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AB125980

Recombinant Human CRM1 protein (His-DHFR)

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(2 Publications)

Recombinant Human CRM1 protein (His-DHFR) is a Human Fragment protein, in the 623 to 868 aa range, expressed in Escherichia coli, with 90%, suitable for SDS-PAGE.

View Alternative Names

CRM1, XPO1, Exportin-1, Exp1, Chromosome region maintenance 1 protein homolog

Key facts

Purity

90% SDS-PAGE

Expression system

Escherichia coli

Tags

His-DHFR tag

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O14980

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"27.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":868,"aminoAcidStart":623,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O14980","tags":[{"tag":"His-DHFR","terminus":""}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

CRM1 also known as exportin 1 is a significant nuclear export protein with a molecular mass of approximately 123 kDa. It is expressed in a wide range of eukaryotic cells being an important component in transporting molecules from the nucleus to the cytoplasm. The CRM1 protein binds cargo proteins bearing a leucine-rich nuclear export signal (NES) and facilitates their passage through the nuclear pore complex. Due to its essential role in nuclear-cytoplasmic transport CRM1 serves as a targeted protein in various research and therapeutic contexts.
Biological function summary

CRM1 participates in the regulation of gene expression by controlling the export of mRNA and ribosomal subunits. It does not act alone but associates with other proteins such as Ran GTPase to form a functioning export complex. This CRM1 complex plays a pivotal role in maintaining cellular homeostasis and responding to cellular stress by regulating the localization of key signaling molecules and transcription factors.

Pathways

CRM1 integrates into critical pathways such as the Wnt signaling pathway and DNA damage response. In the Wnt signaling pathway CRM1 influences the localization and activity of beta-catenin a central protein in the pathway. In the DNA damage response CRM1 interacts with p53 a notable tumor suppressor protein. Through these pathways CRM1 ensures proper control of cell proliferation apoptosis and differentiation.

CRM1 is implicated in cancer and viral infections. Dysregulation of CRM1-mediated nuclear export can lead to abnormal accumulation of oncogenic proteins in the cytoplasm which contributes to cancer pathogenesis. CRM1 overexpression is often observed in several cancers including leukemia and pancreatic cancer linking it to essential regulatory proteins like p53 and NF-kB. Additionally certain viruses exploit CRM1’s export mechanism to enhance their replication making it a target for antiviral research.

Specifications

Form

Lyophilized

Additional notes

Purified via His tag

General info

Function

Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap.. (Microbial infection) Mediates the export of unspliced or incompletely spliced RNAs out of the nucleus from different viruses including HIV-1, HTLV-1 and influenza A. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.

Sequence similarities

Belongs to the exportin family.

Subcellular localisation

Nucleus

Product protocols

Target data

Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap.. (Microbial infection) Mediates the export of unspliced or incompletely spliced RNAs out of the nucleus from different viruses including HIV-1, HTLV-1 and influenza A. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.
See full target information XPO1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nature physics 20:1180-1193 PubMed39036650

2024

Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.

Applications

Unspecified application

Species

Unspecified reactive species

Fani Panagaki,Rafael Tapia-Rojo,Tong Zhu,Natalie Milmoe,Patricia Paracuellos,Stephanie Board,Marc Mora,Jane Walker,Elena Rostkova,Andrew Stannard,Elvira Infante,Sergi Garcia-Manyes

Cell 176:198-212.e15 PubMed30503211

2018

LAP2 Proteins Chaperone GLI1 Movement between the Lamina and Chromatin to Regulate Transcription.

Applications

Unspecified application

Species

Unspecified reactive species

Amar N Mirza,Siegen A McKellar,Nicole M Urman,Alexander S Brown,Tyler Hollmig,Sumaira Z Aasi,Anthony E Oro
View all publications

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