Recombinant Mouse Long-Chain-Fatty-Acid--Coa Ligase 4 (ACSL4) Protein (His)

Name: Recombinant Mouse Long-Chain-Fatty-Acid--Coa Ligase 4 (ACSL4) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01835P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Long-Chain-Fatty-Acid--Coa Ligase 4 (ACSL4) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9QUJ7
Target Symbol	ACSL4
Synonyms	Arachidonate--CoA ligase Long-chain acyl-CoA synthetase 4
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	EILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALVDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGE
Expression Range	100-581aa
Protein Length	Partial
Mol. Weight	59.3 kDa
Research Area	Signal Transduction
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 conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially activates arachidonate and eicosapentaenoate as substrates. Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs. Modulates prostaglandin E2 secretion.
Subcellular Location	Mitochondrion outer membrane; Single-pass type III membrane protein. Peroxisome membrane; Single-pass type III membrane protein. Microsome membrane; Single-pass type III membrane protein. Endoplasmic reticulum membrane; Single-pass type III membrane protein. Cell membrane.
Protein Families	ATP-dependent AMP-binding enzyme family
Database References	KEGG: mmu:50790 STRING: 10090.ENSMUSP00000033634 UniGene: PMID: 24879802 ACSL4 plays a tumor-suppressive role in gastric cancer. PMID: 26949059 Report PPARdelta-mediated regulatory mechanism for ACSL4 expression in liver tissue and cultured hepatic cells. PMID: 25645621 Sequence analysis of a 1.5-kb fragment of the Acsl4 promoter revealed the absence of a TATA box and the presence of many putative binding sites for transcription factors including Sp1 and CREB. PMID: 23376217 Acsl4 is a phosphoprotein whose phosphorylation is hormone-dependent. PMID: 23159612 These results indicate that the ACS4 protein specifically expressed in brain plays an important role in arachidonate metabolism and neuronal differentiation in the brain. PMID: 22366036 the involvement of SHP2 activity in the regulation of the expression of the fatty acid-metabolizing enzyme ACSL4 PMID: 21903867

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.