Recombinant Mouse Cullin-4A (Cul4a)

Code CSB-YP668835MO
MSDS
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Source Yeast
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Code CSB-EP668835MO
MSDS
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Source E.coli
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Code CSB-EP668835MO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP668835MO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP668835MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Cul4a
Uniprot No.
Alternative Names
Cul4aCullin-4A; CUL-4A
Species
Mus musculus (Mouse)
Expression Region
1-759
Target Protein Sequence
MADEGPRKGS VSALMGRTNG LTKPAALAGG PAKPGGTGGS RKLVIKNFRD RPRLPDNYTQ DTWRKLHEAV KAIQSSTSIR YNLEELYQAV ENLCSHKVSP TLYKQLRQVC EDHVQAQILP FREDSLDSVL FLKKINTCWQ DHCRQMIMIR SIFLFLDRTY VLQNSMLPSI WDMGLELFRN HIISDRMVQS KTIDGILLLI GRERSGEAVD RSLLRSLLSM LSDLQVYKDS FELKFLEETN CLYAAEGQRL MQDREVPEYL NHVSKRLEEE ADRVITYLDH STQKPLIACV EKQLLGEHLT AILQKGLEHL LDENRVPDLT QMYQLFSRVK GGQHALLQHW SEYIKTFGTT IVINPEKDKD MVQDLLDFKD KVDHVVEVCF QRNERFINLM KESFETFINK RPNKPAELIA KHVDSKLRAG NKEATDEELE RILDKIMILF RFIHGKDVFE AFYKKDLAKR LLVGKSASVD AEKSMLSKLK HECGAAFTSK LEGMFKDMEL SKDIMVHFKQ HMQNQSAPGP IDLTVNILTM GYWPTYTPME VHLPPEMVRL QEVFKTFYLG KHSGRKLQWQ TTLGHAVLKA DFKEGKKEFQ VSLFQTLVLL MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED GDKFIFNADF KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI VRIMKMRKTL GHNLLVSELY NQLKFPVKPG DLKKRIESLI DRDYMERDKD SPNQYHYVA
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of p53/TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(DTL) directs autoubiquitination of DTL. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. With CUL4B, contributes to ribosome biogenesis. The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes.
Gene References into Functions
  1. These studies identify CUL4-DDB1 complex as a novel post-translational regulator of stem and progenitor maintenance and differentiation. PMID: 26613412
  2. CUL4A facilitates hepatocarcinogenesis by promoting cell cycle progression and epithelial-mesenchymal transition. PMID: 26593394
  3. Findings indicate that Cul4A is oncogenic in vivo and that Cul4A over-expression is associated with cisplatin resistance in lung cancer cells. PMID: 24648314
  4. this study revealed an indispensable role for Cul4a during male germ cell meiosis. PMID: 21624359
  5. The primary spermatocytes in Cul4A-/- mice are deficient in progression through late prophase I, a time point when expression of the X-linked Cul4B gene is silenced due to meiotic sex chromosome inactivation. PMID: 21291880
  6. CUL-4A is critical for early embryonic development. CUL-4A(-/-) embryos die between 4.5 and 7.5 dpc. PMID: 12077329
  7. Enforced CUL-4A expression does not alter the cell cycle distribution of uninduced cells. It increases the proportion of induced cells in S-phase & reduces the proportion in G0/G1. This CUL-4A regulatory function is interconnected with differentiation. PMID: 12393421
  8. a Cul4A ubiquitin ligase positively regulates proliferation by targeting p27 for degradation and that Cul4A down-regulation during terminal erythroid differentiation allows p27 to accumulate and signal cell cycle exit PMID: 16467204
  9. Cul4A(+/-) hematopoietic stem-cells exhibit defects in engraftment and self-renewal capacity PMID: 17616641
  10. Cul4A deficiency resulted in DNA damage and apoptosis of rapidly dividing cells, and mutant mice died within 3 to 10 days after induction with dramatic atrophy of the intestinal villi, bone marrow, and spleen, and with hematopoietic failure PMID: 18339895
  11. Data show that CUL4A was a novel Wnt target gene in both mouse and human cells and that CUL4A physically interacted with p27(KIP1) in Wnt-responding cells. PMID: 19056892
  12. Cul4A is required for efficient cell proliferation, control of centrosome amplification and genome stability. PMID: 19430492
  13. Data show that CUL4A restricts cellular repair capacity by regulating nucleotide excision repair and the G1/S checkpoint through selective degradation of the DDB2 and XPC DNA damage sensors and the p21/CIP1/WAF1 checkpoint effector. PMID: 19481525

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Protein Families
Cullin family
Database Links
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