Human SMPD1 - Recombinant Protein | Custom Made-To-Order

Name: Human SMPD1 (Sphingomyelin Phosphodiesterase) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-07929P
Price: 445.0 USD
Availability: InStock

SDS-PAGE analysis of Human SMPD1 (Sphingomyelin Phosphodiesterase) - Recombinant Protein, CAT# BLT-07929P, showing >90% purity under 15% SDS-PAGE (Reduced)

Price Save $150

Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,030 (Fall Promotion)
1 mg	$1,870 (Fall Promotion)

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 Acid Sphingomyelinase (ASM/SMPD1) Protein
Product Overview	This recombinant human Acid Sphingomyelinase (ASM/SMPD1) protein includes amino acids 62-628aa of the target gene is expressed in 293F cell.The protein is supplied in lyophilized form and formulated in PBSprior to lyophilization.
Target Uniprot Id	P17405
Recommended Name	Sphingomyelin phosphodiesterase
Gene Name	SMPD1
Synonyms	ASM;ASMASE;NPD
Species	Human
Predicted Molecular Mass	71 kDa
Expression System	Mammalian Cell
Expression Range	62-628aa
Tag	C-6His
Purity	>90%
Formulation	Lyophilized
Buffer	PBS
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	Neuroscience
Target Function	Converts sphingomyelin to ceramide. Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form.; In the lysosomes, converts sphingomyelin to ceramide. Plays an important role in the export of cholesterol from the intraendolysosomal membranes. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Modulates stress-induced apoptosis through the production of ceramide.; When secreted, modulates cell signaling with its ability to reorganize the plasma membrane by converting sphingomyelin to ceramide. Secreted form is increased in response to stress and inflammatory mediators such as IL1B, IFNG or TNF as well as upon infection with bacteria and viruses. Produces the release of ceramide in the outer leaflet of the plasma membrane playing a central role in host defense. Ceramide reorganizes these rafts into larger signaling platforms that are required to internalize P. aeruginosa, induce apoptosis and regulate the cytokine response in infected cells. In wounded cells, the lysosomal form is released extracellularly in the presence of Ca(2+) and promotes endocytosis and plasma membrane repair.; Lacks residues that bind the cofactor Zn(2+) and has no enzyme activity.; Lacks residues that bind the cofactor Zn(2+) and has no enzyme activity.; (Microbial infection) Secretion is activated by bacteria such as P. aeruginos, N. gonorrhoeae and others, this activation results in the release of ceramide in the outer leaflet of the plasma membrane which facilitates the infection.; (Microbial infection) Secretion is activated by human coronaviruses SARS-CoV and SARS-CoV-2 as well as Zaire ebolavirus, this activation results in the release of ceramide in the outer leaflet of the plasma membrane which facilitates the infection.
Subcellular Location	Lysosome. Lipid droplet. Secreted.
Protein Family	Acid sphingomyelinase family
Associated Diseases	Niemann-Pick disease A (NPDA); Niemann-Pick disease B (NPDB)

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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.