Recombinant Human Membrane-Bound Transcription Factor Site-1 Protease (MBTPS1) Protein (His-SUMO)

Name: Recombinant Human Membrane-Bound Transcription Factor Site-1 Protease (MBTPS1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03798P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Membrane-Bound Transcription Factor Site-1 Protease (MBTPS1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14703
Target Symbol	MBTPS1
Synonyms	MBTPS1; KIAA0091; S1P; SKI1Membrane-bound transcription factor site-1 protease; EC 3.4.21.112; Endopeptidase S1P; Subtilisin/kexin-isozyme 1; SKI-1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	DTGLSEKHPHFKNVKERTNWTNERTLDDGLGHGTFVAGVIASMRECQGFAPDAELHIFRVFTNNQVSYTSWFLDAFNYAILKKIDVLNLSIGGPDFMDHPFVDKVWELTANNVIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFEDNIARFSSRGMTTWELPGGYGRMKPDIVTYGAGVRGSGVKGGCRALSGTS
Expression Range	218-414aa
Protein Length	Partial
Mol. Weight	37.5kDa
Research Area	Epigenetics And Nuclear Signaling
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	Serine protease that cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4: known substrates are SREBF1/SREBP1, SREBF2/SREBP2, BDNF, GNPTAB, ATF6 and ATF6B. Cleaves substrates after Arg-Ser-Val-Leu (SREBP2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Also mediates the first step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes. Involved in the regulation of M6P-dependent Golgi-to-lysosome trafficking of lysosomal enzymes. It is required for the activation of CREB3L2/BBF2H7, a transcriptional activator of MIA3/TANGO and other genes controlling mega vesicle formation. Therefore, it plays a key role in the regulation of mega vesicle-mediated collagen trafficking.
Subcellular Location	Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein.
Protein Families	Peptidase S8 family
Database References	HGNC: 15456 OMIM: 603355 KEGG: hsa:8720 STRING: 9606.ENSP00000344223 UniGene: PMID: 29301965 In the absence of S1P, the catalytically inactive alpha/beta-subunit precursor of GlcNAc-1-phosphotransferase fails to be activated and results in missorting of newly synthesized lysosomal enzymes, and lysosomal accumulation of non-degraded material, which are biochemical features of defective GlcNAc-1-phosphotransferase subunits and the associated pediatric lysosomal diseases mucolipidosis type II and III. PMID: 28693924 Results suggest that (pro)renin receptor (s(P)RR) is generated by sequential processing by site-1 protease (S1P) and furin protein. PMID: 28013223 primordial SKI-1/S1P likely contained a simpler prodomain consisting of the highly conserved AB fragment that represents an independent folding unit PMID: 26645686 S1P substrate-dependent regulatory mechanisms for lipid synthesis and biogenesis of lysosomes are different PMID: 26108224 The interaction between S1P and C5a plays an important role in neutrophils for antineutrophil cytoplasmic antibody -mediated activation PMID: 25000985 Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments. PMID: 25378398 We show that SKI-1 is constitutively expressed in human pigment cells with higher SKI activity in seven out of eight melanoma cell lines compared with normal melanocytes. PMID: 23884247 Diabetic high-density lipoprotein carries higher levels of S1P compared with normal high-density lipoprotein. PMID: 23360427 Y285 of SKI-1 is crucial for the efficient processing of envelope glycoproteins from Old World and clade C New World arenavirus. PMID: 23536681 The role of MBTPS1 (SKI-1/S1P) peptides in cancer and approaches used to inhibit SKI-1/S1P were studied. PMID: 21568902 study found that the N-acetylglucosamine-1-phosphotransferase alpha/beta-subunit precursor is cleaved by S1P that activates sterol regulatory element-binding proteins in response to cholesterol deprivation; S1P functions in the biogenesis of lysosomes PMID: 21719679 S1P has a role in reducing the size of the luminal domain to prepare ATF6 to be an optimal S2P substrate PMID: 15299016 enzymatic activity of S1P is not calcium dependent, but can be modulated by a variety of mono- and divalent cations. S1P displayed pronounced positive cooperativity with a substrate derived from the viral coat glycoprotein of the lassa virus. PMID: 16973377 SKI-1/S1P inhibition resulted in reduced cholesterol synthesis and mRNA levels of the rate-limiting enzymes, HMG-CoA reductase and squalene epoxidase, in the cholesterol synthetic pathway. PMID: 17867930 Complementation of SKI-1/S1P-deficient cells with a SKI-1/S1P expression vector restored release of infectious Crimean-Congo hemorrhagic fever virus (>106 PFU/ml), confirming that SKI-1/S1P processing is required for incorporation of viral glycoproteins. PMID: 17898072 Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito. PMID: 18400865

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.