Dog E-Selectin / CD62E (SELE) Protein

Product specifications

Proteins and Peptides

E-Selectin / CD62E (SELE)

E. coli

Dog

Unconjugated

Molecular Weight: Calculated MW: 28.3 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Trp23-Val240
Tag: N-terminal His tag

Recombinant

> 95%

50 µg

100 µg

200 µg

500 µg

1 mg

Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 5-7 working days.

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.

No

P33730

ELAM,ESEL,CD62E,ELAM1,LECAM2,selectin-e,E-selectin,CD62 antigen-like family member E,Endothelial leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 2

Protein SELE

RUO

This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Selectin E (SELE) is an adhesion molecule expressed on activated endothelial cells in response to inflammatory cytokines such as TNF-α and IL-1β, playing a pivotal role in the recruitment of leukocytes to sites of inflammation. It mediates the rolling and tethering of leukocytes on the endothelium by binding to specific glycoprotein ligands on the surface of leukocytes, such as PSGL-1, facilitating their migration into tissues. SELE is crucial in early-stage inflammatory responses and is involved in various pathophysiological processes, including atherosclerosis, autoimmune diseases, and cancer metastasis. Dysregulation of SELE expression has been associated with increased endothelial dysfunction and vascular inflammation, contributing to the development of cardiovascular diseases. Its expression is transient and tightly regulated by transcriptional mechanisms, ensuring that leukocyte recruitment occurs precisely during inflammatory responses. Therapeutic targeting of SELE has been explored to mitigate excessive inflammation, with strategies focusing on blocking its interaction with ligands to prevent leukocyte adhesion and infiltration. Additionally, SELE is being investigated as a biomarker for endothelial activation and vascular inflammation in conditions such as sepsis and chronic inflammatory disorders. Its role in mediating cell adhesion under shear stress highlights its importance in maintaining vascular integrity during immune surveillance and inflammatory responses.

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