Recombinant Human Exportin-2 (CSE1L), partial

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Product Specs

Buffer
For liquid delivery forms, the default storage buffer is a Tris/PBS-based buffer containing 5%-50% glycerol.
Note: If you have specific requirements for the glycerol content, please provide them in your order remarks.
For lyophilized powder delivery forms, the buffer prior to lyophilization is a Tris/PBS-based buffer with 6% Trehalose.
Form
The delivery format can be either liquid or lyophilized powder.
Note: We will prioritize shipping the format currently in stock. However, if you have specific format requirements, please provide them in your order remarks. We will accommodate your request if possible.
Lead Time
Delivery times may vary depending on the purchase method and location. For specific delivery times, please contact your local distributor.
Notes
Repeated freezing and thawing of the product is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend briefly centrifuging the vial before opening to ensure the contents settle at the bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%, which you can use as a reference.
Shelf Life
The shelf life of the product depends on several factors, including storage conditions, buffer ingredients, storage temperature, and the stability of the protein itself. Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store the product at -20°C/-80°C. Aliquoting is necessary for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
N-terminal 6xHis-SUMO-tagged
Synonyms
CSE1L; CAS; XPO2; Exportin-2; Exp2; Cellular apoptosis susceptibility protein; Chromosome segregation 1-like protein; Importin-alpha re-exporter
Datasheet & Coa
Please contact us to get it.
Expression Region
1-200aa
Mol. Weight
39.1kDa
Protein Length
Partial
Purity
Greater than 90% as determined by SDS-PAGE.
Research Area
Cell Biology
Source
in vitro E.coli expression system
Species
Homo sapiens (Human)
Target Names
CSE1L
Target Protein Sequence
MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHAN
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Uniprot No.

Target Background

Function
Exportin-2 (CSE1L) is an export receptor for importin-alpha. It mediates the re-export of importin-alpha from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus, it binds cooperatively to importin-alpha and the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembly of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause the release of importin-alpha from the export receptor. CSE1L/XPO2 then returns to the nuclear compartment and mediates another round of transport. 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.
Gene References Into Functions
  1. CSE1L expression was correlated with MSH6 expression in tumor samples and was associated with poor prognosis in patients with osteosarcoma. These findings demonstrate that the CSE1L-MSH6 axis plays a significant role in osteosarcoma progression. PMID: 28387323
  2. CSE1L appears to be essential for the nuclear import of certain key repressive proteins. Specifically, NOVA1, HDAC1, HDAC2, and HDAC8, genes known as silencing factors, became delocalized into the cytosol upon CSE1L depletion. PMID: 29636421
  3. The combination of CTNB1, XPO2, and CAPG achieved 95% sensitivity and 96% specificity for the discrimination of endometrial cancer subtypes. Two uterine aspirate-based signatures were developed to diagnose Endometrial cancer and classify tumors into the most prevalent histologic subtypes. This advancement will improve diagnosis and assist in predicting the optimal surgical treatment. PMID: 28790116
  4. Our data suggest a previously unanticipated link between CAS and integrin beta1 signaling, which correlates with an aggressive hepatocellular carcinoma phenotype. PMID: 27015362
  5. CSE1L knockdown by shRNA inhibited protein expression, resulting in decreased cell proliferation, reduced colony formation in soft agar, and induction of apoptosis. CSE1L protein is expressed early and across all stages of colorectal carcinoma (CRC) development. shRNA knockdown of CSE1L was associated with inhibition of tumorigenesis in CRC cells. CSE1L may represent a potential target for the treatment of CRC. PMID: 27521996
  6. Data suggest that CAS overexpression in thyroid carcinoma depends on the subtype and the disease stage. Our findings also indicate that CAS maintains papillary thyroid cell proliferation and survival. PMID: 26892809
  7. There is a relationship between nuclear CSE1L overexpression and distant metastasis in breast cancer. PMID: 26278417
  8. CAS plays contrasting roles in proliferation and apoptosis. PMID: 26668314
  9. hCAS/CSE1L is responsible for controlling homologous recombinational repair activity by directly interacting with RAD51. PMID: 26123175
  10. Nuclear CSE1L is mainly non-phosphorylated CSE1L and is involved in gene regulation, while cytoplasmic CSE1L is mainly phosphorylated CSE1L and is involved in cytoplasmic signaling regulation in melanocytic tumorigenesis. PMID: 25973023
  11. These results indicate that CSE1L is associated with viability and apoptosis, cellular adhesion and invasion, thus implicating CSE1L in the progression of colorectal cancer. PMID: 22450763
  12. The cellular apoptosis susceptibility/importin-alpha1 transport cycle is linked to X-linked inhibitor (XIAP) and is required to maintain tumor cell survival in hepatocellular carcinoma. PMID: 24799195
  13. CSE1L expression was significantly inhibited in RKO cells, causing cell cycle arrest in the G2/M and S phases, a delay in cell proliferation, induction of apoptosis, and inhibition of colony growth capacity. PMID: 23621178
  14. Most colorectal tumors were positive for CSE1L staining (98.4%). Colorectal tumors with K-Ras mutation or high cytoplasmic CSE1L expression were correlated with T status (depth of tumor penetration; P = .004), stage (P = .004), and lymph node metastasis (P = .019). PMID: 23806821
  15. Our results suggest that urinary CSE1L deserves further evaluation for the screening of bladder cancer. PMID: 22653741
  16. CSE1L- and inhibitor of DNA binding-3 (ID3)-overexpression was associated with the diagnosis of Burkitt lymphoma (BL), and signal transduction and transcription-3 (STAT3) with diffuse large B-cell lymphoma (DLBCL) (P<0.001 for all markers). All three markers were associated with patient outcome in DLBCL. PMID: 22967991
  17. CSE1L may be involved in the "early" and "late" metastasis of tumor cells in tumorigenesis. PMID: 22952058
  18. Nuclear CSE1L may play an oncogenic role in bladder tumor progression, and immunohistochemical staining of nuclear CSE1L may be useful for the prognosis of bladder urothelial carcinomas. PMID: 22476051
  19. CAS protein expression is closely related to tumor differentiation in hepatocellular carcinoma tissues. PMID: 23189846
  20. Data show that CSE1L, DIDO1, and RBM39 mRNA expression levels correlated with chromosome 20q DNA copy number status. PMID: 22711543
  21. The requirement for and the regulation of CAS in the functioning of the Vpr-Impalpha complex. PMID: 22110766
  22. Increased immunoexpression of CAS protein in serous ovarian tumors may be useful in identifying patients with more aggressive disease. PMID: 21290345
  23. These results indicate that examination of CSE1L and E-cadherin distribution in colorectal epithelium glands may be valuable for evaluating the malignance of colorectal disease. PMID: 20734115
  24. Serum cellular apoptosis susceptibility protein may have a role in the progression of metastatic colorectal cancer. PMID: 20150437
  25. CAS/CSE 1 stimulates E-cadhrin-dependent cell polarity in HT-29 human colon epithelial cells. PMID: 12061792
  26. CSE1L/CAS has a role in proliferation and apoptosis [review]. PMID: 12510150
  27. A single phosphorylation site on CAS can effectively separate cell migration from other transformed growth characteristics. PMID: 12972425
  28. Results suggested that CAS may be associated with cell proliferation rather than apoptosis, and further, CAS might play a significant role in the development of human hepatocellular carcinoma. PMID: 16786158
  29. hCAS/CSE1L associates with chromatin and regulates expression of select p53 target genes. PMID: 17719542
  30. These results indicate that CAS may play a significant role in regulating the cytotoxicities of chemotherapeutic drugs. PMID: 18377724
  31. Results show that heat upregulates the initial docking of importin-alpha at the nuclear envelope and stimulates the translocation of cellular apoptosis susceptibility protein into the nuclear interior. PMID: 18425415
  32. PHAPI, CAS, and Hsp70 function together to accelerate nucleotide exchange on Apaf-1 and prevent inactive Apaf-1/cytochrome c aggregation. PMID: 18439902
  33. Herein, we report that cellular apoptosis susceptibility (CAS) (or CSE1L) protein regulates the secretion of HT-29 human colorectal cells. PMID: 19224336

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Database Links

HGNC: 2431

OMIM: 601342

KEGG: hsa:1434

STRING: 9606.ENSP00000262982

UniGene: Hs.90073

Protein Families
XPO2/CSE1 family
Subcellular Location
Cytoplasm. Nucleus.
Tissue Specificity
Detected in brain, placenta, ovary, testis and trachea (at protein level). Widely expressed. Highly expressed in testis and in proliferating cells.

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