Recombinant Human Heterogeneous Nuclear Ribonucleoprotein L (HNRNPL) Protein (His-SUMO)

Name: Recombinant Human Heterogeneous Nuclear Ribonucleoprotein L (HNRNPL) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08563P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Heterogeneous Nuclear Ribonucleoprotein L (HNRNPL) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P14866
Target Symbol	HNRNPL
Synonyms	D830027H13Rik; FLJ35509; Heterogeneous nuclear ribonucleoprotein L; hnRNP L; hnRNP-L; Hnrnpl; hnRPL; HNRPL_HUMAN; P/OKcl.14
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSRRLLPRAEKRRRRLEQRQQPDEQRRRSGAMVKMAAAGGGGGGGRYYGGGSEGGRAPKRLKTDNAGDQHGGGGGGGGGAGAAGGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPEYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKLNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPSSVKVFSGKSERSSSGLLEWESKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS
Expression Range	1-589aa
Protein Length	Full Length
Mol. Weight	80.1kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter.
Subcellular Location	Nucleus, nucleoplasm. Cytoplasm.
Database References	HGNC: 5045 OMIM: 164021 KEGG: hsa:3191 STRING: 9606.ENSP00000221419 UniGene: Hs.644906

Gene Functions References

High expression of HnRNP L is associated with oral squamous cell carcinoma. PMID: 27808105
uc.345 could upregulate the hnRNPL expression and that inhibition of (hnRNPL) dampens the tumorigenesis capability of uc.345. PMID: 27689400
HnRNP L is a novel regulator of HPV16 RNA processing.HnRNP L controls HPV16 RNA polyadenylation and splicing in an Akt kinase-dependent manner. PMID: 28934469
Translation of VEGFA mRNA in myeloid cells is dictated by a bi-directional interaction between miR-574-3p, a CA-rich microRNA, and hnRNP L. In normoxia, miR-574-3p, acting as a decoy, binds cytoplasmic hnRNP L and prevents its binding to the CARE and stimulation of VEGFA mRNA translation, simultaneously permitting miR-297-mediated translational silencing. PMID: 28520992
High HNRNPL expression is associated with prostate cancer. PMID: 28038443
hnRNP-L contributes to poor prognosis and tumor progression of BC by inhibiting the intrinsic apoptotic signaling and enhancing MAPK signaling pathways PMID: 28088793
hnRNP L inhibits proximal 5'SS but promotes two consecutive distal 5'SS splicing, antagonizing SRSF1 roles in KLF6 pre-mRNA splicing. PMID: 28119102
HNRNPL acts as the adaptor to combine the two substructures and form the intact Sam68 nuclear body through the interaction of two sets of RNA recognition motifs with the putative architectural RNA in the respective substructures. PMID: 27377249
hnRNP L controls inclusion of a broad spectrum of alternative cassette exons in T cells. PMID: 26437669
The study presents the structural characterization of the RNA recognition motif domains of hnRNP-L and demonstrate their function in repressing exon 4 of SLC2A2. PMID: 26051023
Data suggest that incorporation of 3(S)-methyl-beta-alanine into a short alpha-helical region of nucleic acid binding domain of hnRNP LL significantly stabilizes helix without affecting its DNA binding properties. PMID: 25982410
Our results reveal that hnRNP L is a new regulator for CD44 V10 exon splicing. PMID: 25623890
hnRNP K and hnRNP L may serve as A1CF-like cofactors in AID-mediated class switch recombination and somatic hypermutation PMID: 25902538
Results show that HNRNPL represses splicing when bound to intronic regions upstream of alternative exons, and in contrast, activates splicing when bound to the downstream intron. PMID: 24526010
hnRNP L is a potential biomarker for the diagnosis of HBV-HCC and show that hnRNP L contributes to HCC progression. PMID: 24125732
HnRNP L and hnRNP LL antagonistically modulate PTB-mediated splicing suppression of CHRNA1 pre-mRNA. PMID: 24121633
THRIL has a role in regulating TNFalpha expression through its interaction with hnRNPL PMID: 24371310
Data show that alternative exons with weak 5' splice site sequences specifically show a strong correlation between hnRNP L binding and hnRNP L-dependent splicing regulation. PMID: 24164894
functional component of hnRNP LL is consistent with the fact that the full-length hnRNP LL has a greater silencing activity than hnRNP L PMID: 23646903
Induction of caspase-9b expression is due to activation of hnRNP L via phosphorylation to compete/inhibit hnRNP U association with exon 3 of Casp9 mRNA. PMID: 23396972
hnRNP L represses CD45 exon 4 by recruiting hnRNP A1 to a sequence upstream of the 5' splice site PMID: 23394998
HnRNPL is a key factor involved in the spermatogenesis by functional proteomic studies of azoospermia patients with sertoli cell only syndrome. PMID: 22245417
Constitutive deletion of splicing factor hnRNP L impedes early embryonic development of transgenic mice. PMID: 22523384
NSP 5a3a's novel interaction with B23 and ribonuclear protein hnRNP-L implicates NSP 5a3a in cellular processes such as ribosome biogenesis and rRNA transcription . PMID: 20237420
Hypoxia induces translocation of nuclear hnRNP L to the cytoplasm, which markedly increases hnRNP L binding to VEGFA mRNA thereby inhibiting miRNA activity. PMID: 21343907
hnRNP L represses splicing by preventing 5' splice site recognition of the U1 snRNP. PMID: 19946215
The binding of hnRNP L to an exon represses strong splice sites but enhances weak splice sites. PMID: 20122404
identified hnRNP L as a novel Sam68-interacting protein partner. PMID: 19912651
AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter PMID: 11809897
HnRNP L may be involved in the regulation of many other genes containing CA repeats or A/C-rich enhancers. PMID: 12447348
hnRNP L plays roles in enhancing stability, polyadenylation, and nucleocytoplasmic export; it does so by directly recruiting to intronless pre-mRNA processing enhancer (PPE) element-containing RNAs cofactors normally recruited to intron-containing RNAs. PMID: 16024770
11 target genes of hnRNP L were describes. PMID: 18073345
hnRNP L is an essential component of CaMKIV-regulated alternative splicing through CA repeats, with its phosphorylation likely playing a critical role. PMID: 19017650
These results strongly demonstrate the functional requirement of cellular hnRNP L for the HCV internal ribosome entry site activity. PMID: 19061868
hnRNP L cross-regulates inclusion of an analogous poison exon in the hnRNP L-like pre-mRNA, which explains the reciprocal expression of the two closely related hnRNP L proteins. PMID: 19124611
CA repeats in the 3'UTR of bcl-2 mRNA interact with hnRNP L in vitro and in vivo; this physical association is partially involved in the decay of bcl-2 mRNA. PMID: 19298794
Identification of a novel, higher eukaryotic specific subunit, heterogeneous nuclear ribonucleoprotein L (HnRNP-L)required for lysine methylation in vivo. PMID: 19332550
confirm the interactions of eEF1A1, p54(nrb), hnRNP-L, GAPDH and ASF/SF2 with the right terminal stem-loop domain of HDV genomic RNA in vitro PMID: 19464723

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.