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MSQC6

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SILuMAB K1 Stable-Isotope Labeled Universal Monoclonal Antibody

recombinant, expressed in CHO cells

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Synonym(s):
SILuMAB Stable-Isotope Labeled Universal Monoclonal Antibody Standard human, IgG1 kappa, K1 Stable-Isotope Labeled Universal Monoclonal Antibody
NACRES:
NA.12

recombinant

expressed in CHO cells

Quality Level

antibody product type

primary antibodies

assay

≥90% (SDS-PAGE)

packaging

vial of 100 μg (± 10% Lot-specific vial content given on certificate of analysis)

shipped in

wet ice

storage temp.

−20°C

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This Item
MSQC7MSQC3MSQC11
storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

packaging

vial of 100 μg (± 10% Lot-specific vial content given on certificate of analysis)

packaging

vial of 100 μg (± 10% Lot-specific vial content given on certificate of analysis)

packaging

vial of 100 μg (± 10% Lot-specific vial content given on certificate of analysis)

packaging

vial of 100 μg

recombinant

expressed in CHO cells

recombinant

expressed in CHO cells

recombinant

expressed in CHO cells

recombinant

expressed in CHO cells

antibody product type

primary antibodies

antibody product type

primary antibodies

antibody product type

-

antibody product type

primary antibodies

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

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Application

SILu MAB K1 Stable-Isotope Labeled Universal Monoclonal Antibody has been used to spike peptide samples to assess preparation reproducibility.

Features and Benefits

Universal Peptide Sequence Location
FNWYVDGVEVHNAK Heavy Chain (IgG1)
VVSVLTVLHQDWLNGK Heavy Chain (IgG1, IgG3, IgG4)
GFYPSDIAVEWESNGQPENNYK Heavy Chain (IgG1, IgG4)
SGTASVVCLLNNFYPR Light Chain (kappa)
VDNALQSGNSQESVTEQDSK Light Chain (kappa)
DSTYSLSSTLTLSK Light Chain (kappa)

SILuMab has been validated as an internal standard for quantitation of relevant biotherapeutics in a complex biological matrix by MRM-based LC-MS/MS.
  • SILuMab yielded reproducible, linear curves from 0.1 μg/mL to 1000 μg/mL without enrichment or depletion.
  • Good agreement was observed between multiple peptides derived from the same target.
  • Label incorporation was determined to be >98% by mass spectrometry.
  • Sequence coverage was confirmed by peptide mapping.

Physical form

Supplied as a lyophilized powder containing phosphate buffered saline

Preparation Note

Produced utilizing enriched media containing stable isotope labeled amino acids are 13C<SUB>6</SUB>, 15N<SUB>4</SUB>-labeled Arginine and 13C<SUB>6</SUB>, 15N<SUB>2</SUB>-labeled Lysine.
SILuMab design is optimized to be used as an internal standard for quantitation of monoclonal antibodies as well as Fc-fusion therapeutics. Because of overlap with the common sequences in the Fc region with candidate antibodies, SILuMab provides univer­sal utility, thus eliminating the need for production of candidate-specific internal standards.

Reconstitution

SILuMab recovery is maximized when 0.1% formic acid is used for reconstitution of the lyophilized product. Reconstitution with other solvents may reduce recovery. Do not freeze after reconstitution.
Procedure
  • Briefly centrifuge the vial at ~10,000 x g to collect the product at the bottom of the vial.
  • Add 500 μL of purified water containing 0.1% formic acid to the vial.
  • Mix the contents by gently inverting the vial a minimum of 5 times.
  • Allow the vial to stand at room temperature for a minimum of 15 minutes and repeat mixing by inversion.

Analysis Note

SILuMAb K1 Heavy Chain

EVQLVESGGGLVQPGGSLRLSCVASGFTLNNYDMHWVRQGIGKGLEWVSKIGTAGDRYYAGSVKGRFTISRENAKDSLYLQMNSLRVGDAAVYYCARGAGRWAPLGAFDIWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG

SILuMAb K1 Light Chain

QSALTQPRSVSGSPGQSVTISCTGTSSDIGGYNFVSWYQQHPGKAPKLMIYDATKRPSGVPDRFSGSKSGNTASLTISGLQAEDEADYYCCSYAGDYTPGVVFGGGTKLTVLTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Target overlap areas are underlined
Package size based on protein content determined by A280 using an extinction coefficient (E0.1%) of 1.4
Quantitative
MRM settings provided (xls)

Legal Information

This product is licensed under U.S. Patent No. 7,396,688 and foreign counterparts from E. I. du Pont de Nemours and Company. The purchase of this product conveys to the buyer the nontransferable right to use the purchased amount of the product for research and development only, including services for a third party for consideration. The buyer cannot sell or otherwise transfer this product, its components or materials made using this product or its components to a third party. Information about licenses for excluded uses is available from: E. I. du Pont de Nemours and Company; Attn: Associate Director, Commercial Development; DuPont Experimental Station E268; 200 Powdermill Rd.; Wilmington, DE 19803; 1-877-881-9787 (voice), 1-302-695-1437 (fax), licensing@dupont.com.
SILu is a trademark of Sigma-Aldrich Co. LLC

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Simone Albrecht et al.
Analytical and bioanalytical chemistry, 410(13), 3197-3207 (2018-04-03)
The monitoring of protein biomarkers for the early prediction of cell stress and death is a valuable tool for process characterization and efficient biomanufacturing control. A representative set of six proteins, namely GPDH, PRDX1, LGALS1, CFL1, TAGLN2 and MDH, which
Bryan E Jones et al.
Science translational medicine, 13(593) (2021-04-07)
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) poses a public health threat for which preventive and therapeutic agents are urgently needed. Neutralizing antibodies are a key class of therapeutics that may bridge widespread vaccination campaigns and offer a treatment solution in
Liyun Zhang et al.
Bioanalysis, 10(13), 1039-1054 (2018-06-29)
The requirements for developing antibody biotherapeutics benefit from understanding the nature and relevant aspects of the entire molecule. The method presented herein employs on-line multidimensional LC-quadrupole time-of-flight (QTOF)-MS for the quantitative determination of an antibody isolated from biological samples while
Xi Qiu et al.
Bioanalysis, 10(13), 1055-1067 (2018-07-05)
Sample extraction using immuno-affinity capture coupled with LC-high-resolution mass spectrometer has recently emerged as a novel approach for the determination of concentrations of large molecules at intact level in biological matrix. In the current work, different data processing strategies for

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