Recombinant Human HOXB4 Protein (L175D, E176K, E178K, N-6His)

Beta LifeScience SKU/CAT #: BL-1626NP
BL-1626NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1626NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human HOXB4 Protein (L175D, E176K, E178K, N-6His)

Beta LifeScience SKU/CAT #: BL-1626NP
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Product Overview

Description Recombinant Human Homeobox Protein B4 is produced by our E.coli expression system and the target gene encoding Met1-Leu251 (Leu175Asp, Glu176Lys, Glu178Lys) is expressed with a 6His tag at the N-terminus.
Accession P17483
Synonym Homeobox protein Hox-B4; Homeobox protein Hox-2.6; Homeobox protein Hox-2F; HOXB4; HOX2F
Gene Background Homeobox B4 (HOXB4) is encoded by the HOXB4 gene which is a member of the the class I homeobox (HOX) gene family and encodes a nuclear protein with a homeobox DNA-binding domain. These genes are master control regulators of developmental programs including embryonic and adult hematopoiesis. Multiple HOX genes, including HOXB4, are highly expressed in the hematopoietic stem cells (HSC) compartment. HOXB4 gene can act in opposite ways when expressed by different cells, promoting the proliferation of stem cells whilst activating the apoptotic pathway in some embryonic structures. The protein HOXB4, as a homeodomain transcription factor, has been shown to be an important regulator of stem cell renewal and hematopoiesis. Incellular or ectopic expression of HOXB4 expands hematopoietic stem and progenitor cells in vivo and in vitro, making it a potential candidate for therapeutic stem cell expansion.
Molecular Mass 29.8 KDa
Apmol Mass 36 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 4mM HCl.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular Location Nucleus.
Protein Families Antp homeobox family, Deformed subfamily
Database References

HGNC: 5115

OMIM: 142965

KEGG: hsa:3214

STRING: 9606.ENSP00000328928

UniGene: PMID: 28969513

  • Authors observed that induced expression of HOXB4 in the UW473 cell line significantly reduced in vitro cell proliferation and migration capability of UW473 cells with no effect on the in vivo tumorigenicity. PMID: 29039487
  • Study revealed that HOXB4 was highly expressed in ovarian cancer cells. HOXB4 silencing enhanced the cytotoxic effect of Taxol and DDP by downregulating ABC transporters via inhibition of the PI3K/Akt signaling pathway. These results for the first time elucidated the critical roles and molecular basis of HOXB4 underlying drug resistance in ovarian cancer cells. PMID: 29660518
  • HOXB4 knockout led to downregulation of P-glycoprotein, multidrug resistance-associated protein 1 and breast cancer resistance protein expression and PI3K/Akt signaling activity, suggesting that repression of HOXB4 might be a key point to reverse Multidrug resistance of K562/ADM cells. PMID: 27779650
  • This study provides novel evidences of the mechanisms integrating Notch and TNF-alpha signaling in the transcriptional induction of GATA3 and HOXB4. PMID: 27251160
  • Increased expression of HOXB4 in human embryonic stem cells enhances the production of hematopoietic Progenitors but does not effect the maturation of red blood cells. PMID: 27352929
  • The analysis of HOX expression in primary mesothelioma tumors indicated that these cells could also be sensitive to the disruption of HOX activity by HXR9, and that the expression of HOXB4 is strongly associated with overall survival PMID: 26867567
  • showed that OAC1 treatment led to OCT4-mediated upregulation of HOXB4 PMID: 26202933
  • a crucial regulator of NK lytic function PMID: 24810639
  • Epigenetic analysis revealed that increased promoter methylation of HOXB4 correlates with decreased expression of its transcript in oral cancer cell lines. HOXB4 may work as an epigenetic biomarker gene. PMID: 24859765
  • Our study demonstrates for the first time the regulation of HOXB4 by miR-23a PMID: 23630040
  • our results outline the effects of HOXB4 in combination with stromal cells in the development of NK cells from embryonic stem cells. PMID: 22761810
  • GATA-2 directly regulates HOXB4 expression in hematopoietic stem cells, which may play an important role in the development and/or progression of aplastic anemia. PMID: 23028422
  • HOXB4-positivity as an independent predictor of overall survival of acute myeloid leukemia patients PMID: 22664110
  • Expressions of ABCB1, BMI-1, HOXB4 were not detected in the patients with non-malignant hematologic diseases, but were higher in de novo acute leukemia patients and lower in patients in complete remission. PMID: 22040961
  • Comparative transcriptome analysis of CD34(+) cells subjected or not to HOXB4 or HOXC4 demonstrated that both homeoproteins regulate the same set of genes, some of which encode key hematopoietic factors and signaling molecules. PMID: 22298821
  • cytomegalovirus infection markedly down-regulated HOXB4 expression which affected proliferation and differentiation of erythroid and lymphocyte progenitor cells. PMID: 22402911
  • Down-regulation of mitochondria and lysosomal genes by HoxB4 plays a role in the impaired lymphoid lineage development from embryonic stem cells-derived hematopoietic stem cells. PMID: 22438249
  • Hox B4 protein is present in the precursor lesions as CC cells, suggesting that Hox B4 could be a protein related to the neoplastic state (non-differentiated cells) of human cervical epithelium. PMID: 22120585
  • These results indicate that transient, but not constitutive, HoxB4 expression is sufficient to augment the hematopoietic differentiation of embryonic stem and induced pluripotent stem cells. PMID: 22000550
  • The demethylation of CpG island in the promoter region of HOXB4 gene may be correlated with the high expression of HOXB4 gene in CD34(+) cells, while the promoter methylation of HOXB4 gene may be associated with HOXB4 gene silencing in PBMCs. PMID: 19549386
  • these data suggest that increased HoxB4 enhanced early megakaryocytic development in human TF1 cells and CD34 positively-selected cord blood cells primarily by upregulating TpoR and Fli-1 expression and downregulating c-Myb expression. PMID: 20599537
  • overexpression of HOXB4 in human ESC did not improve the generation of CD34(+) hematopoietic cells via co-culture methodology PMID: 19878058
  • may play a role in the regulation of cellular proliferation/adhesion in developing fetal human epidermis and in hyperproliferation conditions, including cancers, in adult epidermis PMID: 11984874
  • Retrovirally mediated expression of HOXB4 rapidly triggers an increase in the number of stem cells without alternating the balance of lymphomyeloid reconstitution, suggesting that HOXB4 does not affect control of end-cell output. PMID: 12130496
  • In NOD/SCID mice HOXB4-overexpressing cord blood CD34+ cells had a selective growth advantage in vivo. However, high HOXB4 expression substantially impaired myeloerythroid differentiation & B-cell output. PMID: 12406897
  • NF-Y is a developmentally regulated inducer of the HOXB4 gene in hematopoietic cells. PMID: 12791656
  • The growth promoting effects of HOXB4 are critically dependent on HOXB4 expression levels and that this can result in important species-specific differences in potency. PMID: 17510218
  • The protein transduction domain-Hoxb4protein can be used with other recombinant proteins to efficiently generate transplantable hemaat4opoietic stem cells from human embryonic stem cells. PMID: 17784829
  • contribution of HOXB4 in the maintenance of the intrinsic lymphomyeloid differentiation potential of defined hematopoietic progenitor cell subsets PMID: 17962697
  • overexpression of HoxB4 in differentiating hESCs increases hematopoietic colony formation and hematopoietic cell formation in vitro, but does not affect in vivo repopulation in adult mice hosts PMID: 18511880
  • These data suggest that HoxB4-induced effects on human embryonic stem cell-derived hematopoietic stem cells are concentration-dependent during in vitro development and reduce proliferation of other cell types in vitro and in vivo. PMID: 18617691
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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.

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