Recombinant Mouse C-X-C Motif Chemokine 15 (CXCL15) Protein (His&Myc)

Name: Recombinant Mouse C-X-C Motif Chemokine 15 (CXCL15) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06984P
Price: 680.8 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Chemokines and receptors, Cytokines, Cytokines and growth factors, Recombinant proteins

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Product Overview

Description	Recombinant Mouse C-X-C Motif Chemokine 15 (CXCL15) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9WVL7
Target Symbol	CXCL15
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	QELRCLCIQEHSEFIPLKLIKNIMVIFETIYCNRKEVIAVPKNGSMICLDPDAPWVKATVGPITNRFLPEDLKQKEFPPAMKLLYSVEHEKPLYLSFGRPENKRIFPFPIRETSRHFADLAHNSDRNFLRDSSEVSLTGSDA
Expression Range	26-167aa
Protein Length	Full Length of Mature Protein
Mol. Weight	23.8 kDa
Research Area	Immunology
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	Chemotactic for neutrophils. Involved in lung-specific neutrophil trafficking during normal and inflammatory conditions.
Subcellular Location	Secreted.
Protein Families	Intercrine alpha (chemokine CxC) family
Database References	KEGG: mmu:20309 STRING: 10090.ENSMUSP00000031322 UniGene: Mm.64326
Tissue Specificity	Expression restricted to the lung, produced by bronchoepithelial cells and is released into the airways. Expressed at low levels in fetal lung.

Gene Functions References

inflammation triggered property of Microcystin-LR via IL-8/CXCR2 signaling PMID: 29197248
this study shows that ponciretin may attenuate ethanol-induced gastritis via the regulation of IL-8 secretion PMID: 28013186
Adh binds to OR5M11, which enhances Actinobacillus pleuropneumoniae pathogenicity by activating p38 which induces apoptosis of PAMs and IL-8 release PMID: 27046446
Findings suggest that IL8-dependent osteoclast activation may constitute an early event in the initiation of the joint specific inflammation in anti-citrullinated protein-positive rheumatoid arthritis. PMID: 26612338
Data suggest that CXCL1/IL-8, released from osteoclasts in an autoantibody-dependent manner, produces pain by activating sensory neurons. PMID: 26613766
IL-8 signaling is up-regulated in alcoholic hepatitis. PMID: 26260904
expressions of IL-1beta and IL-8 in the brain increased after ApoE knockout in mice PMID: 25940280
CYLD negatively regulates nontypeable Haemophilus influenzae-induced IL-8 expression via MKP-1-dependent inhibition of ERK. PMID: 25389768
Taken together, these results indicate that CD147 promotes lung cancer-induced osteoclastogenesis by modulating IL-8 secretion, and suggest that CD147 is a potential therapeutic target for cancer-associated bone resorption in lung cancer patients. PMID: 25661002
these data outline a novel role for the P2Y6 receptor in the induction of CXCL8/IL-8 production and barrier dysfunction in response to C. difficile toxin exposure and may provide a new therapeutic target for the treatment of CDI. PMID: 24278446
these data suggest that IL-8 plays an important role in breast cancer osteolysis PMID: 24486955
T. crispa ethanol extract fraction was used to investigate the potential immunomodulatory effect of different T. crispa doses ranging from 25 mug/mL to 1000 mug/mL on RAW 246.7 cells by detecting intracellular INF-gamma, IL-6, and IL-8 expressions. PMID: 24969238
We found that IL-33 could induce and enhance the expression of IL-6 and IL-8 in PBMCs of COPD mice via p38 MAPK pathway. PMID: 24866242
The hepatic expression of IL8 and LAMC2 has high sensitivity for biliary atresia at diagnosis and may serve as a biomarker of disease, with an important role for the IL8 signaling in experimental disease. PMID: 24493287
These results suggest that increased IL-8 (mKC) levels may be involved in steroid-resistant neutrophilic airway inflammation through an NF-kappaB-dependent pathway. PMID: 23456484
The HIF-1alpha/IL-8 signaling pathway plays a critical role in the protective effects of endothelial progenitor cells in the ischemic hind limb of diabetic mice. PMID: 23252631
Changes in IL-8 expression level during development is related to its regulatory role in mouse mammary gland immunity. PMID: 23096912
CagA may potentially interfere with TAK1 activity during NF-kB activation for IL-8 induction in early H. pylori infection PMID: 23409168
These data suggest that IL-8 participates in the formation of cystic structures by Madin-Darby canine kidney cells in 3D culture and that HGF may stimulate tubulogenesis through the suppression of IL-8. PMID: 23485708
ExoU activates NF-kappaB, stimulating IL-8 expression and secretion during P. aeruginosa infection PMID: 22848596
Met signaling regulates the secretion of the pro-angiogenic chemokine interleukin-8/CXCL8 PMID: 22815748

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.