Rat E-Selectin (SELE) Protein

Este producto es parte de SELE - selectin E
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312€ (20 µg)

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935106861
info@markelab.com
name
Rat E-Selectin (SELE) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx694310
tested applications
SDS-PAGE

Description

Rat E-Selectin (SELE) Protein is a recombinant Rat protein expressed in HEK293 cells.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Host
HEK293 cells
Origin
Rat
Observed MW
Molecular Weight: Calculated MW: 54.23 kDa  Observed MW (SDS-PAGE): 85 kDa
Sequence Fragment: Met1-Pro494
Tag: C-terminal His tag
Expression
Recombinant
Purity
>95% (SDS-PAGE)
Size 1
20 µg
Size 2
100 µg
Form
Lyophilized Reconstitute in sterile H2O. Do not vortex.
Tested Applications
SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 5% - 8% Trehalose, Mannitol and 0.01% Tween-80.
Availability
Shipped within 5-15 working days.
Storage
Store lyophilized between -20 °C and -80 °C.
Dry Ice
No
UniProt ID
P98105
Gene ID
25544
Alias
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
Background
Protein SELE
Status
RUO
Note
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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