Recombinant Human 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Protein (His)

Name: Recombinant Human 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09276P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) 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	P22557
Target Symbol	ALAS2
Synonyms	5 @aminolevulinate synthase erythroid specific; 5 aminolevulinate synthase 2; 5 aminolevulinate synthase 5 aminolevulinate synthase 2; 5 aminolevulinate synthase erythroid specific mitochondrial; 5 aminolevulinic acid synthase 2; 5 aminolevulinic acid synthase; 5-aminolevulinate synthase; 5-aminolevulinic acid synthase 2; Alas 2; ALAS; ALAS E; ALAS; erythroid; ALAS-E; Alas2; ALASE; Aminolevulinate delta synthase 2; Aminolevulinic acid synthase 2; erythroid; ANH1; ASB; Delta ALA synthase 2; Delta ALA synthetase; Delta aminolevulinate synthase 2; Delta aminolevulinate synthase; Delta-ALA synthase 2; Delta-aminolevulinate synthase 2; Erythroid specific ALAS; erythroid-specific; FLJ93603; HEM0_HUMAN; mitochondrial; OTTHUMP00000023388; OTTHUMP00000023389; OTTMUSP00000020679; RP23-338A17.1; SIDBA1; XLDPP; XLEPP; XLSA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	QIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQEQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
Expression Range	50-587aa
Protein Length	Full Length of Mature Protein
Mol. Weight	63.5 kDa
Research Area	Cancer
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

Subcellular Location	Mitochondrion matrix.
Protein Families	Class-II pyridoxal-phosphate-dependent aminotransferase family
Database References	HGNC: 397 OMIM: 300751 KEGG: hsa:212 STRING: 9606.ENSP00000332369 UniGene: PMID: 29958424 report confirms the considerable variability in manifestations among patients with ALAS2 or SLC25A38 mutations and draws attention to differences in the assessment and the monitoring of iron overload and its complications PMID: 28772256 A novel ALAS2 missense mutation in exon 9 affects the enzymatic activity of ALAS2 by affecting its interaction with the cofactor pyridoxal 5'-phosphate in X-linked sideroblastic anemia. PMID: 28667034 a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented PMID: 28731922 int-1-GATA site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons. PMID: 28123038 From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations. PMID: 27751851 data indicate that the X-linked protoporphyria variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS PMID: 26300302 In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients. PMID: 24829177 the primary deficiency in ferrochelatase leads to a secondary increase in ALAS2 expression. PMID: 25179834 The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects. PMID: 25705881 the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown. PMID: 23935018 5 families with X-linked sideroblastic anemia had mutations in a GATA transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene. PMID: 24166784 Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria. PMID: 23364466 ALAS2 gain-of-function mutations increas the specific activity (DeltaAT, DeltaAGTG and p.Q548X) or stability (DeltaG) of the enzyme, thereby leading to the increased erythroid protoporphyrin accumulation causing X-linked protoporphyria. PMID: 23348515 A large gain-of-function domain within the C-terminus of ALAS2 is associated with X-linked dominant protoporphyria. PMID: 23263862 Late-onset photosensitivity was caused by ALAS2 mutation in a family with dominant protoporphyria. PMID: 23223129 X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2). PMID: 22740690 the C-terminal region of ALAS2 protein may function as an intrinsic modifier that suppresses catalytic activity and increases the degradation of its protein, each function of which is enhanced by the Met567Ile mutation and Val562Ala mutation, respectively PMID: 22269113 Data suggest that ALAS2 gene mutations should be considered not only as causative of X-linked sideroblastic anemia (XLSA) and XLDPP but may also modulate gene function in other erythropoietic disorders. PMID: 21653323 identification of five probands with sideroblastic anemia and ALAS2 R452S (due to SNP); all were African-American males; all presented with moderate anemia; the four adults presented with iron overload [a multi-case report from the United States] PMID: 21800356 Thirteen different ALAS2 mutations were identified in 16 out of 29 probands with sideroblastic anemia. PMID: 21309041 We found the previously published R452H and R452C ALAS2 mutations in 3 patients with X-linked sideroblastic anemia PMID: 21252495 HIF1-mediated ALAS2 upregulation promotes erythropoiesis to satisfy the needs of an organism under hypoxic conditions. PMID: 21207956 About 4% of unrelated EPP patients have X-linked dominant protoporphyria (MIM 300752) caused by gain-of-function mutations in the ALAS2 gene leading to an increased erythroid heme biosynthesis & protoporphyrin accumulation. Review. PMID: 20850938 Seven ALAS2 mutations were detected in eight sporadic CSA cases, two being novel: V301A in a male patient and R517G in a female patient PMID: 19731322 A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. PMID: 12031592 A C to G transversion at nucleotide -206 from the transcription start site was found in the proximal promoter region of ALAS2 in X-linked sideroblastic anemia. The region of the mutation may bind a novel and important erythroid regulatory element. PMID: 12663458 the major splice isoform of ALAS2 is functional in vivo and could significantly contribute to erythroid heme biosynthesis and hemoglobin formation PMID: 14643893 there is nucleotide variation at Msn and Alas2 on the X chromosome PMID: 15166166 sequence identity of ALAS from Rhodobacter capsulatus and human eALAS is 49% PMID: 16121195 ALAS2 mutations might contribute to more severe iron loading in persons with primary hemochromatosis. PMID: 16446107 upon the NaBu stimulation, binding of Sp1 protein to ALAS2 promoter increased significantly, with concurrent increases in acetylation level of histone H3 and dimethylation level of H3-Lysine4 at ALAS2 promoter PMID: 18555711 An impact of ALAD2 on blood lead levels or hemoglobin was not seen in Romanian women from a lead-contaminated region. PMID: 18569569 gain-of-function mutations in ALAS2 cause a previously unrecognized form of porphyria, X-linked dominant protoporphyria, characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes PMID: 18760763 Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G. PMID: 19066423 Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling. PMID: 19187226

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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.

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