Recombinant Human KLRG1 protein (denatured) (His tag N-Terminus)
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Recombinant Human KLRG1 protein (denatured) (His tag N-Terminus) is a Human Fragment protein, in the 60 to 189 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
CLEC15A, MAFA, MAFAL, KLRG1, Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human KLRG1 protein (denatured) (His tag N-Terminus) (AB139253)
15% SDS-PAGE analysis of 3 µg ab139253.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
KLRG1 serves as a modulator of immune responses by delivering inhibitory signals that regulate immune cell cytotoxicity and cytokine production. It is not part of a larger protein complex but interacts with other molecules on the cell surface to perform its role. The engagement of its ligands mediates the reduction of immune responses which is important during chronic infections and cancer to prevent excessive immune activation.
Pathways
Several immune regulatory pathways involve KLRG1. It notably participates in the balance between immune activation and inhibition within the immune system. KLRG1 interacts with signaling pathways such as those regulated by T-cell receptor (TCR) signaling and NK cell activation. Related proteins in these pathways include CD226 and NKG2A which also play a role in determining the immune cell response.
Specifications
Form
Liquid
General info
Function
Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
Target data
Product promise
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