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I6383

Sigma-Aldrich

Insulin Chain B Oxidized from bovine pancreas

≥80% (HPLC), powder

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About This Item

Empirical Formula (Hill Notation):
C157H232N40O47S2
CAS Number:
30003-72-6
Molecular Weight:
3495.89
MDL number:
MFCD00131380
UNSPSC Code:
12352202
NACRES:
NA.77

sterility

non-sterile

Quality Level

200

Assay

≥80% (HPLC)

form

powder

mol wt

3496 Da by calculation (Average Mass)

UniProt accession no.

P01317

shipped in

ambient

storage temp.

−20°C

InChI

1S/C157H232N40O47S2/c1-79(2)57-104(181-130(211)86(15)172-136(217)103(50-53-125(209)210)180-152(233)127(84(11)12)194-148(229)107(60-82(7)8)184-145(226)113(67-95-70-165-78-171-95)189-150(231)115(74-198)176-123(206)73-169-133(214)116(75-245(239,240)241)191-140(221)105(58-80(3)4)182-144(225)112(66-94-69-164-77-170-94)188-138(219)102(48-51-119(160)202)178-146(227)114(68-120(161)203)190-153(234)126(83(9)10)193-131(212)98(159)61-89-31-21-18-22-32-89)139(220)185-110(64-92-40-44-96(200)45-41-92)142(223)183-106(59-81(5)6)147(228)195-128(85(13)14)154(235)192-117(76-246(242,243)244)134(215)168-71-121(204)174-101(49-52-124(207)208)137(218)177-99(38-29-55-166-157(162)163)132(213)167-72-122(205)175-108(62-90-33-23-19-24-34-90)141(222)186-109(63-91-35-25-20-26-36-91)143(224)187-111(65-93-42-46-97(201)47-43-93)149(230)196-129(88(17)199)155(236)197-56-30-39-118(197)151(232)179-100(37-27-28-54-158)135(216)173-87(16)156(237)238/h18-26,31-36,40-47,69-70,77-88,98-118,126-129,198-201H,27-30,37-39,48-68,71-76,158-159H2,1-17H3,(H2,160,202)(H2,161,203)(H,164,170)(H,165,171)(H,167,213)(H,168,215)(H,169,214)(H,172,217)(H,173,216)(H,174,204)(H,175,205)(H,176,206)(H,177,218)(H,178,227)(H,179,232)(H,180,233)(H,181,211)(H,182,225)(H,183,223)(H,184,226)(H,185,220)(H,186,222)(H,187,224)(H,188,219)(H,189,231)(H,190,234)(H,191,221)(H,192,235)(H,193,212)(H,194,229)(H,195,228)(H,196,230)(H,207,208)(H,209,210)(H,237,238)(H4,162,163,166)(H,239,240,241)(H,242,243,244)/t86-,87-,88+,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,115-,116-,117-,118-,126-,127-,128-,129-/m0/s1

InChI key

CZJQESISDHGFTC-DQCCOYHDSA-N

Gene Information

cow ... INS(280829)

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Amino Acid Sequence

Phe-Val-Asn-Gln-His-Leu-Cys(SO3H)-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys(SO3H)-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala

General description

Insulin is made up of two polypeptide chains (A and B) linked together by two disulfide linkages. Chain A and B are composed of 21 amino acids and 30 amino acids, respectively.

Application

Insulin Chain B Oxidized from bovine pancreas has been used:
  • as a matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry (MS) calibration standard
  • in electrochemical impedance spectroscopy and quartz crystal nanobalance (EQCN) studies of insulin adsorption on platinum
  • as an internal standard to quantify insulin chain B residue in protein samples

Biochem/physiol Actions

Insulin regulates the cellular uptake, utilization, and storage of glucose, amino acids, and fatty acids. It inhibits the breakdown of glycogen, protein, and fat. The β chain is a substrate for carboxypeptidase Y.

Preparation Note

Prepared by modification of Sanger, F., et al.

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

Certificates of Analysis (COA)

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L He et al.
Journal of mass spectrometry : JMS, 34(9), 909-914 (1999-09-24)
Matrix-assisted laser desorption/ionization (MALDI) mass spectra were obtained from single particles injected directly into a time-of-flight mass spectrometer. Aerosol particles were generated at atmospheric pressure using a piezoelectric single-particle generator or a pneumatic nebulizer and introduced into the mass spectrometer
Fractionation of oxidized insulin.
F Sanger
The Biochemical journal, 44(1), 126-128 (1949-01-01)
Johansen, J.T., et al.
Carlsberg Research Communications, 41, 1-1 (1976)
Epitope mapping by a combination of epitope excision and MALDI-MS.
C E Parker et al.
Methods in molecular biology (Clifton, N.J.), 146, 185-201 (2000-08-19)
T Keough et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(13), 7131-7136 (1999-06-23)
A method has been developed for de novo peptide sequencing using matrix-assisted laser desorption ionization mass spectrometry. This method will facilitate biological studies that require rapid determination of peptide or protein sequences, e.g., determination of posttranslational modifications, identification of active
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