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S1444

Sigma-Aldrich

Anti-Sprouty 2 (N-Terminal) from rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-IGAN3, Anti-hSPRY2

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 32-35 kDa (doublet)

species reactivity

human, canine

technique(s)

immunoprecipitation (IP): 5-10 μg using 293-T transfected with human Sprouty 2.
indirect immunofluorescence: 2-4 μg/mL using 293-T cells transfected with human Sprouty 2.
western blot: 0.5-1.0 μg/mL using MDCK (Madin Darby canine kidney) cells.

UniProt accession no.

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SPRY2(10253)

General description

Rabbit polyclonal anti Sprouty 2 (N-Terminal) antibody recognizes Sprouty 2 by immunoblotting (doublet at approx 32-35 kDa), immunofluorescence and immunoprecipitation.
Sprouty 2 was first isolated in Drosophila as a negative regulator of receptor tyrosine kinase signaling (RTK). In vertebrates, the family is composed of four members, Sprouty 1, 2, 3 and 4. Human Spry2 encodes 315 amino acids protein, postranslationally modified by palmytoilation, and by phosphorylation of serine and tyrosine residues. When expressed in COS cells, Spry2 is localized to the cytoplasm and co-localized with microtubule proteins. Upon EGF stimulation, it is translocated to membrane ruffles. Sprouty 1 and 2 inhibit FGF- and VEGF-induced endothelial cell proliferation, at least in part, by repressing pathways leading to p42/44 MAP kinase activation. The role of Sprouty 2 in EGF-mediated MAP kinase signaling is less clear. It was recently shown that Spry can function both as a negative and positive regulator of EGFR mediated MAP kinase signaling. Interaction of Spry2 with Cbl (an E3-ubiquitin ligase) interferes with the ability of hSpry2 to inhibit EGF signaling by specifically intercepting c-Cbl mediated effects on receptor down regulation. Phosphorylation of Spry 2 on Tyr55 leads to its association with c-Cbl. This association prevents formation of an EGF receptor-Cbl complex, consequently inhibiting ubiquitination and down regulation of the latter.
Sprouty proteins are ligand-inducible, negative regulators of RTK signaling pathways that modulate cellular growth, differentiation, and movement. Sprouty 2 (Spry2) mediates apoptosis control by c-Cbl sequestration and growth factor receptor signaling. Additionally, Spry2 downregulates EGFR ubiquitination and endocytosis, and thereby potentiates Ras/ERK signaling. Decreased Spry2 expression has been associated with poor prognosis in breast cancers . Anti-Sprouty 2 (N-Terminal) is specific for Sprouty 2 (doublet at approx. 32-35 kDa). The antibody reacts with human, dog and mouse Spry2.

Immunogen

This sequence differs in one amino acid from the human sequence.
synthetic peptide corresponding to amino acids 79-98 of mouse Sprouty 2 (Spry 2), conjugated to KLH via a C-terminal added lysine residue.

Application

Anti-Sprouty 2 (N-Terminal) is suitable for use in immunoblotting using MEF lysates . The antibody can also be used for immunoprecipitation (5-10 μg using 293-T transfected with human Sprouty 2) and indirect immunofluorescence (2-4 μg/mL using 293-T cells transfected with human Sprouty 2).
Rabbit polyclonal anti Sprouty 2 (N-Terminal) antibody is used to tag Sprouty 2 for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of Sprouty 2 in cell signaling cascades such as the EGFR mediate MAP kinase pathway.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Jung-Chien Cheng et al.
Oncotarget, 7(49), 81645-81660 (2016-11-12)
Similar to Drosophila Sprouty (SPRY), mammalian SPRY proteins inhibit the receptor tyrosine kinase-mediated activation of cellular signaling pathways. SPRY2 expression levels have been shown to be down-regulated in human ovarian cancer, and patients with low SPRY2 expression have significantly poorer
Marta Vaquero et al.
Journal of the American Society of Nephrology : JASN, 30(8), 1398-1411 (2019-07-14)
Studies in mice suggest that perturbations of the GDNF-Ret signaling pathway are a major genetic cause of congenital anomalies of the kidney and urinary tract (CAKUT). Mutations in Sprouty1, an intracellular Ret inhibitor, results in supernumerary kidneys, megaureters, and hydronephrosis
Gisela Altés et al.
Scientific reports, 14(1), 19479-19479 (2024-08-23)
Genes of the Sprouty family (Spry1-4) are feedback inhibitors of receptor tyrosine kinases, especially of Ret and the FGF receptors. As such, they play distinct and overlapping roles in embryo morphogenesis and are considered to be tumor suppressors in adult
Jacqueline M Mason et al.
Trends in cell biology, 16(1), 45-54 (2005-12-13)
Receptor tyrosine kinases (RTKs) control a wide variety of processes in multicellular organisms, including proliferation, differentiation, migration and survival. Their activity is tightly controlled through the coordinated action of both positive and negative regulators that function at multiple levels of
Alice M Walsh et al.
Journal of cell science, 126(Pt 19), 4339-4348 (2013-07-23)
The duration and specificity of epidermal growth factor receptor (EGFR) activation and signaling are determinants of cellular decision processes and are tightly regulated by receptor dephosphorylation, internalization and degradation. In addition, regulatory proteins that are upregulated or activated post-transcriptionally upon

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