Recombinant Human B-Cell Cll/Lymphoma 9 Protein (BCL9) Protein (His&His)

Name: Recombinant Human B-Cell Cll/Lymphoma 9 Protein (BCL9) Protein (His&His)
Brand: Beta LifeScience
SKU: BLC-07812P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human B-Cell Cll/Lymphoma 9 Protein (BCL9) Protein (His&His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00512
Target Symbol	BCL9
Synonyms	Protein legless homolog
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His&C-6His
Target Protein Sequence	AKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNNKTERSTAPLNTQISALRNDPKPLPQQPPAPANQDQNSSQNTRLQPTPPIPAPAPKPAAPPRPLDRESPGVENKLIPSVGSPASSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSSGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNPGVLD
Expression Range	174-396aa
Protein Length	partial
Mol. Weight	26.7 kDa
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	Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity.
Subcellular Location	Nucleus.
Protein Families	BCL9 family
Database References	HGNC: 1008 OMIM: 602597 KEGG: hsa:607 STRING: 9606.ENSP00000234739 UniGene: PMID: 28074862 Results find that BCL9 is upregulated in osteosarcoma (OS) tissues and promotes OS proliferation, migration and invasion. BCL9 is a downstream target of miR-1301 in OS cells. In addition, BCL9 restoration could reversed the functional effects of miR-1301 overexpression on OS cell proliferation, migration and invasion. These results revealed the important role of BCL9 in OS tumor progression. PMID: 30172867 High BCL9 expression is associated with cisplatin-resistance in non-small cell lung cancer. PMID: 30009824 miR-1301 inhibits hepatocellular carcinoma cell migration, invasion, and angiogenesis by decreasing Wnt/beta-catenin signaling through targeting BCL9. PMID: 28817119 results from this study demonstrated that hypoxia induced BCL-9 expression in human CRC cells mainly through HIF-1alpha, which could be an important underlying mechanism for increased BCL-9 expression in CRC. PMID: 27121066 SOX7 inhibits oncogenic beta-catenin-mediated transcription by disrupting the beta-catenin/BCL9 interaction. PMID: 29271667 The authors used CRISPR/Cas9 genome engineering of Drosophila legless (lgs) and human BCL9 and B9L to show that the C-terminus downstream of their adaptor elements is crucial for Wnt responses. PMID: 28296634 MEF2D-BCL9-positive patients had B-cell precursor immunophenotype and were characterized as being older in age, being resistant to chemotherapy, having very early relapse, and having leukemic blasts that mimic morphologically mature B-cell leukemia with markedly high expression of HDAC9. PMID: 27507882 it was demonstrated that miR218 modulated a novel molecular target and the present study provided novel insights into potential mechanisms of RCC oncogenesis. PMID: 27314976 findings indicate that BCL9 most likely does not harbor a common genetic variant that can increase the risk for schizophrenia in the Japanese population PMID: 26494551 BCL9/9L-beta-catenin Signaling is Associated With Poor Outcome in Colorectal Cancer PMID: 26844272 BCL9 is a molecular driver of DCIS invasive progression. PMID: 26384318 PCDH10 antagonized MM cell proliferation via the downregulation of Wnt/beta-catenin/BCL-9 signaling, whereas PCDH10 repressed the expression of AKT to promote the expression of GSK3beta and then to restrain the activation of beta-catenin PMID: 26081897 By beta-catenin's association with LEF1 and BCL9-2/B9L. PMID: 24419084 MiR-30-5p downregulation occurs as a result of interaction between multiple myeloma cells and bone marrow stromal cells, which in turn enhances expression of BCL9. PMID: 24599134 we detected five SNPs in the first two genes/loci - BCL9 and C9orf5 - strongly associated with negative symptoms of schizophrenia PMID: 23382809 Inhibition of the BCL9-beta-catenin interaction and selectively suppresses oncogenic Wnt transcription. PMID: 22914623 growth factor induced proliferation mediates a neutralizing response by significantly increasing miR-30c-2* which reduces BCL9 expression and cell proliferation in SKOV-3 and OVCAR-3 cells PMID: 22024689 These findings indicate that common variations in the BCL9 gene confer risk of schizophrenia and may also be associated with bipolar disorder and major depressive disorder in the Chinese Han population. PMID: 21383261 Pygo2 PHD is the only known PHD finger that is capable of interacting simultaneously with two functional ligands, B9L and BCL9 PMID: 20637214 crystallographic analysis of how beta-catenin, BCL9, BCL9-2 and Tcf4 interact PMID: 17052462 BCL9 itself contains a transcriptional activation domain in the C terminus, which functionally synergizes in lymphoid cells with the C-terminal transactivation domain of beta-catenin. PMID: 18347063 Data show that human and Drosophila Pygo PHD fingers associate with their cognate HD1 domains from BCL9/Legless to bind specifically to the histone H3 tail methylated at lysine 4 (H3K4me). PMID: 18498752 Overexpression and altered subcellular localization of ATG16L1 protein in human oral squamous-cell carcinoma: correlation with lymphovascular invasion and lymph-node metastasis are reported. PMID: 18789482 The amino-terminus of the BCL9 peptide is critical for maintaining the wild-type binding affinity of the BCL9 peptide to beta-catenin. PMID: 19715304 Findings suggest that deregulation of BCL9 is an important contributing factor to tumor progression in multiple myeloma and colon neoplasms. PMID: 19738061

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.