Recombinant Mouse Branched-Chain-Amino-Acid Aminotransferase, Cytosolic (BCAT1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11186P
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bcat1.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bcat1.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bcat1.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bcat1.

Recombinant Mouse Branched-Chain-Amino-Acid Aminotransferase, Cytosolic (BCAT1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11186P
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 Mouse Branched-Chain-Amino-Acid Aminotransferase, Cytosolic (BCAT1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P24288
Target Symbol BCAT1
Synonyms Bcat1; Eca39Branched-chain-amino-acid aminotransferase; cytosolic; BCAT(c); EC 2.6.1.42; Protein ECA39
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His
Target Protein Sequence MKDCSNGCSAPFAGERGSEEVAETFRAKDLIITPATVLKEKPDPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRQSILELAQQWGEFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPKLASRILGKLTDIQYGRVESDWTIELP
Expression Range 1-386aa
Protein Length Full Length
Mol. Weight 46.4 kDa
Research Area Metabolism
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 Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
Subcellular Location Cytoplasm.
Protein Families Class-IV pyridoxal-phosphate-dependent aminotransferase family
Database References
Tissue Specificity Expressed in brain and kidney. Overexpressed in MYC-induced brain tumors, lymphomas, as well as in a teratocarcinoma cell line.

Gene Functions References

  1. regulatory role in macrophage function PMID: 28699638
  2. results suggest transcriptional adaptations occur in BCATm KO mice that along with altered nutrient signaling may contribute to their previously reported protein turnover, metabolic and exercise phenotypes PMID: 26351290
  3. BCATc as a novel regulator of T cell activation and metabolism PMID: 24847056
  4. leucine supplementation increased the expression of enzymes (BCAT1, BCAT2 and BCKDK) that metabolize branched-chain amino acids. PMID: 24349566
  5. analysis of the biochemical mechanism of BCATm (branched-chain aminotransferase) catalysis of reversible transamination of leucine and alpha-ketoglutarate to KIC and glutamate PMID: 20736162
  6. Bcat1 is a candidate for the type I diabetes susceptibility locus Idd6 PMID: 14563018
  7. Bcat1 is part of the complex multigenic Pas1 locus, with a functional role for its intragenic polymorphisms in lung tumor susceptibility. PMID: 15064703
  8. These results demonstrate that the expression of the BCATc gene in the brain is specifically regulated by BDNF in a time- and region-dependent fashion. PMID: 16828066
  9. BCATc mRNA gradually appears in different brain regions starting from early stages of neural development, and is maintained until adulthood. PMID: 17150414
  10. BCATm(-/-) mice had elevated plasma branched-chain amino acids & decreased adiposity & body weight, despite eating more food, along with increased energy expenditure, improvements in glucose & insulin tolerance & protection from diet-induced obesity PMID: 17767905

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.

Recently viewed