Recombinant Human IL-8 Protein (77AA)

Name: Recombinant Human IL-8 Protein (77AA)
Brand: Beta LifeScience
SKU: BL-2883NP
Availability: InStock

BL-2883NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality cytokines for advanced research, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Interleukin-8 is produced by our E.coli expression system and the target gene encoding Ala23-Ser99 is expressed.
Accession	P10145
Synonym	Interleukin-8; IL-8; C-X-C Motif Chemokine 8; Emoctakin; Granulocyte Chemotactic Protein 1; GCP-1; Monocyte-Derived Neutrophil Chemotactic Factor; MDNCF; Monocyte-Derived Neutrophil-Activating Peptide; MONAP; Neutrophil-Activating Protein 1; NAP-1; Protein 3-10C; T-Cell Chemotactic Factor; IL8; CXCL8
Gene Background	Interleukin-8 (IL-8) belongs to the neutrophil-specific CXC family of chemokines. It is one of the initial cytokines released from a variety of cell types, including T cells, endothelial cells and fibroblasts, in response to an inflammatory stimulus and acts by recruiting neutrophils, T-cells and basophils to the site of inflammation. Elevated Interleukin-8 levels are associated with the onset of a variety of disease states.
Molecular Mass	8.9 KDa
Apmol Mass	11 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
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	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively.
Subcellular Location	Secreted.
Protein Families	Intercrine alpha (chemokine CxC) family
Database References	HGNC: 6025 OMIM: 146930 KEGG: hsa:3576 STRING: 9606.ENSP00000306512 UniGene: PMID: 29578433 High levels of LIFR in colorectal cancer (CRC) facilitated proliferation and migration of endothelial cells, resulting in an increase in angiogenic activity. Moreover, IL-8 was found to play a role in the LIFR induced angiogenesis. IL-8 levels were correlated with LIFR levels in CRC tissues, whereas depletion of IL-8 led to a reduced angiogenic activity of LIFR in CRC cells. PMID: 29751081 PKC-delta isoform plays a crucial role in Tat-TLR4 signaling pathway to activate NF-kappaB and CXCL8 production. PMID: 28539656 CXCL8 was a target of miR-204, and miR-204 suppression could not increase cell viability, migration, invasion, and EMT procedure when CXCL8 was silenced. PMID: 29402343 Interleukin 8 - 845 T/C and + 781 C/T polymorphisms were analyzed. For + 781C/T locus, in the dominant genetic model, significant difference between TT vs. CC + CT genotypes that significantly had a protective role against periodontitis disease. Positive association between distribution of IL8 - 845 T/C alleles and risk of periodontitis disease. C allele of IL-8 - 845 increased the risk of periodontitis disease. PMID: 30078118 These results suggest a direct involvement of IL-8-CXCR1/2 axes in GBM progression by promoting both cell proliferation and invasion and indirectly by promoting neovascularization in the form of vascular mimicry. PMID: 30086759 These results show that AKIP1 is crucial in cervical cancer angiogenesis and growth by elevating the levels of the NF-kappaB-dependent chemokines CXCL1, CXCL2, and CXCL8. PMID: 29520695 The extramembranous domain of HofQ (emHofQ) was shown to interact with various cytokines, of which IL-8 exhibited the strongest interaction. PMID: 30088437 he protein expression levels of IL-8 were significantly decreased in SZ patients, but no significant difference in the mRNA levels of IL-8 was observed between SZ patients and NC subjects. PMID: 28476335 immune system process is indispensable in the progression of disease in colon, and identifies that IL-8 and MMP-9 play potential critical roles for the progression. PMID: 30074183 IL-8 production was significantly enhanced following treatment with both IL-17A and CSE, while treatment with either IL-17A or CSE alone caused only a slight increase in IL-8 production. PMID: 29463070 Work identified IL-8 as a positive regulator of homotypic CIC formation via enhancing intercellular adhesion. PMID: 30021676 V2O5 induction of CXCL8 and CXCL11 chemokines may lead to the appearance and perpetuation of an inflammatory reaction into the dermal tissue. Further studies are required to evaluate dermal integrity and manifestations in subjects occupationally exposed, or living in polluted areas. PMID: 29901202 Study findings point out that PAR2 could play an essential role in gastroesophageal reflux disease (GERD) pathogenesis - even repeated short-term exposure to weakly acidic conditions lead to the upregulation of PAR2 and subsequent activation of the intense IL-8 release in the esophageal mucosa and initiation of mucosal immune response in GERD. PMID: 29672302 Given that IL-8, MIP-1beta, and MCP-1 are chemokines that play important roles in recruitment of immunocompetent cells for immune defense and tumor cell clearance, the observed lower levels of these markers with increasing PM2.5 exposure may provide insight into the mechanism by which DEE promotes lung cancer. PMID: 29023999 These results suggested that stemness induction in SKOV3 cells by macrophages co-cultured with SKOV3-derived OCSLCs involved IL-8/STAT3 signaling. PMID: 29656182 IL-8-251T>A (rs4073) Polymorphism is associated with gastric Cancer. PMID: 30275190 expression level of CXCL8 had a positive relationship with recurrence probability in Acute myeloid leukemia. PMID: 29596823 These data were in close agreement with the reduced cell migration and colony formation. Results from the present study suggested that reparixin and SCH527123 may be promising therapeutic agents for the treatment of pancreatic cancer by inhibiting the IL8/CXCR1/2 signaling cascade. PMID: 29749433 A urinary IL-8 level of less than 61.25 pg/ml is more sensitive for prediction of complete remission in idiopathic membranous nephropathy patients. PMID: 29415357 berberine inhibited the expression of MCP-1 and IL-8 induced by LPS. PMID: 28852897 Regarding the IL-8 promoter T - 251A, the TA and AA genotypes were associated with significantly decreased risks of nasopharyngeal carcinoma (NPC) in a Taiwanese population compared with the wild-type TT genotype. The mRNA and protein expression levels for NPC tissues revealed no significant associations among the 20 NPC samples with different genotypes. PMID: 30200105 IL-8 +781 T/C polymorphism is associated with the severe Clostridium difficile infection PMID: 29203364 ShRNA mediated down-regulation of CXCL8 resulted in inhibition of cell proliferation, viability and invasion in vitro and a near complete growth reduction of tumor in vivo. PMID: 29679563 CSF IL-8 concentrations were significantly elevated in CNS tumor patients as compared to non-tumoral individuals. AUC for CSF IL-8 was higher than for its index (CSF IL-8/serum IL-8). PMID: 29086194 High IL8 expression is associated with melanoma. PMID: 29286146 Lipo-CPFX, but not CPFX, retained the anti-IL-8 releasing activity. PMID: 29337216 The results indicate significant contribution of IL8 on survival of hormonal dependent early-stage breast cancer patients and association with established parameters such as estrogen receptors/progesterone receptor and HER2. PMID: 28569250 the frequency of non-classical monocytes expressing CXCL8 was increased in systemic sclerosis patient and monocytes expressing CXCL8 PMID: 29127442 ntermediate Molecular Mass Hyaluronan and CD44 interactions enhanced normal PMN phagocytosis and IL-8 production PMID: 28730511 serum levels in active vitiligo significantly elevated compared to those in stable vitiligo patients PMID: 29115683 High IL8 expression is associated with pancreatic adenocarcinoma. PMID: 29205349 Compared with controls, the interleukin (IL)-8 A/A genotype was more common in acute pancreatitis (AP). PMID: 29215544 The presence of neither the first transmembrane helix of the receptor nor the lipid bilayer significantly affected the interactions of IL-8 with Binding Site-I of CXCR1. PMID: 29143165 CXCL8 is highly expressed in cervical cancer tissues and cell lines, and correlated with malignant status and prognosis in cervical cancer patients. PMID: 28883082 In conclusion, to our knowledge, this is the first study in the association of rs4073 and rs2227306 polymorphisms with childhood asthma risk in the Tunisian population. PMID: 28993876 Results show that IL8 expression level is regulated by APE1 which activates NF-KB. PMID: 27388124 aberrant miR-520c-3p expression may lead to reduced IL-8 expression and promote the mesenchymal phenotype in breast cancer cells, thereby increasing invasive growth. PMID: 29048659 increased levels of IL-8 are associated with factors of worse prognosis in ovarian cancer PMID: 28872976 Significantly elevated blood levels of IL-8 in myelodysplastic syndrome patients. PMID: 28856536 the elevated concentrations of CXCL13, CXCL8, and CXCL10 or their increasing CSF/serum ratios may be potential biomarkers of neurosyphilis PMID: 27650493 Results implicated the important role of PRL-3 in glycolysis metabolism through improving IL-8 secretion in colorectal cancer cells, and PRL-3 mediated glycolysis contributed to the promotion of cancer metastasis. PMID: 28791350 Changes in serum IL-8 levels could be used to monitor and predict clinical benefit from immune checkpoint blockade in melanoma and NSCLC patients PMID: 28595336 Lung cancer patients showed significantly lower levels of serum VEGF (1.9 fold) and IL-8 (~9 fold) than COPD patients. VEGF level was significantly higher (2.6 fold) in metastatic than non-metastatic cancer patients. An increase in MMP-9 (~1.6 fold) levels was observed in lung cancer patients. PMID: 27811960 CXCL1/8 secreted by adipose-derived mesenchymal stem cells could promote breast cancer angiogenesis. PMID: 28514506 our meta-analysis suggests that the IL-8 rs4073, A2767T, T11722T2, rs2234671, rs2230054, rs1126579, rs2227306, rs2227307, rs2227532, and T-738A polymorphisms are not associated with periodontitis while the IL-8 C1633T and rs1126580 polymorphisms may elevate the susceptibility of periodontitis based on the currently available evidences. PMID: 28446725 An analogue of human CXCL8, CXCL8(3-72)K11R/G31P (hG31P) has been developed. PMID: 28754019 inflammation triggered property of Microcystin-LR via IL-8/CXCR2 signaling PMID: 29197248 A high IL-8 content in urine sampled on day 1 after renal transplantation was positively correlated with the activity of metalloproteinase-9 in urine. This proves that both of these chemokines cooperate in ischaemia-reperfusion injuries in transplanted kidneys. PMID: 28494217 We discovered that IL-8 secreted from decidual stromal cells is a key cytokine enhancing the invasiveness of trophoblasts PMID: 28328096

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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.