SDCBP Recombinant Monoclonal Antibody

The SDCBP recombinant monoclonal antibody is produced utilizing in vitro expression systems. The antibody is generated by cloning DNA sequences encoding SDCBP antibodies from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human SDCBP protein. Subsequently, the genes encoding the SDCBP antibodies are incorporated into plasmid vectors, which are then introduced into host cells to facilitate antibody expression. Following expression, the SDCBP recombinant monoclonal antibody undergoes purification through affinity chromatography. Rigorous testing in ELISA, WB, IF, and FC applications conclusively demonstrates its reactivity with the human SDCBP protein.

SDCBP is a versatile protein with diverse roles, including cell adhesion, signaling, intracellular trafficking, and cytoskeleton regulation. Its interactions with syndecan receptors and other binding partners enable participation in a wide array of cellular processes, impacting both normal physiological functions and pathological conditions, including cancer and immune responses.

SDCBP is a multifunctional adapter protein involved in a diverse array of cellular functions. These include:

• Trafficking of transmembrane proteins
• Neuro and immunomodulation
• Exosome biogenesis
• Tumorigenesis

SDCBP positively regulates TGFβ1-mediated SMAD2/3 activation, as well as TGFβ1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. It may enhance TGFβ1 signaling by increasing cell-surface expression of TGFβR1, preventing its interaction with CAV1. This, in turn, inhibits CAV1-dependent internalization and degradation of TGFβR1.

SDCBP, in concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis. It also regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. Within adherens junctions, SDCBP may function to couple syndecans to cytoskeletal proteins or signaling components. It appears to couple the transcription factor SOX4 to the IL-5 receptor (IL5RA). Additionally, SDCBP may play a role in vesicular trafficking. It appears to be essential for targeting TGFA to the cell surface in the early secretory pathway.

Research has uncovered a wide range of functions associated with SDCBP, as evidenced by the following studies:

1. Studied role of melanoma differentiation associated protein-9 (MDA-9)/Syntenin in autophagy of anoikis-resistant glioma stem cells. PMID: 29760085
2. Frizzled 7 and phosphatidylinositol 4,5-diphosphate binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signaling. PMID: 27386966
3. Syntenin mediates SRC function in exosomal cell-to-cell communication. PMID: 29109268
4. These findings demonstrate that syntenin promotes VEGF signaling and, through its PDZ-dependent interaction with ephrin-B2, enhances VEGF-mediated VEGFR2 endocytosis and subsequent downstream signaling and angiogenesis in endothelial cells. PMID: 28418925
5. Syntenin-1 promotes invasion and progression of squamous cell carcinomas of the head and neck. PMID: 27811365
6. MDA-9 upregulated active levels of known modulators of epithelial mesenchymal transformation, the small GTPases RhoA and Cdc42, via TGFbeta1, promoting lung metastasis of breast cancer cells. PMID: 27863394
7. a unique function of MDA-9 as a facilitator and determinant of glioma stemness and survival. PMID: 27472461
8. SDCBP might be an important marker for identifying Triple negative breast cancer cases that are suitable for dasatinib therapy. PMID: 28141839
9. ACTB, CDKN1B, GAPDH, GRB2, RHOA and SDCBP are potent reference genes in neuroendocrine tumors of the lung. PMID: 27802291
10. In summary, the study identifies miR-216b as a regulator of SDCBP expression in breast cancer which can potentially be targeted for developing newer therapies for the effective treatment of this killer disease. PMID: 27720715
11. Data show that patients with high MDA-9/Syntenin and high Slug expressions were associated with poor overall survival compared to those with low expression in lung adenocarcinomas. PMID: 26561205
12. Data suggest that syntenin/SDCBP PDZ domains 1 and 2 recognize a broad range of peptide ligands with preferences for nectin-1, hydrophobic amino acid motifs, and cryptic internal ligands/peptide fragments. PMID: 26787460
13. these findings demonstrate that syntenin may act as an important positive regulator of TGF-b signaling by regulating caveolin-1-mediated internalization of TbRI; thus, providing a novel function for syntenin that is linked to cancer progression. PMID: 25893292
14. To predict mda-9's association with extracellular matrix organization. PMID: 26093898
15. MDA-9, co-expressed with GRP78, as a melanoma protein associated with lymph node metastasis. Investigating how MDA-9 and GRP78 interact to contribute to melanoma metastasis and disease progression could reveal new potential avenues of targeted therapy PMID: 25480418
16. Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2. PMID: 24637612
17. High MDA-9 expresison is associated with glioma. PMID: 24305713
18. ALCAM stably interacts with actin by binding to syntenin-1 and ezrin. PMID: 24662291
19. Our findings indicate that MDA-9/Syntenin might provide an attractive target for developing detection, monitoring, and therapeutic strategies for managing Urothelial cell carcinoma . PMID: 23873690
20. Results suggested that SDCBP played an important role in tumor growth of ER-negative breast cancers. PMID: 23533663
21. Findings establish RKIP as an inhibitor of MDA-9-dependent melanoma metastasis. PMID: 23066033
22. Our studies delineate an unanticipated cell nonautonomous function of MDA-9/syntenin in the context of angiogenesis, which may directly contribute to its metastasis-promoting properties PMID: 23233738
23. results indicate Mda-9/syntenin overexpression could activate FAK-JNK and FAK-Akt signaling and then enhance the migration capacity of human brain glioma cells. PMID: 22938480
24. Data show that syntenin-1 is recruited to the plasma membrane during HIV-1 attachment. PMID: 22535526
25. the key role of syntenin-1 is the generation of functional asymmetry in T cells and provide a novel mechanistic link between receptor activation and actin polymerization and accumulation in response to extracellular stimulation. PMID: 22349701
26. our data demonstrate that the Sox4 C-terminal domain regulates polyubiquitin-independent proteasomal degradation of Sox4 that can be modulated by interaction with syntenin PMID: 21986941
27. MDA-9/syntenin functions as a positive regulator of melanoma progression and metastasis through interactions with c-Src and promotes the formation of an active FAK/c-Src signaling complex leading to NF-k B and matrix metalloproteinase activation. Review. PMID: 22201728
28. mda-9/syntenin is involved in uveal melanoma progression PMID: 22267972
29. ubiquitin-dependent pathway involving syntenin-1 that is regulated by Ulk1. PMID: 21949238
30. mda-9/syntenin, a positive regulator of cancer metastasis, regulates the activation of Akt (also known as protein kinase B) by facilitating ILK adaptor function during adhesion to type I collagen (COL-I) in human breast cancer cells. PMID: 21828040
31. showed that overexpression of wild-type MDA-9/syntenin enhances formation of filopodia, whereas MDA-9/syntenin lacking the PDZ domain inhibits the formation of filopodia PMID: 21359963
32. ST1 were up-regulated with the malignancy of prostate cancer cell lines and have their potential as serum biomarkers for indicating the developmental stage of prostate cancer. PMID: 20233700
33. Large/zonula occludens-1 domains of MDA-9 represent a promosing potential therapeutic target for preventing cancer progression and metastatic spread PMID: 20228839
34. Data show that the functional properties of syntenin are a result of independent interactions with target peptides. PMID: 12679023
35. melanoma metastasis is associated with increased expression of the syntenin gene which may participate in signal transduction and cell adhesion via the multifunctional protein-binding properties of its tandem PDZ domains PMID: 15254681
36. eIF5A may be a regulator of p53, and syntenin might regulate p53 by balancing the regulation of eIF5A signaling to p53 for apoptosis PMID: 15371445
37. This review discusses the identification, structure and function of mda-9/syntenin and delineates future studies to address its role in regulating key physiological and pathological processes. PMID: 15518882
38. Study provides the first direct link between mda-9/syntenin expression and tumor cell dissemination in vivo and indicates that mda-9/syntenin expression activates specific signal transduction pathways. PMID: 16322237
39. Together, these results suggest that downregulation of syntenin by RNA interference could provide a means of inhibiting tumor invasion and possibly metastasis in different cancers, and point to syntenin as a potential cancer biomarker and drug target. PMID: 17451681
40. Syntenin binding to Delta1 plays a dual role in promoting intercellular adhesion and regulating Notch signalling. PMID: 17666427
41. Suggest that syntenin is a physiological suppressor of TRAF6 and plays an inhibitory role in IL-1R- and TLR4- mediated NF-kappaB activation pathways. PMID: 18234474
42. Syntenin stimulates c-jun phosphorylation and modulates Frizzled 7 signaling, in particular the PKCalpha/CDC42 noncanonical Wnt signaling cascade. PMID: 18256285
43. data are compatible with a model wherein interaction of MDA-9/syntenin with c-Src promotes the formation of an active FAK/c-Src signaling complex, leading to enhanced tumor cell invasion and metastatic spread PMID: 18832467
44. Syntenin interacts with the aminoacyl tRNA synthetase complex in a lysyl-tRNA synthetase-dependent manner. PMID: 18839981
45. Syntenin-1 serves as one of IgA-inducing factors for B cells. PMID: 19592421
46. Syntenin forms complexes with multiple IL-5Ralpha chains PMID: 19654410

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HGNC: 10662

OMIM: 602217

KEGG: hsa:6386

STRING: 9606.ENSP00000260130

UniGene: Hs.200804