Recombinant Mouse Protein sprouty homolog 1 (Spry1)

Code CSB-YP870757MO
MSDS
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Source Yeast
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Code CSB-EP870757MO
MSDS
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Source E.coli
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Code CSB-EP870757MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP870757MO
MSDS
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Source Baculovirus
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Code CSB-MP870757MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Spry1
Uniprot No.
Alternative Names
Spry1; Protein sprouty homolog 1; Spry-1
Species
Mus musculus (Mouse)
Expression Region
1-313
Target Protein Sequence
MDSPSQHGSH TSLVVIQPPA VEGRQRLDYD RDTQPATILS LDQIKAIRGS NEYTEGPSVA RRPAPRTAPR PEKQERTHEI IPANVNSSYE HRPASHPGNA RGSVLSRSTS TGSAASSGSS SSVSSEQGLL GRSPPTRPIP GHRSDRVIRT QPKQLLVEDL KASLKEDPTQ HKFICEQCGK CKCGECTAPR ALPSCLACDR QCLCSAESMV EYGTCMCLVK GIFYHCSNDD DGGSYSDNPC SCSQSHCCSR YLCMGALSLC LPCLLCYPPA KGCLKLCRGC YDWTHRPGCR CRNSNTVYCK LESCPSRAQG KLS
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2. Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells.
Gene References into Functions
  1. Study demonstrated that Spry1 has a role in supporting mitogen-induced vascular hyperplasia, at least in part by promoting Akt/Rb signaling and increasing mitogen-induced cyclinD1 expression and decreasing p27Kip1 expression. PMID: 29105817
  2. Loss of Spry1/2 enhances the survival of effector CD8+ T cells and results in the formation of more protective memory cells. Deleting Spry1/2 in antigen-specific CD8+ T cells may have therapeutic potential for enhancing the survival and functionality of effector and memory CD8+ T cells in vivo. PMID: 30126987
  3. Inhibition of miR-29b could attenuate atherosclerosis by inhibiting the SPRY1/MAPK signaling pathway and inflammation in aorta. PMID: 29398368
  4. modulation of stromal paracrine signaling and extracellular matrix remodeling by SPRY1 regulates mammary epithelial morphogenesis during postnatal development. PMID: 27621461
  5. Here, we present a novel mouse model of pheochromocytoma consisting of double-heterozygous mice for Pten and Sprouty1 (Spry1), which leads to pheochromocytomas that appear at earlier onset and grow at a higher rate than those from Pten+/- mice. PMID: 26830459
  6. Cosuppression of Sprouty and Sprouty-related negative regulators of FGF signalling in prostate cancer PMID: 26075267
  7. Sprouty gain of function disrupts lens cellular processes and growth by restricting receptor tyrosine kinase signaling. PMID: 26375880
  8. In vivo analysis of thyroid glands from Spry1 knockout mice reveals that Spry1 induces a senescence-associated secretory phenotype via activation of the NFkappaB pathway. PMID: 24270409
  9. showed that hSpry1 overexpression prevents VEGF secretion PMID: 24510305
  10. Spry1 and Spry2 coordination is required for normal development of the external genitalia in mice PMID: 24361260
  11. conjunctival epithelial Spry1 and Spry2 redundantly promote eyelid closure. PMID: 24055172
  12. Findings demonstrate that Pokemon suppresses Sprouty1 expression through a miR-21-mediated mechanism, affecting the growth and proliferation of liver cancer cells. PMID: 23355454
  13. ISG15 mRNA expression and IFN-dependent antiviral responses are enhanced in Spry1,2,4 triple knock-out mouse embryonic fibroblasts, consistent with negative feedback regulatory roles for Spry proteins in IFN-mediated signaling. PMID: 23074222
  14. When Spry1 and Spry2 loss-of-function occurs in the context of heterozygosity for a null allele of the tumor suppressor gene Pten, there is a striking increase in prostatic intraepithelial neoplasia and evidence of neoplastic invasion. PMID: 23150596
  15. To determine whether modulating RTK signalling may overcome the abnormal nephrogenesis of Fraser syndrome, we introduced a single null Sprouty1 allele into Fras1(bl/bl) mice, reducing the ureteric bud's expression of this anti-branching molecule. PMID: 23064016
  16. investigation of role of Spry1: Overexpression of Spry1 in transgenic mice leads to lower body fat, reduced bone loss, and normal metabolic function (i.e., prevents liver steatosis/glucose intolerance) compared with Spry1-negative transgenic mice. PMID: 22142492
  17. findings identify Spry1 as a candidate tumor-suppressor gene in medullary thyroid carcinoma PMID: 22158037
  18. Studies implicate Spry1 as a novel regulator of erythropoiesis during anemia, transducer of EPO/EPOR signals, and candidate suppressor of Jak2 activity. PMID: 22508938
  19. SHP2, a major determinant of balance between mESC self-renewal and differentiation, directly regulates Spry1 activity to modulate ERK1/2 signaling and lineage-specific differentiation in mESCs PMID: 21595564
  20. Spry1/Spry2 highly expressed in lateral pterygoid and temporal muscles. combined inactivation of Spry1 and Spry2 results in muscle overgrowth disrupting normal glenoid fossa development. TMJ condyle and disc develop independently of the mandibular fossa. PMID: 22328578
  21. Sprouty genes are essential for the normal development of epibranchial ganglia in the mouse embryo. PMID: 21806979
  22. Corneal epithelial precursors in Spry1 and -2 double mutants showed increased proliferation with elevated expression of Erm and DUSP6 and decreased expression of the corneal differentiation marker K12. PMID: 21743007
  23. Using deletion mutants we identified the N-terminus and the CR conserved region (CR) 3 of E1A- and the C-terminal half of Spry1, which contains the highly conserved Spry domain, as the essential sites for direct interaction between Spry and E1A. PMID: 21518456
  24. Sprouty genes prevent excessive FGF signalling in multiple cell types throughout development of the cerebellum. PMID: 21693512
  25. Spry1 over expression inhibits primitive hematopoietic progenitor and erythroblastic cell development and expansion while having no obvious effect on endothelial cell development PMID: 21483770
  26. report that in Spry1, Spry2 compound mutant embryos, the otic placode is increased in size PMID: 21362415
  27. the role of miR-29c in a previously unrecognized signaling cascade involving Spry1 and Rho kinase activation. PMID: 21310958
  28. Phosphatidylinositol-specific phospholipase C (PLC)-gamma was identified as a partner of the Spry1 and Spry2 proteins. PMID: 20719962
  29. Results suggest that SPRY1 is an endogenous angiogenesis inhibitor. PMID: 20813052
  30. Spry1 is a critical regulator of adipocyte differentiation and mesenchymal stem cell (MSC) lineage allocation, potentially acting through regulation of CEBP-beta and TAZ. PMID: 20410440
  31. These data suggest that Spry1 is an important regulator of craniofacial and cardiac morphogenesis and perturbations in Spry1 levels may contribute to congenital disorders involving tissues of neural crest origin. PMID: 20459789
  32. demonstrate that Sprouty1 (Spry1) is expressed in quiescent Pax7(+) satellite cells in uninjured muscle, downregulated in proliferating myogenic cells after injury, and reinduced as Pax7(+) cells re-enter quiescence. PMID: 20144785
  33. Fgf10 cooperates with Gdnf to promote Kidney morphogenesis, and can compensate for the loss of Gdnf/Ret in the absence of Spry1. PMID: 20084103
  34. sprouty1 represents a physiologically relevant target gene of WT1 during kidney development PMID: 12882970
  35. Spry1(-/-) embryos have supernumerary ureteric buds, resulting in the development of multiple ureters and multiplex kidneys. PMID: 15691764
  36. Spry1 uses a novel mechanism to bring about differential effects on T cell receptor signaling through the same receptor, depending on the differentiation state of the T cell. PMID: 16670312
  37. Epithelial cysts develop in Spry1-deficient kidneys that share several molecular characteristics with those observed in human disease, suggesting that Spry1 null mice may be useful animal models for cystic hyperplasia. PMID: 17022962
  38. Results suggest that constitutive expression of Spry1 in chondrocytes results in attenuated FGFR2 degradation, sustained ERK activation, and up-regulation of p21Cip and STAT1 causing dysregulated chondrocyte proliferation and terminal differentiation. PMID: 18582454
  39. Sprouty1 can modulate ERK signaling downstream of Ret, independent of Grb2/Sos/Ras, during renal morphogenesis PMID: 19056869
  40. Fgf4 positively regulated Pea3, Sprouty1, and 2 expression in chick limb mesenchyme. PMID: 19384958
  41. Sprouty1 induced by TCR signal negatively regulates further TCR signaling by interacting with proximal signaling molecules in immune synapse, providing a novel regulatory mechanism of T cells. PMID: 19915061

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Subcellular Location
Cytoplasm. Membrane; Peripheral membrane protein. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).
Protein Families
Sprouty family
Database Links
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