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SAB4503872

Sigma-Aldrich

Anti-phospho-Fyn (pTyr530) antibody produced in rabbit

affinity isolated antibody

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

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 60 kDa

species reactivity

rat, human, mouse

concentration

~1 mg/mL

technique(s)

ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pTyr530)

Gene Information

human ... FYN(2534)

General description

Tyrosine-protein kinase FYN is a neuronally enriched cytoplasmic protein. It is encoded by the genes mapped to human chromosome 6q21. FYN protein belongs to the proto-oncogene tyrosine-protein kinase, Src family.

Immunogen

The antiserum was produced against synthesized peptide derived from human Fyn around the phosphorylation site of Tyr530.

Immunogen Range: 488-537

Application

Anti-phospho-Fyn (pTyr530) antibody produced in rabbit has been used in immunoprecipitation and immunoblotting.

Biochem/physiol Actions

Tyrosine-protein kinase FYN and phospho-FYN act as signaling systems for spatial memory. Phospho-FYN plays a vital role in the regulation of oligodendrocyte myelination and neurofilament phosphorylation. FYN aids in the development and activation of T cells in various physiological conditions. Overexpression of the FYN gene has been observed in various types of cancer.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Novel modeling of cancer cell signaling pathways enables systematic drug repositioning for distinct breast cancer metastases.
Zhao, et al.
Cancer research, 73, 6149-6163 (2018)
Matthias Schmitz et al.
Molecular neurobiology, 50(3), 923-936 (2014-03-08)
The cellular prion protein (PrPC) is a highly conserved protein whose exact physiological role remains elusive. In the present study, we investigated age-dependent behavioral abnormalities in PrPC-knockout (Prnp0/0) mice and wild-type (WT) controls. Prnp0/0 mice showed age-dependent behavioral deficits in
Feng Xue et al.
Surgical oncology, 33, 108-117 (2020-06-21)
Tyrosine-protein kinase Fyn (FYN) plays a crucial role in Src family, which participates in the signal transduction of brain nerves and the development and activation of T lymphocytes in physiological conditions. We probed into the roles and mechanisms of FYN
Yuta Shimanaka et al.
Nature medicine, 23(11), 1287-1297 (2017-10-17)
Critical to the function of mast cells in immune responses including allergy is their production of lipid mediators, among which only omega-6 (ω-6) arachidonate-derived eicosanoids have been well characterized. Here, by employing comprehensive lipidomics, we identify omega-3 (ω-3) fatty acid
Haley Peckham et al.
Glia, 64(2), 255-269 (2015-10-10)
Fyn, a member of the Src family of nonreceptor tyrosine kinases, promotes central nervous system myelination during development; however the mechanisms mediating this effect remain unknown. Here we show that Fyn phosphorylation is modulated by BDNF in vivo. Concordant with

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