Recombinant Human Syntenin-1 (SDCBP) Protein (His-KSI)

Name: Recombinant Human Syntenin-1 (SDCBP) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-07147P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Syntenin-1 (SDCBP) Protein (His-KSI) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00560
Target Symbol	SDCBP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	SLYPSLEDLKVDKVIQAQTAFSANPANPAILSEASAPIPHDGNLYPRLYPELSQYMGLSLNEEEIRANVAVVSGAPLQGQLVARPSSINYMVAPVTGNDVGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTITMHKDSTGHVGFIFKNGKITSIVKDSSAARNGLLTEHNICEINGQNVIGLKDSQIADILSTSGTVVTITIMPAFIFEHIIKRMAPSIMKSLMDHTIPEV
Expression Range	2-298aa
Protein Length	Full Length of Mature Protein
Mol. Weight	47.6 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis. Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.
Subcellular Location	Cell junction, focal adhesion. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Melanosome. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Secreted, extracellular exosome. Membrane raft.
Database References	HGNC: 10662 OMIM: 602217 KEGG: hsa:6386 STRING: 9606.ENSP00000260130 UniGene: Hs.200804
Tissue Specificity	Expressed in lung cancers, including adenocarcinoma, squamous cell carcinoma and small-cell carcinoma (at protein level). Widely expressed. Expressed in fetal kidney, liver, lung and brain. In adult highest expression in heart and placenta.

Gene Functions References

Studied role of melanoma differentiation associated protein-9 (MDA-9)/Syntenin in autophagy of anoikis-resistant glioma stem cells. PMID: 29760085
Frizzled 7 and phosphatidylinositol 4,5-diphosphate binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signaling. PMID: 27386966
Syntenin mediates SRC function in exosomal cell-to-cell communication. PMID: 29109268
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
Syntenin-1 promotes invasion and progression of squamous cell carcinomas of the head and neck. PMID: 27811365
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
a unique function of MDA-9 as a facilitator and determinant of glioma stemness and survival. PMID: 27472461
SDCBP might be an important marker for identifying Triple negative breast cancer cases that are suitable for dasatinib therapy. PMID: 28141839
ACTB, CDKN1B, GAPDH, GRB2, RHOA and SDCBP are potent reference genes in neuroendocrine tumors of the lung. PMID: 27802291
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
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
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
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
To predict mda-9's association with extracellular matrix organization. PMID: 26093898
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
Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2. PMID: 24637612
High MDA-9 expresison is associated with glioma. PMID: 24305713
ALCAM stably interacts with actin by binding to syntenin-1 and ezrin. PMID: 24662291
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
Results suggested that SDCBP played an important role in tumor growth of ER-negative breast cancers. PMID: 23533663
Findings establish RKIP as an inhibitor of MDA-9-dependent melanoma metastasis. PMID: 23066033
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
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
Data show that syntenin-1 is recruited to the plasma membrane during HIV-1 attachment. PMID: 22535526
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
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
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
mda-9/syntenin is involved in uveal melanoma progression PMID: 22267972
ubiquitin-dependent pathway involving syntenin-1 that is regulated by Ulk1. PMID: 21949238
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
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
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
Large/zonula occludens-1 domains of MDA-9 represent a promosing potential therapeutic target for preventing cancer progression and metastatic spread PMID: 20228839
Data show that the functional properties of syntenin are a result of independent interactions with target peptides. PMID: 12679023
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
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
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
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
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
Syntenin binding to Delta1 plays a dual role in promoting intercellular adhesion and regulating Notch signalling. PMID: 17666427
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
Syntenin stimulates c-jun phosphorylation and modulates Frizzled 7 signaling, in particular the PKCalpha/CDC42 noncanonical Wnt signaling cascade. PMID: 18256285
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
Syntenin interacts with the aminoacyl tRNA synthetase complex in a lysyl-tRNA synthetase-dependent manner. PMID: 18839981
Syntenin-1 serves as one of IgA-inducing factors for B cells. PMID: 19592421
Syntenin forms complexes with multiple IL-5Ralpha chains PMID: 19654410

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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