KLRG1 Protein, Human (His-SUMO)

KLRG1 Protein exerts inhibitory effects on NK cells and T-cells by binding to their non-MHC ligands, potentially recognizing "missing self" through conserved sites on classical cadherins like E-cadherin/CDH1, N-cadherin/CDH2, and R-cadherin/CDH4. Existing as a monomer and homodimer connected by disulfide bonds, KLRG1 interacts with PTPN11 and INPP5D via its ITIM motif, suggesting involvement in signal transduction pathways. KLRG1 Protein, Human (His-SUMO) is the recombinant human-derived KLRG1 protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of KLRG1 Protein, Human (His-SUMO) is 136 a.a., with molecular weight of ~31.5 kDa.

The KLRG1 protein exhibits an inhibitory role on the functions of natural killer (NK) cells and T-cells by binding to their non-MHC ligands. It is potentially involved in the recognition of "missing self" by binding to a conserved site on classical cadherins, specifically monitoring the expression of E-cadherin/CDH1, N-cadherin/CDH2, and R-cadherin/CDH4 on target cells. KLRG1 forms a monomer and homodimer that are connected by disulfide bonds. Furthermore, it interacts with PTPN11 and INPP5D through its ITIM motif, potentially participating in signal transduction pathways.

Human

E. coli

N-SUMO;N-6*His

Q96E93 (L60-F195)

10219  [NCBI]

LCQGSNYSTCASCPSCPDRWMKYGNHCYYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLRNNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKKCPFADQALF

Approximately 31.5 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm sterile filtered 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.