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1008750-58-0

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1008750-58-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1008750-58-0 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,0,0,8,7,5 and 0 respectively; the second part has 2 digits, 5 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 1008750-58:
(9*1)+(8*0)+(7*0)+(6*8)+(5*7)+(4*5)+(3*0)+(2*5)+(1*8)=130
130 % 10 = 0
So 1008750-58-0 is a valid CAS Registry Number.

1008750-58-0Downstream Products

1008750-58-0Relevant articles and documents

Structure-Activity relationship studies on acremomannolipin A, the potent calcium signal modulator with a novel glycolipid structure 4: Role of acyl side chains on d-mannose

Tsutsui, Nozomi,Tanabe, Genzoh,Ikeda, Nami,Okamura, Saika,Ogawa, Marika,Miyazaki, Kuniko,Kita, Ayako,Sugiura, Reiko,Muraoka, Osamu

, p. 250 - 271 (2016/06/09)

As part of an ongoing study on the structure-Activity relationship of acremomannolipin A (1)-the novel glycolipid isolated from Acremonium strictum possessing potent calcium signal-modulating activity-the role of acyl substituents on the d-mannose moiety was examined. Three partially deacylated homologs (2a-2c) and 20 homologs (2d-2w) bearing different acyloxy side chains were synthesized via the stereoselective β-mannosylation of appropriately protected mannosyl sulfoxides (3) with d-mannitol derivatives (4), and their calcium signal-modulating activities were examined. The activities of 2a-2c were completely lost. Homologs bearing relatively short acyloxy groups at C-3, C-4, and C-6 positions (2t-2v) exhibited less activity than 1, whereas a heptanoyl homolog (2w: C7) maintained activity nearly equal to that of 1. When the acyl groups at these three positions were substituted by an octanoyl group (2i: C8), the activity was completely lost. On the other hand, of the 10 homologs in which the octanoyl at C-2 was substituted by other acyloxy moieties (2j-2s), three (2m: C7, 2n: C9, 2o: C10) maintained potent activity. These results suggested that peracylated mannose structure is critical for calcium signal-modulating activity, and this activity is precisely dependent on the length of four acyl side chains on d-mannose.

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