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail (89 amino acids).


Catalog Number: (10088-996)
Supplier: Proteintech
Description: The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands . They are transmembrane αβ heterodimers and at least 24 distinct integrin heterodimers are formed by the combination of 18 α and eight β known subunits . In addition to mediating cell adhesion, integrins also play important roles in modulating signal transduction pathways that control cellular responses including migration, proliferation, differentiation, and apoptosis . Integrin alpha-IIb (ITGA2B, CD41) is expressed on platelets, megakaryocytes and some hematopoietic progenitor cells . This protein undergoes post-translational cleavage to yield disulfide linked light and heavy chains which join with integrin beta3 (CD61) to form a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrin alpha-IIb/beta-3 is crucial for platelet aggregation through binding of soluble fibrinogen.


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