Recombinant Human Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) Protein (His-SUMO)

Name: Recombinant Human Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10161P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) 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	O95831
Target Symbol	AIFM1
Synonyms	AIFM1; AIFM1_HUMAN; Apoptosis inducing factor 1, mitochondrial; Apoptosis inducing factor; Apoptosis inducing factor, mitochondrion associated, 1; Apoptosis-inducing factor 1; CMTX4; COWCK; COXPD6; Harlequin; Hq; mAIF; MGC111425; MGC5706; mitochondrial; Neuropathy, axonal motor-sensory, with deafness and mental retardation; neuropathy, axonal, motor-sensory with deafness and mental retardation (Cowchock syndrome); PDCD 8; PDCD8; Programmed cell death 8 (apoptosis inducing factor); Programmed cell death 8; Programmed cell death 8 isoform 1; Programmed cell death 8 isoform 2; Programmed cell death 8 isoform 3; Programmed cell death protein 8; Programmed cell death protein 8 mitochondrial; Programmed cell death protein 8 mitochondrial precursor; Programmed cell death protein 8 mitochondrial precursor; Striatal apoptosis inducing factor
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHE
Expression Range	103-612aa
Protein Length	Partial
Mol. Weight	71.6kDa
Research Area	Apoptosis
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	Functions both as NADH oxidoreductase and as regulator of apoptosis. In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Binds to DNA in a sequence-independent manner. Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import.; Has NADH oxidoreductase activity. Does not induce nuclear apoptosis.; Pro-apoptotic isoform.
Subcellular Location	Mitochondrion intermembrane space. Mitochondrion inner membrane. Cytoplasm. Nucleus. Cytoplasm, perinuclear region.; [Isoform 3]: Mitochondrion intermembrane space. Mitochondrion inner membrane.; [Isoform 4]: Mitochondrion. Cytoplasm, cytosol.; [Isoform 5]: Cytoplasm.
Protein Families	FAD-dependent oxidoreductase family
Database References	HGNC: 8768 OMIM: 300169 KEGG: hsa:9131 STRING: 9606.ENSP00000287295 UniGene: PMID: 28442737 new form of motor neuropathy expands the phenotypic spectrum of AIFM1 mutations and therefore, the AIFM1 gene should be considered in the diagnosis of hereditary motor neuropathies PMID: 28975462 X-linked hypomyelination with spondylometaphyseal dysplasia associated with mutations in AIFM1 PMID: 28842795 report of a family carrying a novel missense mutation in AIFM1 that exhibits an isolated axonal polyneuropathy with misassembly of mitochondrial complex I and III. PMID: 28888069 we sought to investigate mechanisms mediated by Hsp70 acetylation in relation to apoptotic and autophagic programmed cell death. Upon stress-induced apoptosis, Hsp70 acetylation inhibits apoptotic cell death, mediated by Hsp70 association with apoptotic protease-activating factor (Apaf)-1 and apoptosis-inducing factor (AIF), key modulators of caspase-dependent and -independent apoptotic pathways, respectively PMID: 28627586 Overexpression of full-length AIFM1 suppresses proliferation and induces apoptosis of HepG2 and Hep3B cells. Caspase 3 and DRAM are involved in full-length AIFM1-induced apoptosis in HepG2 and Hep3B cells. PMID: 29501488 Real-time PCR results showed that apoptosis-inducing factor (AIF) and calpain-1 mRNAs were highly expressed in the transitional segmentof the Hirschsprung's disease bowel, whereas autophagy protein 5 (Atg5) was highly expressed in the narrow segment. Western blot results were consistent with mRNA levels, with increased AIF, calpain-1, and Atg5 expressions in the transitional segment compared with the dilated segment. PMID: 28562483 Data revealed that under a nutrient deficient condition, CD317 functions as an anti-apoptotic factor through AIF-mediated caspase and autophagy-independent manner. PMID: 27444183 we report that AIF-independent PARP-1-dependent necrosis constitutes a major mechanism of RPE cell death leading to retinal degeneration in dry age-related macular degeneration . PMID: 28055012 Downregulation of AIF by hypoxia causes oxidative inactivation of the lipid phosphatase activity of phosphatase and tensin homolog on chromosome 10 (PTEN), with ensuing activation of Akt kinase, phosphorylation of the Akt substrate GSK-3beta and activation of WNT/beta-catenin signaling in colon cancer cells. PMID: 27543779 novel pathway for mda-7/IL-24-induced caspase-independent apoptosis in neuroblastoma cells mediated through modulation of AIF, ATM, and gamma-H2AX. PMID: 27197168 Study defines the mechanism whereby AIF is allosterically modulated by charge-complex formation with NADH. Two distinct molecular pathways couple AIF's active site to dimerization and release of its regulatory C-loop insert with implications for AIF allosteric switching in cell survival and death. PMID: 27818101 Whole exome sequencing indicated a single plausible candidate - the p.Asp237Gly variant in apoptosis inducing factor mitochondria associated 1 (AIFM1; chr. Xq26.1), and the p.Asp237Gly segregated with disease in two families. PMID: 27102849 Only a drastic decrease in the expression level or/and redox activity of AIF tends to cause an early and severe neurodegeneration, whereas less pronounced changes in the AIF properties could lead to a broad range of slowly progressive neurological disorders. PMID: 27178839 AIF translocation plays a role in influenza-virus-induced apoptosis. PMID: 27853862 Copper induces the activation of apoptosis through casp3/casp8/casp9/AIF/TP53 signaling pathways. Suggest that apoptosis activation mechanism is dependent on the concentration, time of exposure to Cu and cell type. PMID: 27046389 Estradiol inhibits oxidative stress-induced accumulation of AIF in nucleolus and PARP1-dependent cell death via estrogen receptor alpha in MCF-7 cells. PMID: 25280774 AIF may participate in but not be dominant in the process of retinal pigment epithelium cell apoptosis induced by oxidative stress. PMID: 27453270 Altogether these data indicate that AIF supports the growth and survival of metabolically defined pancreatic cancer cells and that this metabolic function may derive from a novel mechanism so far undocumented in other cancer types. PMID: 27108222 Cdk5-mediated phosphorylation of CHIP negatively regulates its neuroprotective function, thereby contributing to truncated AIF mediated neuronal cell death progression following neurotoxic stimuli. PMID: 26206088 Results identify PTEN as the substrate of AIF oxidoreductase and reveal a novel function for AIF in controlling tumor metastasis. PMID: 26415504 UDA decreased the St-induced changes in mitochondrial and cytosolic AIF level, whereas in Dox-model it affected only the cytosolic AIF content. PMID: 26012840 strongly support a direct relationship between AIF nuclear translocation and radiation induced cell death in hepatocellular carcinoma cell line HepG2 PMID: 26920061 identification of the novel interaction between Trx1 and AIF has provided opportunities to design and develop therapeutically relevant strategies that either promote or prevent this protein-protein interaction for the treatment of different disease PMID: 26119781 AIF bears a HSP-70 binding domain allowing association with HSP-70. PMID: 26165468 Missense mutations in AIFM1 are associated with X-linked recessive auditory neuropathy spectrum disorder. PMID: 25986071 AIF and its family member protein, AMID, are rotenone-sensitive NADH:ubiquinone oxidoreductases (of the NDH-2 type). PMID: 26063804 Summarizing what is known today, mutations in AIFM1 are associated with a progressive disorder with myopathy, ataxia and neuropathy. PMID: 25583628 These results suggest that AIF downregulation is a common event in kidney tumor development. AIF loss may lead to decreased STK3 activity, defective apoptosis and malignant transformation PMID: 24992339 Residues Regulating the Reductase Activity of the Human Mitochondrial Apoptosis Inducing Factor PMID: 26237213 Data indicate that poptosis-inducing factor (AIF) controls the mitochondrial import of mitochondrial membrane transport protein CHCHD4. PMID: 26004228 review describes the multistep course of parthanatos and its dependence on PAR signalling and nuclear AIF translocation. PMID: 24684389 Increased trophoblast apoptosis and altered expression levels of syncytin-1, calpain 1, and AIF is observed in preeclamptic placentas. PMID: 24413738 Inhibition of the AIF/CypA complex protects against intrinsic death pathways induced by oxidative stress. PMID: 24434516 both the mitochondrial and apoptotic functions of hAIF are interconnected and coenzyme controlled: a key information in the understanding of the physiological role of AIF in the cellular life and death cycle. PMID: 24914854 The E1B-55K or E4orf3 proteins independently prevented nuclear fragmentation subsequent to release of AIF from the mitochondria, possibly by altering the intracellular distribution of PAR-modified proteins. PMID: 24889240 Data show that buthionine sulfoximine and synergizes with hydroxychavicol in inducing apoptosis of chronic myeloid leukemic (CML) cells through the GSH-ROS-JNK-ERK-iNOS pathway by apoptosis inducing factor (AIF)-dependent manner. PMID: 24040019 Aif seems to have pro-apoptotic and anti-apoptotic roles in the same lineage in different contexts and at different stages PMID: 24434313 Bit1 plays pivotal roles in the development and progression of ESCC, and its biological functions in ESCC may be closely associated with AIF and Bcl-2 levels. PMID: 23955799 Apoptosis-inducing factor and leukocyte elastase inhibitor derived DNase II interact and can cooperate to induce cell death. PMID: 23673989 The diarylheptanoid hirsutenone sensitizes chemoresistant ovarian cancer cells to cisplatin via modulation of apoptosis-inducing factor and X-linked inhibitor of apoptosis. PMID: 24247248 the caspase-independent mitochondrial apoptosis factor, apoptosis-inducing factor (AIF) was upregulated following SPG treatment. These findings indicate that SPG exerts its anticancer effects on RC-58T/h/SA#4 primary prostate cancer cells PMID: 23443329 Calpain activation via Ca(2) flux plays an essential role in eliciting an AIF-mediated, caspase-independent apoptotic pathway in EV71-infected cells. PMID: 23515028 AIF knockdown disrupts function of complex I and therefore increases the superoxide production in mitochondria PMID: 23682427 Taken together our results demonstrate that parthenolide causes in the two cell lines a caspase-independent cell death, which is mediated by AIF(apoptosis-inducing factor ). PMID: 22688575 AIF is an important factor for advanced prostate cancer cells and that through control of energy metabolism and redox balance, the enzymatic activity of AIF is critical for this support. PMID: 23118229 Our findings expand the spectrum of AIF-related disease and provide insight into the effects of AIFM1 mutations. PMID: 23217327 We found AIF to be strongly expressed in the villous trophoblast and that small amounts of AIF were localized to the nucleus of the cells. PMID: 22133578 AIF is imported from the endoplasmic reticulum to the mitochondria via mitochondria-associated membranes and transport vesicles. PMID: 22134679 Different mechanisms preserve translation of programmed cell death 8 and JunB in poliovirus-infected endothelial cells. PMID: 22328780

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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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