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pTH-Related Protein (7-34) amide (human, mouse, rat)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

pTH-Related Protein (7-34) amide is a potent antagonist of the effects of pTH-related protein (1-34) in vitro and in vivo.

Category

Peptide Inhibitors

Catalog number

BAT-015870

CAS number

115695-30-2

Molecular Formula

C153H247N49O37

Molecular Weight

3364.90

pTH-Related Protein (7-34) amide (human, mouse, rat)

Specification
Reference Reading

Synonyms

L-Alaninamide,l-Leucyl-L-Leucyl-L-histidyl-L-a-aspartyl-L-Lysylglycyl-L-Lysyl-L-seryl-L-isoleucyl-L-glutaminyl-L-a-aspartyl-L-Leucyl-L-arginyl-l-arginyl-l-arginyl-l-phenylalanyl-l-phenylalanyl-l-leucy; Hypercalcemia of Malignancy Factor (7-34) amide (human, mouse, rat)

Purity

95%

Density

1.44±0.1 g/cm3

Sequence

LLHDKGKSIQDLRRRFFLHHLIAEIHTA

InChI

InChI=1S/C153H247N49O37/c1-20-82(14)120(147(236)178-86(18)125(214)180-101(46-48-117(207)208)133(222)199-122(84(16)22-3)149(238)197-111(64-93-70-168-76-176-93)145(234)202-123(87(19)204)150(239)177-85(17)124(158)213)200-144(233)105(58-81(12)13)189-139(228)108(61-90-67-165-73-173-90)194-140(229)109(62-91-68-166-74-174-91)193-136(225)104(57-80(10)11)187-137(226)107(60-89-38-27-24-28-39-89)191-138(227)106(59-88-36-25-23-26-37-88)190-131(220)99(44-35-53-171-153(163)164)183-129(218)97(42-33-51-169-151(159)160)182-130(219)98(43-34-52-170-152(161)162)184-134(223)103(56-79(8)9)188-143(232)113(66-119(211)212)195-132(221)100(45-47-115(157)205)185-148(237)121(83(15)21-2)201-146(235)114(72-203)198-128(217)96(41-30-32-50-155)179-116(206)71-172-127(216)95(40-29-31-49-154)181-142(231)112(65-118(209)210)196-141(230)110(63-92-69-167-75-175-92)192-135(224)102(55-78(6)7)186-126(215)94(156)54-77(4)5/h23-28,36-39,67-70,73-87,94-114,120-123,203-204H,20-22,29-35,40-66,71-72,154-156H2,1-19H3,(H2,157,205)(H2,158,213)(H,165,173)(H,166,174)(H,167,175)(H,168,176)(H,172,216)(H,177,239)(H,178,236)(H,179,206)(H,180,214)(H,181,231)(H,182,219)(H,183,218)(H,184,223)(H,185,237)(H,186,215)(H,187,226)(H,188,232)(H,189,228)(H,190,220)(H,191,227)(H,192,224)(H,193,225)(H,194,229)(H,195,221)(H,196,230)(H,197,238)(H,198,217)(H,199,222)(H,200,233)(H,201,235)(H,202,234)(H,207,208)(H,209,210)(H,211,212)(H4,159,160,169)(H4,161,162,170)(H4,163,164,171)/t82-,83-,84-,85-,86-,87+,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,120-,121-,122-,123-/m0/s1

InChI Key

LMYVBBOUSGMYHN-HPMYYUFQSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC1=CNC=N1)C(=O)NC(C(C)O)C(=O)NC(C)C(=O)N)NC(=O)C(CCC(=O)O)NC(=O)C(C)NC(=O)C(C(C)CC)NC(=O)C(CC(C)C)NC(=O)C(CC2=CNC=N2)NC(=O)C(CC3=CNC=N3)NC(=O)C(CC(C)C)NC(=O)C(CC4=CC=CC=C4)NC(=O)C(CC5=CC=CC=C5)NC(=O)C(CCCNC(=N)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC(C)C)NC(=O)C(CC(=O)O)NC(=O)C(CCC(=O)N)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(CCCCN)NC(=O)CNC(=O)C(CCCCN)NC(=O)C(CC(=O)O)NC(=O)C(CC6=CNC=N6)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)N

1. Inactivation by plasma may be responsible for lack of efficacy of parathyroid hormone antagonists in hypercalcemia of malignancy

R L McKee, S A Wimbiscus, J J D'Anza, M P Caulfield, S C Kukreja, M Rosenblatt, J E Fisher Endocrinology . 1994 May;134(5):2184-8. doi: 10.1210/endo.134.5.8156920.

PTH-related protein (PTHrP) has been shown to be a major factor responsible for hypercalcemia of malignancy. PTHrP acts via the PTH/PTHrP receptor, and therefore, PTH antagonists might be expected to reverse the hypercalcemia in malignancy. In the present studies, the PTH antagonists [Tyr34]bovine (b) PTH-(7-34)NH2, [D-Trp12,Tyr34]-bPTH-(7-34)NH2, or PTHrP-(7-34)NH2, were administered to hypercalcemic athymic nude mice bearing a human squamous cell carcinoma of the lung in 60- to 500-fold molar excess of a dose of PTHrP-(1-34) known to produce hypercalcemia. The antagonists had no significant effect on serum calcium levels. In an adenylyl cyclase assay using the ROS 17/2.8 cells, a potent PTH antagonist, [Leu11,D-Trp12]PTHrP-(7-34)NH2 was rapidly inactivated in the presence of rat or human plasma. This inactivation by plasma was not blocked by common inhibitors of proteolysis (aprotinin, soybean trypsin inhibitor, and leupeptin). Preliminary studies demonstrated that inactivation of the PTHrP antagonist was caused by a plasma component with an apparent mol wt of 230,000 daltons. The knowledge of the structure of the PTH/PTHrP receptor combined with the identification of a hormone-inactivating plasma factor should facilitate the design of PTH-antagonists that are effective in vivo.