protein

MERS-CoV Spike/S1 Protein (CHO, hFc)

HY-P79037

5 μg;10 μg;50 μg

80;130;360 USD

MERS-CoV Spike/S1 Protein (CHO, hFc)

proteins

CHO

5 μg;10 μg;50 μg

80;130;360 USD

MERS-CoV Spike/S1 Proteinas, a crucial component of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV), mediates viral entry into host cells by binding to the host receptor DPP4. The Spike/S1 protein initiates the infection process and is a key target for antiviral strategies. Understanding its structure and interactions is vital for developing effective interventions against MERS-CoV. MERS-CoV Spike/S1 Protein (CHO, hFc) is the recombinant Virus-derived MERS-CoV Spike/S1 protein, expressed by CHO , with C-hFc labeled tag.

Virus

ABCD2, an ATP-dependent transporter belonging to the ATP-binding cassette (ABC) family, plays a crucial role in facilitating the transport of very long-chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen. Similar to ABCD1, ABCD2 exhibits fatty acyl-CoA thioesterase (ACOT) and ATPase activities. According to the proposed model, VLCFA-CoA is transported in an ATP-dependent manner into peroxisomes after the hydrolysis of VLCFA-CoA, mediated by ABCD2's ACOT activity (probable). Notably, ABCD2 shares overlapping substrate specificities with ABCD1, particularly towards saturated fatty acids (FA) and monounsaturated FA (MUFA). However, ABCD2 demonstrates a distinct substrate preference for shorter VLCFA (C22:0) and polyunsaturated fatty acids (PUFA) such as C22:6-CoA and C24:6-CoA, as observed in vitro. This substrate specificity suggests a potential regulatory role for ABCD2 in very long-chain fatty acids (VLCFAs) and energy metabolism, particularly in the degradation and biosynthesis of fatty acids through beta-oxidation.

Spike glycoprotein; S; S glycoprotein; E2; Peplomer protein; Spike Protein, S1 Subunit

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4, 8% trehalose.

Room temperature in continental US; may vary elsewhere.