Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

HJURP

Uniprot No.

Q8NCD3

Research Area

Cell Cycle

Alternative Names

HJURP; FAKTS; FLEG1; URLC9; Holliday junction recognition protein; 14-3-3-associated AKT substrate; Fetal liver-expressing gene 1 protein; Up-regulated in lung cancer 9

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

1-748aa

Target Protein Sequence

MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQDSSMKPADRTDGSVQAAAWGPELPSHRTVLGADSKSGEVDATSDQEESVAWALAPAVPQSPLKNELRRKYLTQVDILLQGAEYFECAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSSKENFIPCSEPVKGTGALRDCKNVLDVSCRKTGLKLEKAFLEVNRPQIHKLDPSWKERKVTPSKYSSLIYFDSSATYNLDEENRFRTLKWLISPVKIVSRPTIRQGHGENRQREIEIRFDQLHREYCLSPRNQPRRMCLPDSWAMNMYRGGPASPGGLQGLETRRLSLPSSKAKAKSLSEAFENLGKRSLEAGRCLPKSDSSSSLPKTNPTHSATRPQQTSDLHVQGNSSGIFRKSVSPSKTLSVPDKEVPGHGRNRYDEIKEEFDKLHQKYCLKSPGQMTVPLCIGVSTDKASMEVRYQTEGFLGKLNPDPHFQGFQKLPSSPLGCRKSLLGSTAIEAPSSTCVARAITRDGTRDHQFPAKRPRLSEPQGSGRQGNSLGASDGVDNTVRPGDQGSSSQPNSEERGENTSYRMEEKSDFMLEKLETKSV
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

99.5kDa

Protein Length

Full Length

Tag Info

N-terminal 6xHis-SUMO-tagged

Form

Liquid or 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

Tris-based buffer,50% glycerol

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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein 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

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Function

Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions.

Gene References into Functions

Increased expression of HJURP was identified as an independent negative prognostic biomarker for patients with advanced serous ovarian cancer. PMID: 29743473
during the CENP-A/H4 deposition process, the chaperone HJURP protects various substructures of the dimer, serving both as a folding and binding chaperone PMID: 27454815
Functional p53 elicits a cell cycle arrest response, whereas, in p53-null transformed cells, the absence of arrest enables the loss of HJURP to induce severe aneuploidy and, ultimately, apoptotic cell death PMID: 28356341
An increased occurrence of hepatocellular carcinoma was consistently associated with A/C or C/C genotypes of the non-synonymous SNP rs3771333 compared with the A/A genotype in both the Fusui and Haimen populations. PMID: 26863619
Authors propose that this centromere expansion activity reflects the functional properties of HJURP, which uses this activity to contribute to the plastic establishment of a centromeric chromatin structure. PMID: 26063729
3 biomarkers in 44 patients with in situ breast cancers were evaluated: TG2 (transglutaminase 2), HJURP (Holliday junction recognition protein), and HIF-1alpha (hypoxia inducible factor-1 alpha). PMID: 25243117
On the basis of our findings, we propose that HJURP serves a dual chaperone function in coordinating CenH3(CENP-A) and CENP-C recruitment. PMID: 25843710
HJURP can discriminate favorable and unfavorable outcome within the luminal A subtype, outperforming the currently utilized proliferation marker Ki67, as an independent prognostic marker for luminal A patients. PMID: 25497280
Phosphorylation state of HJURP controls its centromeric recruitment. HJURP binding to DNA promotes loading of CenH3CENP-A at centromeres. PMID: 25001279
The study describes a novel function for human centromeric long non-coding RNAs in the recruitment of HJURP and CENP-A, implicating RNA-based chaperone targeting in histone variant assembly. PMID: 25117489
The levels of the EDNRB, HJURP and p60/CAF-1 proteins were strongly associated with overall survival in high-grade gliomas patients (p<0.001, p<0.001 and p=0.002, respectively), whereas the one of PDLI4 was not (P=0.11). PMID: 24039914
Mis18beta binds with and specifies the centromere localization of HJURP. PMID: 24519934
HJURP has an important role in the maintenance of extremely proliferative cells of high-grade gliomas PMID: 23638004
a mechanism whereby the CENP-A pre-nucleosomal complex achieves assembly of the octameric CENP-A nucleosome through the dimerization of the CENP-A chaperone HJURP. PMID: 23771058
Downregulation of HJURP in young cells led to premature senescence. p53 knockdown, but not p16 knockdown, abolished senescence phenotypes caused by HJURP reduction. PMID: 23292286
And-1 together with HJURP regulates the assembly of new CENP-A onto centromeres. PMID: 23184928
stringent regulation of HJURP and SCM3 expression are critical for genome stability. PMID: 21980305
An amino-terminal fragment of HJURP was able to assemble CENP-A nucleosomes in vitro, demonstrating that HJURP is a chromatin assembly factor. PMID: 21768289
The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer PMID: 21478274
Data show that HJURP mRNA level is a prognostic factor for disease-free and overall survival in patients with breast cancer and is a predictive biomarker for sensitivity to radiotherapy. PMID: 20211017
found that HJURP, a member of the complex, was required for cell cycle specific targeting of CENP-A to centromeres. PMID: 20080577
HJURP is a possible cell-cycle-regulated CENP-A-specific histone chaperone required for centromeric chromatin assembly PMID: 19410544
HJURP is a key factor for CENP-A deposition and maintenance at centromeres PMID: 19410545
hFLEG1 is associated with the CENP-A centromeric nucleosome PMID: 16622419

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Subcellular Location

Nucleus, nucleolus. Chromosome, centromere. Note=Localizes in centromeres during late telophase and early G1, when CENPA nucleosomes are assembled. Localizes to nucleolus during S phase, nucleolus site being often related to storage.

Tissue Specificity

According to PubMed:17256767, highly expressed in the thymus with lower levels in the placenta, small intestine, liver, skeletal muscle, and colon. According to PubMed:17823411, highly expressed in testis, and at a relatively lower level in thymus and bon

Database Links

HGNC: 25444

OMIM: 612667

KEGG: hsa:55355

STRING: 9606.ENSP00000414109

UniGene: Hs.532968

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Code	CSB-EP010467HU
MSDS	MSDS
Size	$224
	Order now
Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP010467HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HJURP. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP010467HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HJURP.
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Recombinant Human Holliday junction recognition protein (HJURP)

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