Human ACKR3 - Recombinant Protein | Custom Made-To-Order

Name: Human ACKR3 (Atypical Chemokine Receptor 3) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-08636P
Price: 545.0 USD
Availability: InStock

Beta Lifescience recombinant protein notice with SDS-PAGE availability in next QC run

Price Save $50

Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,375
1 mg	$2,245

For direct online orders, quantity pricing will be displayed in cart when you add 5x100ug or 10x100ug

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Product Overview

Product Name	Recombinant Human Atypical chemokine receptor 3 (ACKR3) Protein
Product Overview	This recombinant human Atypical chemokine receptor 3 (ACKR3) protein includes amino acids 1-40 of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in PBS pH 7.4, 0.01% SKL, 5% Trehalose, 1% Mannitolprior to lyophilization.
Target Uniprot Id	P25106
Recommended Name	Atypical chemokine receptor 3
Gene Name	ACKR3
Species	Human
Predicted Molecular Mass	21 kDa
Expression System	E.coli
Expression Range	1-40
Tag	N-6His+sumo
Purity	>90%
Formulation	Lyophilized
Buffer	PBS pH 7.4, 0.01% SKL, 5% Trehalose, 1% Mannitol
Storage Condition	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.
Reconstitution Instruction	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%.
Applications	Positive Control; Immunogen; SDS-PAGE; WB
Research Area	Signal Transduction
Target Function	Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Cytoplasm, perinuclear region. Early endosome. Recycling endosome. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin-dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane.
Protein Family	G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily
Tissue Specificity	Expressed in monocytes, basophils, B-cells, umbilical vein endothelial cells (HUVEC) and B-lymphoblastoid cells. Lower expression detected in CD4+ T-lymphocytes and natural killer cells. In the brain, detected in endothelial cells and capillaries, and in

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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.