Passa al contenuto
Merck
Tutte le immagini(1)

Documenti fondamentali

C4999

Sigma-Aldrich

Proinsulin C-Peptide (55-89) human

≥95% (HPLC)

Sinonimo/i:

Proinsulin connecting peptide

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali


About This Item

Formula empirica (notazione di Hill):
C153H259N49O52
Numero CAS:
Peso molecolare:
3616.99
Numero MDL:
Codice UNSPSC:
12352209
ID PubChem:
NACRES:
NA.26
Prezzi e disponibilità al momento non sono disponibili

Nome del prodotto

Proinsulin C-Peptide (55-89) human, bioactive peptide hormone

Livello qualitativo

Saggio

≥95% (HPLC)

Stato

powder

Colore

white

Temperatura di conservazione

−20°C

Stringa SMILE

CC(C)C[C@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)CCCNC(N)=N)C(C)C)C(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O

InChI

1S/C153H259N49O52/c1-71(2)55-94(193-134(237)91(40-48-119(222)223)189-148(251)122(78(15)16)200-135(238)86(33-41-105(156)205)179-112(212)67-175-147(250)121(77(13)14)199-136(239)88(35-43-107(158)207)188-139(242)97(58-74(7)8)194-142(245)100(61-120(224)225)197-133(236)90(39-47-118(220)221)182-124(227)80(18)177-129(232)89(38-46-117(218)219)186-130(233)84(29-23-51-167-152(162)163)183-126(229)82(155)27-22-50-166-151(160)161)128(231)172-63-110(210)169-62-109(209)170-68-115(215)201-53-25-31-103(201)145(248)174-64-111(211)176-79(17)123(226)171-65-113(213)180-101(69-203)144(247)196-99(60-76(11)12)141(244)190-92(36-44-108(159)208)149(252)202-54-26-32-104(202)146(249)198-95(56-72(3)4)137(240)178-81(19)125(228)192-96(57-73(5)6)138(241)185-85(37-45-116(216)217)127(230)173-66-114(214)181-102(70-204)143(246)195-98(59-75(9)10)140(243)187-87(34-42-106(157)206)132(235)184-83(28-20-21-49-154)131(234)191-93(150(253)254)30-24-52-168-153(164)165/h71-104,121-122,203-204H,20-70,154-155H2,1-19H3,(H2,156,205)(H2,157,206)(H2,158,207)(H2,159,208)(H,169,210)(H,170,209)(H,171,226)(H,172,231)(H,173,230)(H,174,248)(H,175,250)(H,176,211)(H,177,232)(H,178,240)(H,179,212)(H,180,213)(H,181,214)(H,182,227)(H,183,229)(H,184,235)(H,185,241)(H,186,233)(H,187,243)(H,188,242)(H,189,251)(H,190,244)(H,191,234)(H,192,228)(H,193,237)(H,194,245)(H,195,246)(H,196,247)(H,197,236)(H,198,249)(H,199,239)(H,200,238)(H,216,217)(H,218,219)(H,220,221)(H,222,223)(H,224,225)(H,253,254)(H4,160,161,166)(H4,162,163,167)(H4,164,165,168)/t79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,121-,122-/m0/s1
JEPNOJXFZHBCTB-ZCUALFGZSA-N

Amino Acid Sequence

Arg-Arg-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-Lys-Arg

Descrizione generale

Human proinsulin, the single-chain peptide precursor of insulin, consists of the insulin A and B chains connected by the 31 amino acid C-peptide. Cleavage of proinsulin by proteolytic enzymes produces insulin and free C-peptide. The product here is the 35-mer peptide (Arg−Arg-C-Peptide-Lys-Arg) observed to separate the insulin A and B chains.[1]

Azioni biochim/fisiol

C-Peptide Fragment (55-89) is a fragment derived from the proinsulin C-peptide. C-peptide has cell signaling activity that involves calcium-dependent intracellular signaling. C-Peptide Fragment 55-89 may be used to help researchers understand the role of specific sequences within the C-peptide in binding, conformation and function of C-peptide.
C-Peptide was initially thought to have no intrinsic biological activity. More recent research has identified multiple biological effects of C-peptide, including binding to cell membranes, activation of signaling pathways, and stimulation of Na+,K+-ATPase and endothelial nitric oxide synthetase.[2][3][4] However, the exact function of C-peptide is unclear due to conflicting physiological effects.[5]

Altre note

Lyophilized from 0.1% TFA in H2O

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Scegli una delle versioni più recenti:

Certificati d'analisi (COA)

Lot/Batch Number

Non trovi la versione di tuo interesse?

Se hai bisogno di una versione specifica, puoi cercare il certificato tramite il numero di lotto.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

I clienti hanno visto anche

Slide 1 of 2

1 of 2

Insulina recombinant, expressed in yeast (proprietary host)

Sigma-Aldrich

I2643

Insulina

R S Mughal et al.
Diabetologia, 53(8), 1761-1771 (2010-05-13)
Endothelial cells (ECs) and smooth muscle cells (SMCs) play key roles in the development of intimal hyperplasia in saphenous vein (SV) bypass grafts. In diabetic patients, insulin administration controls hyperglycaemia but cardiovascular complications remain. Insulin is synthesised as a pro-peptide
C-Peptide: A new mediator of atherosclerosis in diabetes.
Vasic, D., and Walcher, D.
Mediators of Inflammation, 858692-858692 (2012)
Proinsulin C-peptide prevents type-1 diabetes-induced decrease of renal Na+-K+-ATPase α1-subunit in rats.
Nordquist L, Shimada K, et al.
Diabetes and Metabolism, 26, 193-199 (2010)
John Wahren et al.
Experimental diabesity research, 5(1), 15-23 (2004-06-17)
New results present C-peptide as a biologically active peptide hormone in its own right. Although C-peptide is formed from proinsulin and cosecreted with insulin, it is a separate entity with biochemical and physiological characteristics that differ from those of insulin.
The conformational protential of porcine proinsulin C-peptide.
Vogt HP, Wollmer A, et al.
Hoppe-Seyler'S Zeitschrift fur Physiologische Chemie, 357, 107-116 (1971)

Questions

Reviews

No rating value

Active Filters

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.