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HPA001231

Sigma-Aldrich

Anti-LYN antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-Tyrosine-protein kinase Lyn antibody produced in rabbit

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About This Item

MDL number:
UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

rat, human, mouse

enhanced validation

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

KGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPG

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LYN(4067)

Immunogen

LYN proto-oncogene, Src family tyrosine kinase

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

LYN (LYN proto-oncogene, Src family tyrosine kinase) gene encodes a non-receptor tyrosine protein kinase that regulates innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines and integrin signaling. It is involved in the antigen receptor mediated tyrosine phosphorylation of CD19. It is activated in response to DNA-damage. Src kinase Lyn interacts with growth arrest and DNA damage protein 34 (GADD34) and negatively regulates genotoxic apoptosis. Mutation in SH2 domain of LYN has been reported in breast cancer. It has also been documented that LYN gene may associate with melanoma and endometrial, lung, and colorectal carcinoma.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST78876

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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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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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C M Roifman et al.
Biochemical and biophysical research communications, 194(1), 222-225 (1993-07-15)
The B cell antigen receptor, mIg, is part of a multimolecular complex including Ig alpha, Ig beta, and CD19. We provide evidence here that upon ligation of mIg CD19 becomes phosphorylated on tyrosine residues. Further, protein tyrosine kinase lyn, which
B S Gaul et al.
The Journal of biological chemistry, 275(21), 16174-16182 (2000-04-05)
The immunoreceptor tyrosine-based activation motif (ITAM) plays a central role in transmembrane signal transduction in hematopoietic cells by mediating responses leading to proliferation and differentiation. An initial signaling event following activation of the B cell antigen receptor is phosphorylation of
A V Grishin et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(18), 10172-10177 (2001-08-23)
Genotoxic stresses activate intracellular signaling molecules, which lead to growth arrest, DNA repair, and/or apoptosis. Among these molecules are the growth arrest and DNA damage protein 34 (GADD34) and the Src-related protein tyrosine kinase Lyn. Here, we report that these
Anna Maria Brunati et al.
The Journal of biological chemistry, 280(22), 21029-21035 (2005-03-30)
Thrombin stimulation of platelets triggers Tyr phosphorylation of several signaling proteins, most of which remain unidentified. In this study, we demonstrate for the first time that hematopoietic lineage cell-specific protein 1 (HS1) undergoes a transient Tyr phosphorylation in human platelets
K Yoshida et al.
The Journal of biological chemistry, 274(49), 34663-34668 (1999-11-27)
The Lyn protein-tyrosine kinase is activated in the cellular response to DNA-damaging agents. Here we demonstrate that Lyn associates constitutively with the SHPTP1 protein-tyrosine phosphatase. The SH3 domain of Lyn interacts directly with SHPTP1. The results show that Lyn phosphorylates

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