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T1567

Sigma-Aldrich

Tertiapin-Q trifluoroacetate salt

≥97% (HPLC)

Synonym(s):

[Gln13]-Tertiapin, Ala-Leu-Cys-Asn-Cys-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys-Trp-Lys-Lys-Cys-Gly-Lys-Lys-NH2 [Disulfide bridges 3–14, 5–18], TPNQ

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About This Item

Empirical Formula (Hill Notation):
C106H175N35O24S4
CAS Number:
910044-56-3
Molecular Weight:
2452.00
MDL number:
MFCD02684419
UNSPSC Code:
12352200
NACRES:
NA.32
Pricing and availability is not currently available.

Quality Level

200

Assay

≥97% (HPLC)

form

lyophilized

storage temp.

−20°C

Gene Information

human ... KCNJ1(3758)
mouse ... KCNJ1(56379)
rat ... KCNJ1(24521)

Amino Acid Sequence

Ala-Leu-Cys-Asn-Cys-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys-Trp-Lys-Lys-Cys-Gly-Lys-Lys-NH2 [Disulfide bridges 3–14, 5–18]

Biochem/physiol Actions

Blocks the GIRK1/4 and ROMK1 members of the inward-rectifier K+ channel family.

Other Notes

Non-air oxidizable tertiapin derivative.
Lyophilized from 0.1% TFA in H2O

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
0000178706
0000178706
042M4807V
018K4753
017K4859

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W Jin et al.
Biochemistry, 38(43), 14286-14293 (1999-11-26)
Tertiapin (TPN), a small protein derived from honey bee venom, inhibits the GIRK1/4 and ROMK1 channels with nanomolar affinities. Methionine residue 13 in TPN interacts with residue F148 in the channel, located just outside of the narrow region of the
W Jin et al.
Biochemistry, 38(43), 14294-14301 (1999-11-26)
Tertiapin-Q (TPN(Q)) is a derivative of honey bee toxin tertiapin (TPN) whose methionine residue is replaced with a glutamine residue. TPN(Q) inhibits the ROMK1 and GIRK1/4 inward-rectifier K(+) channels with affinities very similar to TPN. However, unlike native TPN, TPN(Q)
W Jin et al.
Biochemistry, 37(38), 13291-13299 (1998-09-28)
Inward-rectifier K+ channels are a group of highly specialized K+ channels that accomplish a variety of important biological tasks. Inward-rectifier K+ channels differ from voltage-activated K+ channels not only functionally but also structurally. Each of the four subunits of the

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