Recombinant Human Protein Sprouty Homolog 2 (SPRY2) Protein (His&Myc)

Name: Recombinant Human Protein Sprouty Homolog 2 (SPRY2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00900P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Protein Sprouty Homolog 2 (SPRY2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O43597
Target Symbol	SPRY2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT
Expression Range	1-315aa
Protein Length	Full Length
Mol. Weight	42.1 kDa
Research Area	Cardiovascular
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	Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2. Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis. Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells. Inhibits CBL/C-CBL-mediated EGFR ubiquitination.
Subcellular Location	Cytoplasm, cytoskeleton. Cell projection, ruffle membrane.
Protein Families	Sprouty family
Database References	HGNC: 11270 OMIM: 602466 KEGG: hsa:10253 STRING: 9606.ENSP00000366306 UniGene: Hs.18676
Associated Diseases	IgA nephropathy 3 (IGAN3)

Gene Functions References

Overexpression of miR-592 promotes GC proliferation, migration, and invasion and induces the EMT via the PI3K/AKT and MAPK/ERK signaling pathways by inhibiting Spry2, suggesting a potential therapeutic target for Gastric cancer. PMID: 29949784
nuclear Spry2 acts as a molecular link which co-ordinates airway and vascular growth of the cardiopulmonary system. PMID: 29409968
activation of ERK1/2 signaling was required for hCG-induced up-regulation of SPRY2 expression. Further, SPRY2 knockdown attenuated the AREG-induced COX-2 expression and PGE2 production by inhibiting AREG-activated ERK1/2 signaling. PMID: 27539669
Result demonstrated that SPRY2 low-expression was significantly associated with unfavorable prognosis of gastric adenocarcinoma and that SPRY2 could inhibit FGFR2-induced ERK phosphorylation and suppress FGFR2-elicited gastric cancer cell proliferation and invasion. PMID: 28002800
Sprouty2 inhibits amphiregulin-induced down-regulation of E-cadherin and cell invasion in human ovarian cancer cells. PMID: 27835572
Sprouty2 (Spry2), a negative regulator of the extracellular signal regulated kinase/mitogen-activated protein kinase (Erk/MAPK) signalling pathway, was a downstream target of miR-122-5p possibly involved in regulating the keratinocyte proliferation. PMID: 27943426
results shows the involvement of Spry2 in regulation of FosB and Runx2 genes, MAPK signaling and proliferation of mesenchymal stem cells. PMID: 28387432
MYB acts on MAPK signaling by directly regulating transcription of the gene encoding the negative modulator SPRY2. PMID: 27748374
ZEB1 upregulation by SPRY2 results from the combined induction of ETS1 transcription factor and the repression of microRNAs (miR-200 family, miR-150) that target ZEB1 RNA. Moreover, SPRY2 increased AKT activation by epidermal growth factor, whereas AKT and also Src inhibition reduced the induction of ZEB1. PMID: 26455323
upregulated in human CRC. Suppression of SPRY2 repressed AKT2 and EMT-inducing transcription factors and significantly increased E-cadherin expression. Concurrent downregulation of SPRY1 and SPRY2 also increased E-cadherin and suppressed mesenchymal markers in colon cancer cells. PMID: 26434583
In cells harbouring a K-Ras mutation the serine conversion weakens the reduction of migration velocity indicating that dependent on the status of K-Ras the serine influences Sprouty2 functions differently. PMID: 26727965
Increased nuclear localization of p21(WAF1/CIP1) in SPRY2 downregulated colon cancer cells may explain the inhibition of cell proliferation in colon cancer cells. PMID: 26293890
Data suggest a common mechanism by which DNA methyltransferase1 (DNMT1) and hypoxia inducible factors HIF1alpha/HIF2alpha regulate Sprouty2 (Spry2) transcription. PMID: 28196140
We showed that Spry2 is a novel unfolded protein response target and its upregulation is dependent on PERK. PMID: 28246293
has an inhibitory role in TGFbeta signaling pathway in lens epithelial cells PMID: 27415760
these results establish SPRY2 as a critical negative regulator of BCR-mediated MAPK-Erk signaling in chronic lymphocytic leukemia , thereby providing one of the molecular mechanisms to explain the clinical heterogeneity of chronic lymphocytic leukemia. PMID: 26809508
spry2 can inhibit MM cell growth and survival with a concomitant reduction in phosphorylation of extracellular signal-regulated kinases 1 and 2 in vitro and in vivo. PMID: 27016275
data suggest that Spry2 acts as a scaffold to bring more pVHL/associated E3 ligase in proximity of HIF1alpha and increase its ubiquitylation and degradation. This represents a novel action for Spry2 in modulating biological processes regulated by HIFalpha subunits. PMID: 27281823
MiR-122 could act as a tumor promoter and potentially target Sprouty2. MiR-122 promotes renal cell carcinoma cell proliferation, migration, and invasion. PMID: 28231730
miR27b promotes the migration and invasion of gastric cancer cells via inhibition of SPRY2mediated ERK signaling. PMID: 26781754
Arg119Trp variant in the SPRY2 gene was identified as the probable IgA nephropathy-causing mutation. This variant is responsible for inhibition of the MAPK/ERK1/2 pathway. PMID: 25782674
SPRY2, counter to its roles in other cancer settings, promotes glioma cell and tumor growth and cellular resistance to targeted inhibitors of oncogenic RTKs PMID: 25934697
Data show that proto-oncogene protein B-raf (BRAF) inhibition induces c-Jun N-terminal kinase (c-JUN) expression and c-JUN abundance and activation by down-regulating SPRY2/4 protein expression. PMID: 26286024
The purpose of this study was to determine whether SPRY2 might have antiinflammatory effects on rheumatoid arthritis fibroblast-like synoviocytes. PMID: 26265114
miR21 may represent a negative regulator involved in the downregulation of SPRY2 in MM. PMID: 25633921
No association between SPRY2, single-nucleotide polymorphisms, and nonsyndromic cleft lip with or without cleft palate risk were observed in this cohort of patients. PMID: 25339627
A decrease in SPRY2 and RECK expression by nickel-induced miR-21 may promote invasiveness in lung cancer cells. PMID: 26026961
Sprouty 2 protein, but not Sprouty 4, is an independent prognostic biomarker for human epithelial ovarian cancer. PMID: 25630587
Results suggest a link between placental SPRY2 mRNA levels and placental growth, which may be modulated by maternal metabolic status and placental inflammation. PMID: 24969401
This study reveals the loss of SPRY2 in HGSC and indicates an important tumor-suppressive role for SPRY2 in mediating the stimulatory effect of EGF on human EOC progression. PMID: 25533808
CK1 activity and binding are necessary for SPRY2 inhibition of FGF-stimulated neurite outgrowth in PC12 cells PMID: 24469046
Data indicate that the proliferation and survival rates of HEK293T cells transfected with pDC315/hSPRY2 were significantly higher than those transfected with pDC315/EGFP (green fluorescent proteins). PMID: 24796743
Mechanistic model of EGFR endocytosis to determine the relative contributions of three parallel pathways of MIG6, ubiquitin ligase CBL and Sprouty2. PMID: 24445374
The ERK-MAPK signaling pathway is regulated by Sprouty2 expression via a miR-21-mediated mechanism during mesenchymal stem cell differentiation. PMID: 23239100
SPRY2 and MIG6 are important regulators of wild-type and mutant EGFR trafficking and points to an EGFR expression-independent function of SPRY2 in the regulation of ERK activity that may impact cellular sensitivity to EGFR inhibitors PMID: 23868981
involvement of PAX9, EDA, SPRY2, SPRY4, and WNT10A as risk factors for MLIA. uncovered 3 strong synergistic interactions between MLIA liability and MSX1-TGFA, AXIN2-TGFA, and SPRY2-SPRY4 gene pairs. 1st evidence of sprouty genes in MLIA susceptibility. PMID: 24554542
we reveal that SPRY2 expression is regulated by FOXO3a and beta-catenin nuclear activity in colon cancer PMID: 23624922
Increased SPRY2 expression during chronic viral infection reduces T cell polyfunctionality. PMID: 24292711
hypothesize that the level of SPRY2 expression contributes to MAPK/ERK pathway output and accounts for BRAF V600E+ and clinical heterogeneity in papillary thyroid cancer PMID: 24094449
Sprouty2 (but not Sprouty4) has a role in inhibition of cell proliferation and migration of osteosarcoma cells PMID: 23831057
SPRY2 is an important regulator of branching morphogenesis and epithelial to mesenchymal transition in the mammary gland. PMID: 23573284
Our results have raised the possibility that Spry2 might play a role in the pathogenesis and progression of renal cell carcinoma. PMID: 23688375
Data suggest epidermal growth factor induced the expression of c-MYC, which promoted the expression of mature miR-23a, miR-24-2, and miR-27a and subsequently decreased expression of Sprouty2 (SPRY2). PMID: 23649631
miR-27a regulates MET, EGFR, and Sprouty2 in lung cancer. PMID: 23650389
SPRY2, PTEN, and PP2A status is an important determinant of prostate cancer progression. PMID: 23434594
In conclusion, SPRY2 is an important tumour suppressor in prostate cancer since its loss drives the PI3K/AKT pathway via functional interaction with the ErbB system. PMID: 22649008
G Protein-regulated inducer of neurite outgrowth (GRIN) modulates Sprouty protein repression of mitogen-activated protein kinase (MAPK) activation by growth factor stimulation PMID: 22383529
ITSN1 binds Pro-rich regions in both Cbl and Spry2, and interaction of ITSN1 with Spry2 disrupts Spry2-Cbl interaction, resulting in enhanced ubiquitylation of the EGFR. PMID: 22158968
A significant association of rs10906115 in CDC123/CAMK1D and rs1359790 near SPRY2 was identified with type 2 diabetes in a Japanese population. PMID: 21909839
analysis of regulation of cellular levels of Sprouty2 protein by prolyl hydroxylase domain and von Hippel-Lindau proteins PMID: 22006925

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.