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L4542

Sigma-Aldrich

Anti-phospho-Lck (pTyr505) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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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

species reactivity

human

technique(s)

western blot: 0.1-1.0 μg/mL using full length recombinant human Lck protein.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

target post-translational modification

phosphorylation (pTyr505)

Gene Information

human ... LCK(3932)
mouse ... Lck(16818)
rat ... Lck(313050)

General description

The signalling in T cells is mediated by receptor and non-receptor protein tyrosine kinases (PTK). Among the family of non-receptors PTK, Lck is a lymphoid-specific cytosolic PTK essential for T-cell development and function. Lck is essential for selection and maturation of developing T cells in the thymus. It plays a significant role in T-cell receptors mediated signalling by constitutive association with CD4 and CD8 receptors. In addition, Lck undergoes phosphorylation and activation by association with CD2 molecule. Lck also plays a role in T-cell proliferation in response to IL-2 receptor pathway. The activity of Lck is known to be regulated by phosphorylation of two conserved tyrosine residues, tyrosine 505 (equivalent to tyrosine 529 in c-Src) and tyrosine 394 (equivalent to tyrosine 418 in c-Src). Phosphorylation at Tyr505 stabillizes Lck and renders it biologically inactive.
Anti-phospho Lck (pTyr505) specifically recognizes human Lck (pTyr505). Mouse (100% homology) and chicken (91.7% homology) are expected to react.

Immunogen

synthetic phosphopeptide derived from the region of Lck that is phosphorylated on tyrosine 505. Rat and mouse have 100% homology with human.

Application

A working concentration of 0.1-1.0 μg/mL is recommended for detection of human Lck protein by immunoblotting.

Physical form

Solution in phosphate buffer, pH 7.4, with 1 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.

Preparation Note

The antibody is preadsorbed to remove any reactivity towards a non-phosphorylated Lck.

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


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S J Anderson et al.
Immunology today, 16(2), 99-105 (1995-02-01)
Recent evidence supports the view that p56lck, a non-receptor protein tyrosine kinase, serves as the signaling element that 'senses' synthesis of a functional T-cell receptor beta chain, thereby promoting thymocyte maturation. Here, Steven Anderson and Roger Perlmutter review current data
N Isakov et al.
European journal of biochemistry, 267(12), 3413-3421 (2000-06-10)
Protein tyrosine kinases (PTKs) are critically involved in signaling pathways that regulate cell growth, differentiation, activation, and transformation. It is not surprising, therefore, that viruses acquire effector molecules targeting these kinases to ensure their own replication and/or persistence. This review
Tahir M Razzaq et al.
Immunology, 113(4), 413-426 (2004-11-24)
There is now considerable evidence suggesting that the plasma membrane of mammalian cells is compartmentalized by functional lipid raft microdomains. These structures are assemblies of specialized lipids and proteins and have been implicated in diverse biological functions. Analysis of their
The lck tyrosine protein kinase.
B M Sefton
Oncogene, 6(5), 683-686 (1991-05-01)
C N Levelt et al.
Immunity, 3(2), 215-222 (1995-08-01)
We studied the extent of functional linkage between CD3 sigma and p56lck in pre-TCR-dependent thymocyte development. Differentiation of DN to DP cells was examined by treatment of RAG2/CD3 sigma and RAG1/p56lck double-deficient mice with anti-CD3 epsilon antibodies. The results suggest

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