目录号 | 产品详情 | 靶点 | |
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TP1489 | |||
Risuteganib is a synthetic RGD (arginyl-glycyl-aspartic acid)-class peptide that regulates the functions of multiple integrin isoforms. | |||
TP1530 | |||
This is a fibronectin fragment, an adhesion peptide that displays strong binding affinity to thrombin-stimulated platelets. It is RGD consisting of sequence. | |||
TP1696 | |||
CGGRGD is a RGD derivative with cysteine as the n-terminal. CGGRGD was synthesized by solid phase peptide synthesis technology, and amino2-cyanobenzothiazole (2-cyanobenzothiazole) (2-cyanobenzothiazole (CBT) was added on the surface of PCL fiber for ammo | |||
T80142 | Integrin | ||
Cyclo(Gly-Arg-Gly-Asp-Ser-Pro)(c(GRGDSP))为RGD 抑制肽。该化合物作为合成的α5β1整联蛋白配体,能够竞争性阻断 invasin(Inv)与Caco-2细胞表面α5β1整联蛋白的相互结合。 | |||
T36291 | |||
Integrin modulator 1 is a potent and selective α4β1 integrin agonist, with an IC50 of 9.8 nM for RGD-binding α4β1. Integrin modulator 1 increases cell adhesion mediated by α4β1 integrin, with an EC50 of 12.9 nM[1]. Integrin modulator 1 (2-10 μg/mL; 30 min) significantly increases Jurkat E6.1 cell adhesion[1].Integrin modulator 1 (1-100 nM; 1 h) strongly and significantly increases ERK1/2 phosphorylation in Jurkat E6.1 cells[1].Integrin modulator 1 (1 nM-10 μM; 30 min) significantly increases the binding of HUTS-21 antibody to Jurkat E6.1 cells in a concentration-dependent manner[1]. [1]. Baiula M, et, al. New β-Lactam Derivatives Modulate Cell Adhesion and Signaling Mediated by RGD-Binding and Leukocyte Integrins. J Med Chem. 2016 Nov 10;59(21):9721-9742. | |||
T35582 | |||
H-Arg-Gly-Asp-Cys-OH is a tetrapeptide that contains the arginine-glycine-aspartate (RGD) motif, a sequence that acts as a recognition site for various adhesion proteins.1It inhibits the binding of fibrinogen to endothelial cells and ADP-stimulated platelets with IC50values of 320 and 35 μM, respectively.2Implantation of titanium rods coated with H-Arg-Gly-Asp-Cys-OH increases bone formation in rat femurs.3H-Arg-Gly-Asp-Cys-OH has been conjugated to polyethylenimine to improve gene transfection efficiency.4 1.Park, H.S., Kim, C., and Kang, Y.K.Preferred conformations of RGDX tetrapeptides to inhibit the binding of fibrinogen to plateletsBiopolymers63(5)298-313(2002) 2.Tranqui, L., Andrieux, A., Hudry-Clergeon, G., et al.Differential structural requirements for fibrinogen binding to platelets and to endothelial cellsJ. Cell Biol.108(6)2519-2527(1989) 3.Ferris, D.M., Moodie, G.D., Dimond, P.M., et al.RGD-coated titanium implants stimulate increased bone formation in vivoBiomaterials20(23-24)2323-2331(1999) 4.Kunath, K., Merdan, T., Hegener, O., et al.Integrin targeting using RGD-PEI conjugates for in vitro gene transferJ. Gene Med.5(7)588-599(2003) | |||
T76068 | |||
Cyclo(Arg-Gly-Asp-D-Phe-Cys) TFA 是一种环状RGD多肽, 对αvβ3有高亲和性,能干扰细胞整合素之间的相互作用。此化合物能抑制胚胎干细胞(ESC)的多潜能性基因表达,并可在体内减少mESC的致瘤潜力,因此适用于肿瘤研究领域。 | |||
T76255 | |||
Certepetide (CEND-1),即双功能环肽(a.k.a. iRGD),是一种具有穿透肿瘤功能的多肽。通过与α-V整联蛋白(alphav-integrins)的RGD motif相互作用,以及激活神经纤毛蛋白1(NRP-1),Certepetide能够将实体瘤微环境转化成临时的活性分子通道,从而在肿瘤中累积。该化合物在胰腺癌和其他实体瘤的研究中具有应用潜力。 | |||
T78219 | Integrin | ||
Obtustatin triacetate 是一种从 Vipera lebetina obtusa 毒液中提取、含有 41 个残基的非 RGD 型解整合素。它作为整合素α1β1与 IV 型胶原蛋白粘附的高效且选择性抑制剂,能够抑制血管生成,因此在癌症研究中有应用。 | |||
T75724 | |||
LXW7 TFA, 包含 Arg-Gly-Asp (RGD) 的环状肽,作为整合素αvβ3抑制剂,展示出对αvβ3整联蛋白高度的结合亲和力,其IC50值为0.68 μM。此外,LXW7 TFA 能够促进 VEGFR-2 磷酸化和 ERK1/2 激活,显示出抗炎活性。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPK-00760 | IgG1 Fc Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Recombinant murine Fc fragment contains the hinge region, CH2, and CH3 region of the mouse IgG1 isotype. IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.
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TMPK-00759 | IgG1 Fc Protein, Human, Recombinant | Human | HEK293 | ||
IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.IgG1 Fc was reported has a novel role as a potential anti-inflammatory drug for treatment of human autoimmune diseases.
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TMPY-05744 | TIGIT Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
TIGIT, also known as V-set and transmembrane domain-containing protein 3 (VSTM3) or V-set and immunoglobulin domain-containing protein 9 (VSIG9) is a new surface protein containing an immunoglobulin variable domain, a transmembrane domain and an immunoreceptor tyrosine-based inhibitory motif (ITIM). TIGIT is expressed on regulatory, memory, activated T cells and NK cells. It binds PVR with high affinity, and PVRL2 with lower affinity, but not PVRL3. Knockdown of TIGIT with siRNA in human memory T cells did not affect T cell responses, however, TIGIT inhibits NK cytotoxicity directly through its ITIM. TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells. The binding of PVR to TIGIT on human dendritic cells enhanced the production of IL-1 and diminished the production of IL-12p4. Also, TIGIT counter inhibits the NK-mediated killing of tumor cells and protects normal cells from NK-mediated cytotoxicity thus providing an "alternative self" mechanism for MHC class I inhibition.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-01009 | TGFBI Protein, Human, Recombinant (His) | Human | HEK293 | ||
TGFBI is an RGD-containing protein that binds to type I, II and IV collagens. The RGD motif is found in many extracellular matrix proteins modulating cell adhesion and serves as a ligand recognition sequence for several integrins. TGFBI plays a role in cell-collagen interactions and may be involved in endochondral bone formation in cartilage. TGFBI is induced by transforming growth factor-beta and acts to inhibit cell adhesion. Mutations in TGFBI are associated with multiple types of corneal dystrophy. TGFBI can bind to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, TGFBI may be involved in endochondral bone formation. Loss of the TGFBI is sufficient to induce specific resistance.
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TMPY-01384 | Endoglin/CD105 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Endoglin, also known as CD105, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity not by itself but by associating with TGF-β type II receptor (TβRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.
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TMPY-05717 | Integrin alpha V beta 8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Integrin alpha V beta 8 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligands. ITGAVB8 does not appear to assume different activation states; and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif; including vitronectin; fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP; which releases active TGF-beta. This mechanism differs from that of alpha V beta 6; the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms.
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TMPY-01431 | L1CAM Protein, Human, Recombinant (His) | Human | HEK293 | ||
L1 cell adhesion molecule (L1CAM), also designated as CD171, is a cell adhesion receptor of the immunoglobulin superfamily, known for its roles in nerve cell function. While originally believed to be present only in brain cells, in recent years L1-CAM has been detected in other tissues, and a variety of cancer cells, including some common types of human cancer. L1CAM interacts with a variety of ligands including axonin-1, CD9, neurocan, and integrins, and it has been revealed that the RGD motif in the sixth Ig domain of L1CAM is a binding site for integrins, thus important for nuclear signaling. Disruption of L1CAM function causes three X-linked neurological syndromes, i.e. hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait, and adducted thumbs), and spastic paraplegia syndrome. Overexpression of L1CAM in normal and cancer cells increased motility, enhanced growth rate, and promoted cell transformation and tumorigenicity. Recent work has identified L1CAM (CD171) as a novel marker for human carcinoma progression, and a candidate for anti-cancer therapy.
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TMPY-01288 | Osteopontin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Osteopontin, also known as Secreted phosphoprotein 1, Bone sialoprotein 1, BSP-1, OPN, and SPP1, is a member of the osteopontin family and a SIBLING glycoprotein. Osteopontin has been classified as T-helper 1 cytokine and thus believed to exacerbate inflammation in several chronic inflammatory diseases, including atherosclerosis. Besides proinflammatory functions, physiologically Osteopontin is a potent inhibitor of mineralization, it prevents ectopic calcium deposits and is a potent inducible inhibitor of vascular calcification. Osteopontin is expressed and secreted by various cells, and has a role in cell adhesion, chemotaxis, prevention of apoptosis, invasion, migration and anchorage-independent growth of tumor cells. Osteopontin recruitment functions of inflammatory cells are thought to be mediated through its adhesive domains, especially the arginine-glycine-aspartate (RGD) sequence that interacts with several integrin heterodimers. Osteopontin has emerged as a potential biomarker and mediator in cardiovascular disease. In the context of atherosclerosis, OPN is generally regarded as a proinflammatory and proatherogenic molecule. However, the role of OPN in vascular calcification (VC), which is closely related to chronic and active inflammation, is that of a negative regulator because it is an inhibitor of calcification and an active inducer of decalcification. Extensive research has demonstrated the pivotal participation of Osteopontin in the regulation of cell signaling which controls neoplastic and malignant transformation. The elevated expression of Osteopontin has been observed in a variety of cancers. It has been linked with tumor metastasis and signifies a poor prognosis for the patient.
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TMPY-06988 | Osteopontin Protein, Human, Recombinant (aa 17-166, His) | Human | HEK293 | ||
Osteopontin, also known as Secreted phosphoprotein 1, Bone sialoprotein 1, BSP-1, OPN, and SPP1, is a member of the osteopontin family and a SIBLING glycoprotein. Osteopontin has been classified as T-helper 1 cytokine and thus believed to exacerbate inflammation in several chronic inflammatory diseases, including atherosclerosis. Besides proinflammatory functions, physiologically Osteopontin is a potent inhibitor of mineralization, it prevents ectopic calcium deposits and is a potent inducible inhibitor of vascular calcification. Osteopontin is expressed and secreted by various cells, and has a role in cell adhesion, chemotaxis, prevention of apoptosis, invasion, migration and anchorage-independent growth of tumor cells. Osteopontin recruitment functions of inflammatory cells are thought to be mediated through its adhesive domains, especially the arginine-glycine-aspartate (RGD) sequence that interacts with several integrin heterodimers. Osteopontin has emerged as a potential biomarker and mediator in cardiovascular disease. In the context of atherosclerosis, OPN is generally regarded as a proinflammatory and proatherogenic molecule. However, the role of OPN in vascular calcification (VC), which is closely related to chronic and active inflammation, is that of a negative regulator because it is an inhibitor of calcification and an active inducer of decalcification. Extensive research has demonstrated the pivotal participation of Osteopontin in the regulation of cell signaling which controls neoplastic and malignant transformation. The elevated expression of Osteopontin has been observed in a variety of cancers. It has been linked with tumor metastasis and signifies a poor prognosis for the patient.
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TMPH-02591 | COL4A3 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms.
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TMPY-00783 | Endoglin/CD105 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Endoglin, also known as CD105, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity not by itself but by associating with TGF-β type II receptor (TβRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.
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TMPY-01615 | Endoglin/CD105 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Endoglin, also known as CD105, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity not by itself but by associating with TGF-β type II receptor (TβRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.
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TMPJ-01375 | HSPB7 Protein, Human, Recombinant (His) | Human | E. coli | ||
PSG2 is a secreted protein that in humans is encoded by the PSG2 gene. It is a member of the human pregnancy-specific glycoproteins (PSGs) family. These proteins are synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. PSG2 consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. It has an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain.
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TMPJ-00838 | PSG2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
PSG2 is a secreted protein that in humans is encoded by the PSG2 gene. It is a member of the human pregnancy-specific glycoproteins (PSGs) family. These proteins are synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. PSG2 consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. It has an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain.
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TMPJ-00361 | Endoglin Protein, Human, Recombinant (Trx & His) | Human | E. coli | ||
Endoglin is a single-pass type I membrane protein which restricted to endothelial cells in all tissues except bone marrow. Endoglin as major glycoprotein of vascular endothelium, it has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Homodimer forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and/or TGFBR2. It may have an important role in the binding of endothelial cells to integrins and/or other RGD receptors. Defects in ENG are the cause of hereditary hemorrhagic telangiectasia type 1 (HHT1), which is an autosomal dominant multisystemic vascular dysplasia, characterized by recurrent epistaxis, muco-cutaneous telangiectases, gastro-intestinal hemorrhage, and pulmonary (PAVM), cerebral (CAVM) and hepatic arteriovenous malformations.
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TMPY-00961 | ADAM15 Protein, Human, Recombinant (His) | Human | HEK293 | ||
ADAM15, also known as Metargidin, is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain) family of proteins and is widely expressed in different tissues and cell types. Members of this family contain an amino-terminal metalloprotease domain followed by a disintegrin domain, a cysteine-rich region and a membrane proximal EGF-like domain. The disintegrin domain of ADAM15/metargidin contains an RGD tripeptide sequence, suggesting that it may potentially interact with the integrin family of proteins. ADAM15 is a transmembrane multi-domain proteins implicated in proteolysis, cell-cell and cell-matrix interactions in various disease conditions. There is also evidence supporting a role for ADAM15 in angiogenesis and angioinvasion of tumor cells, which are critical for unrestrained tumor growth and metastatic spread. Given its diverse functions, ADAM15 may represent a pivotal regulatory component of tumor progression, an important target for therapeutic intervention, or emerge as a biomarker of disease progression.
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TMPY-02280 | ADAM15 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
ADAM15, also known as Metargidin, is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain) family of proteins and is widely expressed in different tissues and cell types. Members of this family contain an amino-terminal metalloprotease domain followed by a disintegrin domain, a cysteine-rich region and a membrane proximal EGF-like domain. The disintegrin domain of ADAM15/metargidin contains an RGD tripeptide sequence, suggesting that it may potentially interact with the integrin family of proteins. ADAM15 is a transmembrane multi-domain proteins implicated in proteolysis, cell-cell and cell-matrix interactions in various disease conditions. There is also evidence supporting a role for ADAM15 in angiogenesis and angioinvasion of tumor cells, which are critical for unrestrained tumor growth and metastatic spread. Given its diverse functions, ADAM15 may represent a pivotal regulatory component of tumor progression, an important target for therapeutic intervention, or emerge as a biomarker of disease progression.
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TMPY-06796 | L1CAM Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
L1 cell adhesion molecule (L1CAM), also designated as CD171, is a cell adhesion receptor of the immunoglobulin superfamily, known for its roles in nerve cell function. While originally believed to be present only in brain cells, in recent years L1-CAM has been detected in other tissues, and a variety of cancer cells, including some common types of human cancer. L1CAM interacts with a variety of ligands including axonin-1, CD9, neurocan, and integrins, and it has been revealed that the RGD motif in the sixth Ig domain of L1CAM is a binding site for integrins, thus important for nuclear signaling. Disruption of L1CAM function causes three X-linked neurological syndromes, i.e. hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait, and adducted thumbs), and spastic paraplegia syndrome. Overexpression of L1CAM in normal and cancer cells increased motility, enhanced growth rate, and promoted cell transformation and tumorigenicity. Recent work has identified L1CAM (CD171) as a novel marker for human carcinoma progression, and a candidate for anti-cancer therapy.
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TMPY-06857 | L1CAM Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
L1 cell adhesion molecule (L1CAM), also designated as CD171, is a cell adhesion receptor of the immunoglobulin superfamily, known for its roles in nerve cell function. While originally believed to be present only in brain cells, in recent years L1-CAM has been detected in other tissues, and a variety of cancer cells, including some common types of human cancer. L1CAM interacts with a variety of ligands including axonin-1, CD9, neurocan, and integrins, and it has been revealed that the RGD motif in the sixth Ig domain of L1CAM is a binding site for integrins, thus important for nuclear signaling. Disruption of L1CAM function causes three X-linked neurological syndromes, i.e. hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait, and adducted thumbs), and spastic paraplegia syndrome. Overexpression of L1CAM in normal and cancer cells increased motility, enhanced growth rate, and promoted cell transformation and tumorigenicity. Recent work has identified L1CAM (CD171) as a novel marker for human carcinoma progression, and a candidate for anti-cancer therapy.
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TMPY-06759 | L1CAM Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
L1 cell adhesion molecule (L1CAM), also designated as CD171, is a cell adhesion receptor of the immunoglobulin superfamily, known for its roles in nerve cell function. While originally believed to be present only in brain cells, in recent years L1-CAM has been detected in other tissues, and a variety of cancer cells, including some common types of human cancer. L1CAM interacts with a variety of ligands including axonin-1, CD9, neurocan, and integrins, and it has been revealed that the RGD motif in the sixth Ig domain of L1CAM is a binding site for integrins, thus important for nuclear signaling. Disruption of L1CAM function causes three X-linked neurological syndromes, i.e. hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait, and adducted thumbs), and spastic paraplegia syndrome. Overexpression of L1CAM in normal and cancer cells increased motility, enhanced growth rate, and promoted cell transformation and tumorigenicity. Recent work has identified L1CAM (CD171) as a novel marker for human carcinoma progression, and a candidate for anti-cancer therapy.
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TMPY-04131 | KIRREL Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
NEPH1 (KIRREL1) belongs to a family of three closely related transmembrane proteins of the Ig superfamily with a structure similar to that of nephrin. All three Neph proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of Neph1 for podocin. Neph1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. Neph1 consists of a signal peptide, five Ig-like C2-type domains with the middle domain overlapping with a PKD-like domain, an RGD sequence, a transmembrane domain, and a cytoplasmic tail, which is expressed in slit diaphragm domains of podocytes and vertebrate and invertebrate nervous systems. Neph1 is abundantly expressed in the kidney, specifically expressed in podocytes of kidney glomeruli, and plays a significant role in the normal development and function of the glomerular permeability. Neph1 interacts with nephrin in vitro and in vivo, and able to stimulate transcriptional activation in a model system, such as the activation of the transcription factor AP-1 via the stimulation of a MAPK module. Neph1 is crucial for the integrity of the slit diaphragm, as Neph1 gene knockout mice result in effacement of glomerular podocytes, heavy proteinuria, and early postnatal death.
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TMPY-01015 | KIRREL Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
NEPH1 (KIRREL1) belongs to a family of three closely related transmembrane proteins of the Ig superfamily with a structure similar to that of nephrin. All three Neph proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of Neph1 for podocin. Neph1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. Neph1 consists of a signal peptide, five Ig-like C2-type domains with the middle domain overlapping with a PKD-like domain, an RGD sequence, a transmembrane domain, and a cytoplasmic tail, which is expressed in slit diaphragm domains of podocytes and vertebrate and invertebrate nervous systems. Neph1 is abundantly expressed in the kidney, specifically expressed in podocytes of kidney glomeruli, and plays a significant role in the normal development and function of the glomerular permeability. Neph1 interacts with nephrin in vitro and in vivo, and able to stimulate transcriptional activation in a model system, such as the activation of the transcription factor AP-1 via the stimulation of a MAPK module. Neph1 is crucial for the integrity of the slit diaphragm, as Neph1 gene knockout mice result in effacement of glomerular podocytes, heavy proteinuria, and early postnatal death.
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