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Human CAPRIN1 Recombinant Protein (N-His-SUMO & C-Strep) (HC541012)

Human CAPRIN1 Recombinant Protein (N-His-SUMO & C-Strep)
Human CAPRIN1 Recombinant Protein (N-His-SUMO & C-Strep)
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Overview
Catalog No.HC541012
Description
Recombinant Human CAPRIN1 Protein, N-His-SUMO & C-Strep (HC541012) expressed in E. coli, spanning Arg132-Asn251. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionQ14444
Protein lengthArg132-Asn251
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 27.85 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet.

RECONSTITUTION PROTOCOL
1. Allow the product to be reconstituted and the reconstitution diluent to reach room temperature.
2. Tap or briefly centrifuge the product vial before opening to dislodge any lyophilized material that may be dispersed on the wall or cap of the vial.
3. Use the diluent and stock concentration recommended in the product datasheet. If preparing a stock concentration higher than recommended, contact Technical Service.
4. After adding the diluent, re-cap the vial and invert gently by hand or place on a slow rocking platform to allow the reconstitution diluent to coat all the surfaces inside the vial. Note: Do not mix by vortexing or by pipetting the material up and down.
5. Allow the vial to sit at room temperature with gentle agitation for at least 15 minutes before aliquotting or using.
6. Store the reconstituted material in single use aliquots in polypropylene or siliconized tubes. Aliquots of 10 μL or larger are recommended.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesGPI-anchored protein p137, Cytoplasmic activation- and proliferation-associated protein 1, p137GPI, RNG105, M11S1, Caprin-1, Cell cycle-associated protein 1, RNA granule protein 105, CAPRIN1, GPIP137, GPI-anchored membrane protein 1, GPI-p137, GPIAP1, Membrane component chromosome 11 surface marker 1
Background

Caprin-1 (CAPRIN1) is a ~78 kDa protein. mRNA-binding protein that acts as a regulator of mRNAs transport, translation and/or stability, and which is involved in neurogenesis, synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. Plays an essential role in cytoplasmic stress granule formation. Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors. Undergoes liquid-liquid phase separation following phosphorylation and interaction with FMR1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs. In these cytoplasmic ribonucleoprotein granules, CAPRIN1 mediates recruitment of CNOT7 deadenylase, leading to mRNA deadenylation and degradation.

1. Solomon, S. et al. (2007) Molecular and cellular biology 27, 2324-42. PMID: 17210633
2. Kim, TH. et al. (2019) Science (New York, N.Y.) 365, 825-829. PMID: 31439799
3. Pavinato, L. et al. (2023) Brain : a journal of neurology 146, 534-548. PMID: 35979925
4. Jia, X. et al. (2022) Science advances 8, eabo7112. PMID: 35977029
5. Sanders, DW. et al. (2020) Cell 181, 306-324.e28. PMID: 32302570
6. Yang, P. et al. (2020) Cell 181, 325-345.e28. PMID: 32302571
7. Guillén-Boixet, J. et al. (2020) Cell 181, 346-361.e17. PMID: 32302572
8. Kim, TH. et al. (2021) Proceedings of the National Academy of Sciences of the United States of America 118. PMID: 34074792
9. Toyama, Y. et al. (2022) Proceedings of the National Academy of Sciences of the United States of America 119, e2210492119. PMID: 36040869
Note For research use only.
Images
  • Human CAPRIN1 Recombinant Protein (N-His-SUMO & C-Strep)

    SDS-PAGE

    SDS-PAGE for Recombinant Human CAPRIN1 Protein, N-His-SUMO & C-Strep

Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
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Formula
C₁ × V₁ = C₂ × V₂
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Stock Solution
C₁ (Stock Conc.)
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V₁ (Stock Vol.)
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Working Solution
C₂ (Working Conc.)
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