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Catalog Number: (10457-268)
Supplier: Bioss
Description: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.


Catalog Number: (89416-394)
Supplier: Prosci
Description: TEM1 Antibody: Tumor endothelial marker (TEM) 1 was originally identified as a human embryonic fibroblast-specific antigen and was later determined to be endosialin, a single-pass transmembrane glycoprotein that has multiple extracellular domains, including three EGF-like domains, a sushi-like domain, and a C lectin-like domain. TEM proteins are significantly up-regulated during angiogenesis and neoangiogenesis that are crucial for the growth of solid tumors. While TEM1 is not required for angiogenesis during fetal development, postnatal growth or wound healing, it plays a role in tumor growth, invasion, and metastasis. Fibronectin and collagen types I and IV act as specific ligands of TEM1, leading to suggestions that these molecules may cause changes in the extracellular matrix, cell adhesion and migration during tumor invasion.


Catalog Number: (89416-392)
Supplier: Prosci
Description: TEM1 Antibody: Tumor endothelial marker (TEM) 1 was originally identified as a human embryonic fibroblast-specific antigen and was later determined to be endosialin, a single-pass transmembrane glycoprotein that has multiple extracellular domains, including three EGF-like domains, a sushi-like domain, and a C lectin-like domain. TEM proteins are significantly up-regulated during angiogenesis and neoangiogenesis that are crucial for the growth of solid tumors. While TEM1 is not required for angiogenesis during fetal development, postnatal growth or wound healing, it plays a role in tumor growth, invasion, and metastasis. Fibronectin and collagen types I and IV act as specific ligands of TEM1, leading to suggestions that these molecules may cause changes in the extracellular matrix, cell adhesion and migration during tumor invasion.


Catalog Number: (75791-692)
Supplier: Prosci
Description: Activin Receptor-Like Kinase 1 (ALK-1) is a type I cell-surface receptor for the TGF- beta superfamily of ligands, which mediates signaling of BMP9 (bone morphogenetic protein) and BMP10. ALK1 signaling is necessary for angiogenesis during embryogenesis, wound healing, and tumor growth. ALK-1 has a high degree of similarity in serine-threonine kinase subdomains, a glycine and serine rich region preceding the kinase-domain, and a C-terminal tail with other activin receptor-like kinase proteins. ALK-1 is mainly expressed in endothelial cells regulating proliferation and migration in vitro and angiogenesis in vivo. Mutations in ALK-1 as well as in endoglin are associated with hereditary hemorrhagic telangiectasia (HHT), suggesting ALK-1 plays a critical role for in the control of blood vessel development or repair.


Supplier: Adipogen
Description: Fibroblast growth factors (FGFs) constitute a family of heparin-binding polypeptides involved in the regulation of biological responses such as growth, differentiation and angiogenesis. The biological effects of FGFs are mediated by four structurally related receptor tyrosine kinases denoted FGFR1, FGFR2, FGFR3 and FGFR4. FGF-1 is a powerful mitogen of cells of mesodermal, ectodermal and endodermal origin. FGF-1 association with heparan sulfate is a prerequisite for activation of FGF receptors. FGF-1 plays a role in various stages of development and morphogenesis as well as in angiogenesis and wound healing processes. Recent data indicate a role of FGF-1 in inflammation and obesity. FGF-1 is selectively induced in fat cells by high-fat diet feeding and established the PPARgamma-FGF-1 axis as a critical pathway that regulates adipose tissue remodeling.

Supplier: STEMCELL Technologies
Description: Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick <i>et al.</i>). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata <i>et al.</i>). This product is animal component-free.

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Catalog Number: (10073-048)
Supplier: Prosci
Description: SPARC/Osteonectin is a secreted, evolutionarily conserved collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains; an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation.


Catalog Number: (10095-062)
Supplier: Proteintech
Description: SPARC, also known as ON (Osteonectin) or BM-40 (Basement-membrane protein 40), is a 43-kDa extracellular glycoprotein that belongs to a group of matricellular proteins defined as secreted components that do not contribute directly to the formation of structural elements but serve to modulate cell-matrix interactions and cellular functions . SPARC is expressed at high levels in bone tissue, is distributed widely in many other tissues and cell types, and is associated generally with tissues undergoing morphogenesis, remodeling and wound repair . It elicits changes in cell shape, inhibits cell-cycle progression, and influences the synthesis of extracellular matrix . Altered expression of SPARC has been reported in a variety of cancers, which include breast, ovarian, colorectal, and pancreatic cancer as well as melanoma and glioblastomas .


Catalog Number: (10090-308)
Supplier: Proteintech
Description: Matrix metalloproteinase-7 (MMP-7)/ matrilysin is a member of the MMP family, but is structurally different from the other MMPs by virtue of the absence of a conserved COOH-terminal protein domain. MMPs are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and cancer metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP-7 degrades proteoglycans, fibronectin, elastin and casein, and is involved in wound healing, tumor progression, pulmonary fibrosis, and development of choroidal neovascularization in age-related macular degeneration. The expression of MMP-7 is increased in most tumors. The gene encoding MMP-7 is part of a cluster of MMP genes which localize to chromosome 11q22.3.


Catalog Number: (10751-002)
Supplier: Prosci
Description: ZEB2 Antibody: ZEB2, initially identified as Smad interacting-protein 1, is normally located in the nucleus and functions as a DNA-binding transcriptional repressor that interacts with activated SMADs. Like the homologous ZEB1, ZEB2 inhibits the transcription of the E-cadherin gene and induces epithelial-mesenchymal transition, a genetic program controlling cell migration during embryonic development and wound healing, in vitro. ZEB2 can also protect cells from DNA damage-induced apoptosis, suggesting that its expression may contribute to tumor progression. Recent evidence has shown that ZEB2 is often observed in the cytoplasm in numerous cancer tissues, indicating that its localization may be regulated in normal and tumor tissues. Mutations in this gene are also associated with Hirschsprung disease/Mowat-Wilson syndrome.


Catalog Number: (10749-998)
Supplier: Prosci
Description: TEM1 Antibody: Tumor endothelial marker (TEM) 1 was originally identified as a human embryonic fibroblast-specific antigen and was later determined to be endosialin, a single-pass transmembrane glycoprotein that has multiple extracellular domains, including three EGF-like domains, a sushi-like domain, and a C lectin-like domain. TEM proteins are significantly up-regulated during angiogenesis and neoangiogenesis that are crucial for the growth of solid tumors. While TEM1 is not required for angiogenesis during fetal development, postnatal growth or wound healing, it plays a role in tumor growth, invasion, and metastasis. Fibronectin and collagen types I and IV act as specific ligands of TEM1, leading to suggestions that these molecules may cause changes in the extracellular matrix, cell adhesion and migration during tumor invasion.


Catalog Number: (103010-388)
Supplier: Anaspec Inc
Description: Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-10 (stromelysin 2) is involved in several pathological conditions, such as cancer, arthritis and wound healing. MMP-10 is secreted as zymogen with a prodomain, a catalytic domain, a hinge region, and a hemopexin-like domain. It can activate other MMPs such as MMP-1, MMP-8 and degrade a variety of substrates, including gelatin, collagens III, IV and V, fibronectin, aggrecan

This recombinant human MMP-10 was expressed as a pro-enzyme enzyme from its DNA sequence7 transfected into a mouse myeloma cell line, NS0. The apparent Mr on SDS-PAGE is 58-kDa. Incubation with 1 mM APMA at 37°C for 1-2 hours will activate pro-MMP-10. Its activity can be measured by FRET peptides


Catalog Number: (75793-836)
Supplier: Prosci
Description: Fibroblast growth factors (FGFs) constitute a family of heparin-binding polypeptides involved in the regulation of biological responses such as growth, differentiation and angiogenesis. The biological effects of FGFs are mediated by four structurally related receptor tyrosine kinases denoted FGFR1, FGFR2, FGFR3 and FGFR4. FGF-1 [FGF-acidic; ECGF; HBGF-1] is a powerful mitogen of cells of mesodermal, ectodermal and endodermal origin. FGF-1 association with heparan sulfate is a prerequisite for activation of FGF receptors. FGF-1 plays a role in various stages of development and morphogenesis as well as in angiogenesis and wound healing processes. Recent data indicate a role of FGF-1 in inflammation and obesity. FGF-1 is selectively induced in fat cells by high-fat diet feeding and established the PPARgamma-FGF-1 axis as a critical pathway that regulates adipose tissue remodeling.


Catalog Number: (10426-296)
Supplier: Bioss
Description: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.


Catalog Number: (10426-278)
Supplier: Bioss
Description: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.


Catalog Number: (102979-992)
Supplier: Adipogen
Description: The proteolysis of collagens plays an important role in numerous physiological and pathological situations such as morphogenesis, wound healing, arthritis, arteriosclerosis and tumor metastasis. Triple helical type I collagens are made up of two alpha1 (I) and one alpha2 (I) chains, and are found in skin, tendon, ligament and interstitial tissues. Due to their fibrillary structure native collagens are resistant to most proteases. They are substrates for certain matrix metalloproteinases (MMPs), which constitute a family of zinc-dependent enzymes catalyzing the degradation of extracellular matrix components. Initial MMP-8 dependent cleavage of collagen into the characteristic ¾ and ¼ fragments has been shown to enable MMP-9 diffusion along the protein helix with preferential binding to the collagen ¾ fragment tail. Finally, untwisting of the helix end results in the local denaturation of the triple helical structure.


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