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Hela digest

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The HeLa digest is a laboratory product derived from the HeLa cell line, a widely used human cell line in biomedical research. The product provides a standardized and consistent source of cellular material for use in various applications, such as cell culture studies and biochemical analyses. The core function of the HeLa digest is to serve as a reliable and reproducible reference material for research purposes.

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Lab products found in correlation

Affi gel 10, by Bio-Rad (1 mentions) Amicon filter, by Merck Group (1 mentions) Irt peptide, by Biognosys (1 mentions) Micro bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Trypsin, by Promega (1 mentions) Anoacquity uplc system, by Waters Corporation (1 mentions) Synapt g2 si hdms mass spectrometer, by Waters Corporation (1 mentions) Nanoacquity uplc system, by Waters Corporation (1 mentions)

Close spelling variants of this product

Pierce HeLa Protein Digest Standard (18 citations) Pierce HeLa tryptic Digest Standard (2 citations) HeLa protein digest standard (6 citations) HeLa digest standard (3 citations) HeLa tryptic digest standard (2 citations)

4 protocols using hela digest

1

Standard Peptide Acquisition and Preparation

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Example 6

Standard peptides TAGTSFMMTPYVVTR (SEQ ID NO: 1) and GAILTTMLATR (SEQ ID NO: 2) were purchased from JPT (Berlin, Germany). iRT peptides were from Biognosys (Zurich, Switzerland). MrsA, apomyoglobin and HeLa digest were purchased from Thermo Fisher (San Jose, Calif.). Affi-Gel® 10 was purchased from Biorad® (Hercules, Calif.). Amicon® filters were purchased from EMD Millipore® (Billerica, Mass.).

US10266866B2. Reduction of oxidated methionine peptides for mass spectrometry (2019-04-23). CALIFORNIA INSTITUTE OF TECHNOLOGY [US]. Inventors: Michael Sweredoski [US], Annie Moradian [US], Tanya R. Yakushi [US], Sonja Hess [US], Roxana Eggleston-Rangel [US].
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2

Escherichia coli Proteome Preparation

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The Escherichia coli DH5α cell pellet was lysed by sonication using a Covaris M220 in a buffer containing 8 M urea and 100 mM TEAB. The protein amount was measured using a micro BCA protein assay kit (23235; ThermoFisher). The sample was reduced using a final concentration of 0.25 M DTT and alkylated with a final concentration of 8 mM IAA. The trypsin (V5280; Promega) was then added to 1:50 enzyme-to-protein ratio in 100 mM TEAB. The sample was acidified with a final concentration of 1% TFA before being loaded into the SPE micro-column. The peptides were eluted after two times of washing and were dried in a SpeedVac. Finally, E. coli proteins were reconstituted with 0.1% TFA and 1% ACN buffer. The HeLa digest (88329, ThermoFisher) was reconstituted with 0.1% TFA and 1% ACN. The E. coli digest and HeLa digest were mixed at the total mass ratio of 94:6 or 97:3.
, & Zhang Y. (2023). pepDESC: A Method for the Detection of Differentially Expressed Proteins for Mass Spectrometry-Based Single-Cell Proteomics Using Peptide-level Information. Molecular & Cellular Proteomics : MCP, 22(7), 100583.
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3

Tryptic Peptide Analysis by UPLC-MS

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For tryptic peptide analysis, a
nanoAcquity UPLC system equipped with a C18, 5 μm, 180 μm
× 20 mm trap column and a HSS-T3 C18 1.8 μm, 75 μm
× 250 mm analytical column (Waters Corporation, Manchester, UK)
was coupled to a Synapt G2 Si HDMS mass spectrometer with an electrospray
ionization source (Waters Corporation, Manchester, UK). Mobile phase
A contained 0.1% formic acid and 3% dimethyl sulfoxide in water and
mobile phase B 0.1% formic acid and 3% dimethyl sulfoxide in acetonitrile.
300 ng of protein was injected in trapping mode. The peptides were
separated at 40 °C with a gradient run from 3 to 40% (v/v) mobile
phase B at a flow rate of 0.3 μL/min over 120 min. Via the reference
channel, a lock mass solution composed of [Glu1]-fibrinopeptide B
(0.1 μM) and leu-enkephalin (1 μM) was introduced every
60 s. Peptide analysis was performed in positive ionization mode using
the ultra-definition MSE (UDMSE) approach.19 (link),20 (link) The reproducibility and stability of the method were controlled
with a commercially available HeLa digest (Thermo Scientific, Waltham,
MA).
Sandbaumhüter F.A., Nezhyva M., Eriksson O., Engberg A., Kreuger J., Andrén P.E, & Jansson E.T. (2022). Well-Plate μFASP for Proteomic Analysis of Single Pancreatic Islets. Journal of Proteome Research, 21(4), 1167-1174.
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4

Nanoflow UPLC-MS/MS Proteomic Analysis

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Tryptic
peptides were analyzed with a nanoAcquity UPLC system coupled to a
Synapt G2-Si HDMS mass spectrometer with a nanoelectrospray ionization
source (Waters Corporation, Manchester, UK). The nanoAcquity UPLC
system consisted of a C18, 5 μm, 180 μm × 20 mm trap
column and an HSS-T3 C18 1.8 μm, 75 μm × 250 mm analytical
column (Waters Corporation, Manchester, UK) set to trapping mode.
Samples containing 300 ng of protein were injected in each run. Mobile
phases A and B consisted of 0.1% formic acid and 3% dimethyl sulfoxide
in water (v/v) and 0.1% formic acid and 3% dimethyl sulfoxide in acetonitrile
(v/v), respectively. Peptide separation was done using a gradient
from 3% to 40% (v/v) of mobile phase B at a constant flow rate of
0.3 μL/min over 120 min. Lock-mass correction was performed
by spraying a lock-mass solution containing [Glu1]-fibrinopeptide
B (0.1 μM) and leu-enkephalin (1 μM) through the reference
channel every 60 s. Data were acquired using a data-independent acquisition
workflow in positive ion mode with a UDMSE method.19 (link)−21 (link) The system’s performance and stability were monitored by
injecting a commercially available HeLa digest (Thermo Scientific,
Waltham, MA) after every seventh sample injection.
Sandbaumhüter F.A., Nezhyva M., Andrén P.E, & Jansson E.T. (2023). Label-Free Quantitative Thermal Proteome Profiling Reveals Target Transcription Factors with Activities Modulated by MC3R Signaling. Analytical Chemistry, 95(41), 15400-15408.
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