LSP1 (pS190)
Lymphocyte-specific protein 1

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Product Preparation
A synthetic peptide corresponding to the C-terminus with a phosphorylated serine of human lymphocyte-specific protein 1. This sequence is identical to mouse species
Leukocyte-specific protein 1 (LSP1), an F-actin binding protein and a major downstream substrate of p38 mitogen-activated protein kinase as well as protein kinase C, is important in leukocyte chemotaxis. Two serine residues at positions 204 and 252 are potential phosphorylation sites. The amino acid sequences surrounding these two sites are in agreement with the consensus sequence (Xaa-Xaa-Hyd-Xaa-Arg-Xaa-Xaa-Ser-Xaa-Xaa) for phosphorylation by MAPKAP kinase 2. Both serine residues in human LSP1 and the corresponding conserved serine residues in human and mouse LSP1 are in the basic C-terminal F-actin binding domain. LSP1 is a substrate for MAPKAP kinase 2 in vitro and that the phosphorylation sites are located in the basic C-terminal domain of LSP1.
The Rabbit IgG is purified by site-modified Epitope Affinity Purification.
This antibody recognizes ~52 kDa of human LSP1 protein at a phosphorylated serine 252. It does not recognize non-phosphorylated peptides confirmed by dot blot. This antibody also reacts with mouse. The other species are not tested.
This affinity purified antibody is supplied in sterile Tris-buffered saline (pH7.2) containing antibody stabilizer.
The antibodies are stable for 12 months from date of receipt when stored at –20oC. The antibodies can be stored at 2oC-8oC for one month without detectable loss of activity. Avoid repeated freezing-thawing cycles.
Gene ID
Applications/Suggested Working Dilutions
Western Blot
0.1-1 µg/ml
0.01-0.1 µg/ml
2-5 µg/ml
2-10 µg/ml
Flow cytometry
5-10 µg/ml
Order Info
Catalog #: 602-250
Lot #: See the label
Size: 100 ug
Host: Rabbit
Isotyping: Rabbit IgG
Applications: ELISA, WB, IP
Reactivity: Hu, Ms, Rt
Price: $ 299.00
Lixin Liu, et al. LSP1 is an endothelial gatekeeper of leukocyte transendothelial migration. (2005), JEM, 201(3): 409–418.
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