SELP Specific Neutra™ Antibody Products

Product list

The 140 kDa protein selectin P (SELP) is stored within the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Moreover, following platelet degranulation and activation, this protein experiences redistribution to the plasma membrane, promoting the interaction between platelets and leukocytes or activated endothelial cells.

Its Gene ID: 6403, UniProtKB ID: P16109, and OMIM ID: 173610.

SELP Pathway

Upon tissue injury or infection, a sequential recruitment process guides neutrophils from the bloodstream to the surrounding tissue. Binding of SELP to P-selectin glycoprotein ligand-1 (PSGL-1) on the neutrophil surface initiates a distinct intracellular signaling pathway, resulting in the affinity activation of lymphocyte-function-associated antigen-1 (LFA-1). The interplay between selectins and their counter-receptors enables the initial interaction of neutrophils with the endothelium, followed by the subsequent rolling of neutrophils along the endothelial surface. The integrin activation dysregulation is related to severe pathological conditions, and is induced by SELP in neutrophiles.

Fig.1 Signaling cascade triggered by SELP-ligand binding. (Cappenberg, Kardell & Zarbock, 2022) Fig.1 Neutrophil inside-out signaling cascade triggered by SELP-ligand binding.¹

Antibodies in SELP related Therapeutics

Endothelial cells maintain chronic expression of SELP, and the interaction between sickled red blood cells (RBCs) and endothelial SELP plays a pivotal role in initiating the vaso-occlusive cascade through downstream engagement of multiple adhesion receptor/ligand pairs. Consequently, diverse innovative antibodies have been developed with the aim of enhancing the effectiveness of therapy for blood disorders through the targeting of SELP.

Monoclonal antibody inhibiting SELP can improve microvascular flow dynamics

SELP monoclonal antibody binding to and inhibiting P-selectin, effectively disrupts its interaction with the ligand, PSGL-1. By engaging SELP on the activated endothelium and platelets, the medication impedes interactions among endothelial cells, platelets, RBCs, and leukocytes. This interference leads to improved microvascular flow dynamics and the potential reversal of specific established aberrant adhesive interactions.

Fig.2 SELP monoclonal antibody. (Morikis, et al., 2021) Fig.2 Schematic diagram of SELP monoclonal antibody.²

Function of anti-SELP antibodies in SCD

Neutrophils play a crucial role in safeguarding the host against invading pathogens; however, in sickle cell disease (SCD), they can contribute to disease progression by adhering to inflamed microvascular networks in peripheral tissues throughout the body. In the inflammatory response, leukocytes extravasate from the bloodstream through SELP and migrate to sites of tissue insult by activating integrins crucial for combating pathogens. In the context of vaso-occlusion associated with SCD, neutrophils undergo activation during tethering and rolling on selectins upregulated on the activated endothelium lining blood vessels. Investigating anti-SELP antibodies holds promise for advancing therapeutic approaches to managing SCD.

Creative Biolabs delivers an assortment of anti-SELP antibody products, expressively generated through recombinant methods. Additionally, customization options are available for tailoring SELP-based blocking/neutralizing antibodies to meet specific requirements.

REFERENCES

Cappenberg, Anika, Marina Kardell, and Alexander Zarbock. "Selectin-mediated signaling—Shedding light on the regulation of integrin activity in neutrophils." Cells 11.8 (2022): 1310.
Morikis, Vasilios A., et al. "Targeting neutrophil adhesive events to address vaso-occlusive crisis in sickle cell patients." Frontiers in Immunology 12 (2021): 663886.

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