Type of antibody:
Primary antibodies, Recombinant antibodies
recombinant human IgG1
Alternative names:

Specifications for SLP-76 Antibody, anti-human, REAfinity™


Clone REA427 recognizes the human SH2 domain-containing leukocyte protein of 76 kDa (SLP-76) regardless of phosphorylation status. SLP-76 is a signal-transducing tyrosine phosphoprotein also known as lymphocyte cytosolic protein 2 (LCP2). It is involved in T cell antigen receptor–mediated signaling and is highly expressed in spleen, thymus, and peripheral blood leukocytes. The adapter molecule SLP-76 plays a central roles in T cell activation by recruiting enzymes and other adapters into multiprotein complexes that coordinate highly regulated signal transduction pathways. TCR stimulation facilitates phosphorylation of the TCRζ chains by the Src family kinase Lck, which allows for the recruitment and activation of the protein tyrosine kinase Zap-70. Phosphorylation of the essential adapter protein SLP-76 by Zap-70 creates docking sites for SH2 domain-containing adapter and effector proteins. The Grb2-related adapter, Gads, recruits the adapter SLP-76. SLP-76 recruits other signaling proteins, thereby inducing the assembly of multiprotein complexes.
Additional information: Clone REA427 displays negligible binding to Fc receptors.

Alternative names


Detailed product information

Technical specifications

Isotyperecombinant human IgG1
Isotype controlREA Control Antibody (I), human IgG1
Hosthuman cell line
Type of antibodyPrimary antibodies, Recombinant antibodies
Alternative names of antigenLCP2, SLP76
Molecular mass of antigen [kDa]60
Distribution of antigenleukocytes, spleen
Entrez Gene ID3937
RRIDAB_2653477, AB_2653478, AB_2653479, AB_2653480, AB_2653481, AB_2653476

Resources for SLP-76 Antibody, anti-human, REAfinity™


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References for SLP-76 Antibody, anti-human, REAfinity™


  1. Sela, M. et al. (2011) Sequential phosphorylation of SLP-76 at tyrosine 173 is required for activation of T and mast cells. EMBO J. 30(15): 3160-3172
  2. Jackman, J. K. et al. (1995) Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells. J. Biol. Chem. 270(13): 7029-7032
  3. Coussens, N. P. et al. (2013) Multipoint binding of the SLP-76 SH2 domain to ADAP is critical for oligomerization of SLP-76 signaling complexes in stimulated T cells. Mol. Cell. Biol. 33(21): 4140-4151

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