Recombinant Human Cytochrome P450 26B1 (CYP26B1) Protein (His)

Name: Recombinant Human Cytochrome P450 26B1 (CYP26B1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01254P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Cytochrome P450 26B1 (CYP26B1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NR63
Target Symbol	CYP26B1
Synonyms	(Cytochrome P450 26A2)(Cytochrome P450 retinoic acid-inactivating 2)(Cytochrome P450RAI-2)(Retinoic acid-metabolizing cytochrome)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MLFEGLDLVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHHLVSTEWPRSTRMLLGPNTVSNSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSHPEAINVYQEAQKLTFRMAIRVLLGFSIPEEDLGHLFEVYQQFVDNVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYLDALDLLIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPTVLEKLRDELRAHGILHSGGCPCEGTLRLDTLSGLRYLDCVIKEVMRLFTPISGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFSQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNEILPETEAMLSATV
Expression Range	1-512aa
Protein Length	Full Length
Mol. Weight	63.5 kDa
Research Area	Cardiovascular
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	Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. Catalyzes the hydroxylation of carbon hydrogen bonds of atRA primarily at C-4. Essential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints.; Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Protein Families	Cytochrome P450 family
Database References	HGNC: 20581 OMIM: 605207 KEGG: hsa:56603 STRING: 9606.ENSP00000001146 UniGene: PMID: 27410456 Study investigated the distribution of Cyp26a1 and Cyp26b1 transcripts in the rat and human brain, identifying several novel regions of expression, including the cerebral cortex for both enzymes and striatum for Cyp26b1. PMID: 26374207 Holo-CRABPs had higher affinity for CYP26B1 than free atRA, but both apo-CRABPs(CRABP-I and CRABP-II ) inhibited the formation of 4-OH-RA by CYP26B1. PMID: 27416800 There was increased expression of mRNA CYP26B1 in oral cancer tissue compared to adjacent noncancerous tissues. PMID: 25839051 Our results suggested that the CYP26B1 splice variant is associated with the occurrence of BQ-related oral cancer. PMID: 25114974 homozygous carriers of the major (T) allele, relative to homozygous carriers of the minor (C) allele, of the CYP26B1 polymorphism rs2241057 may have an increased risk for the development of Crohn's disease. PMID: 23977348 inhibits fibroblasts-induced activation of mast cells and dermatitis PMID: 24726878 We report a 2p13.2 microdeletion in 2 subjects encompasing 2 genes, EXOC6B and CYP26B12 with clinical effects on cognitive function, and craniofacial and skeletal development. PMID: 23837398 Single nucleotide polymorphisms in CYP26B1, NANOS1 and STRA8 genes support involvement of meiotic program initiation genes in modifying the risk of azoospermia and oligozoospermia in a Han-Chinese population PMID: 23320086 CYP26B1 capacity is genetically regulated and suggest that local CYP26B1 activity may influence atherosclerosis. PMID: 22415012 Vascular cells express the spliced variant of CYP26B1 lacking exon 2 and it is also increased in atherosclerotic lesions PMID: 22666329 Detection of the methylation prevalence of KCNA4 and CYP26B1 together in serum demonstrated the good sensitivity and specificityin gastric cancer PMID: 21945024 Human null and hypomorphic mutations were identified in the gene encoding the retinoic acid degrading enzyme CYP26B1 that lead to skeletal and craniofacial anomalies, including fusions of long bones, calvarial bone hypoplasia, and craniosynostosis PMID: 22019272 The mRNA expression of CYP26A1 and CYP26B1 correlated between human tissues except for human cerebellum in which CYP26B1 was the predominant CYP26 and liver in which CYP26A1 dominated. PMID: 22020119 The presence of CYP26B1 in normal lung development (A549 cell line), & the capacity to convert retinol to retinoic acid, indicates that fetal human lung has the ability to regulate the supply of vitamin A from the pseudoglandular stage. PMID: 21482329 Increased expression of the CYP26B1 gene was observed in tumor tissue compared with adjacent normal tissue and it plays a novel role in the betel dependent pathogenesis of oral squamous cell carcinoma. PMID: 21641851 role of CYP26 in the regulation of all trans retinoic acid levels in human aortic smooth muscle cells PMID: 20606468 The predominant expression of CYP26A1 in the liver is in agreement with previous reports of tissue distribution of CYP26 mRNA in adult humans. PMID: 19884280 Studies in mice found that regulation of retinoid levels, affected by the retinoid-degrading enzyme CYP26B1, during fetal gonad development determined whether germ cells would become oocytes or spermatogonia. PMID: 16574820 CYP26B1 mRNA levels were approximately twice the level in adult cerebellum compared to adult whole brain samples. CYP26B1 levels were 10x higher in earlier gestational times than in later gestational times. PMID: 12101034 Mouse studies identified different expression patterns of the retinoic acid-metabolizing enzymes CYP26A1 and CYP26B1 during development. PMID: 11744378

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.