Recombinant Human Lipopolysaccharide-Induced Tumor Necrosis Factor-Alpha Factor (LITAF) Protein (GST)

Name: Recombinant Human Lipopolysaccharide-Induced Tumor Necrosis Factor-Alpha Factor (LITAF) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08159P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Human Lipopolysaccharide-Induced Tumor Necrosis Factor-Alpha Factor (LITAF) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99732
Target Symbol	LITAF
Synonyms	Lipopolysaccharide induced TNF alpha factor; CMT1C; FLJ38636; Lipopolysaccharide induced TNF alpha factor; Lipopolysaccharide induced TNF factor; Lipopolysaccharide induced tumor necrosis factor alpha factor; Lipopolysaccharide-induced tumor necrosis factor-alpha factor; LITAF; LITAF_HUMAN; LPS induced TNF alpha factor; LPS-induced TNF-alpha factor; MGC116698; MGC116700; MGC116701; MGC125274; MGC125275; MGC125276; p53 induced gene 7 protein; p53-induced gene 7 protein; PIG 7; PIG7; SIMPLE; Small integral membrane protein of lysosome/late endosome; TP53I7; Tumor protein p53 inducible protein 7
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSVPGPYQAATGPSSAPSAPPSYEETVAVNSYYPTPPAPMPGPTTGLVTGPDGKGMNPPSYYTQPAPIPNNNPITVQTVYVQHPITFLDRPIQMCCPSCNKMIVSQLSYNAGALTWLSCGSLCLLGCIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL
Expression Range	1-161aa
Protein Length	Full Length
Mol. Weight	44.1kDa
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	Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps downregulate downstream signaling cascades. Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes. Probably plays a role in regulating protein degradation via its interaction with NEDD4. May also contribute to the regulation of gene expression in the nucleus. Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines. May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10.
Subcellular Location	Cytoplasm. Nucleus. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane. Late endosome membrane. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane.
Protein Families	CDIP1/LITAF family
Database References	HGNC: 16841 OMIM: 601098 KEGG: hsa:9516 STRING: 9606.ENSP00000340118 UniGene: Hs.459940
Associated Diseases	Charcot-Marie-Tooth disease 1C (CMT1C)
Tissue Specificity	Ubiquitously and abundantly expressed. Expressed predominantly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.

Gene Functions References

results indicate that SIMPLE may regulate protein trafficking physiologically by localizing to the TGN and/or REs by binding PI4P. PMID: 29953492
our findings provide a novel apoptotic regulatory pathway in which LITAF, as a transcription factor, inhibits the expression of BCL6, which leads to activation of the intrinsic mitochondrial pathway and tumor apoptosis. PMID: 27764808
In this Chinese Han population a novel Charcot-Marie-Tooth disease-associated gene mutations the LITAF (c.32C>G) was discovered. PMID: 27862672
Molecular analysis of Charcot-Marie-Tooth 1C revealed five new LITAF/SIMPLE mutations PMID: 28211240
The Gly112Ser mutation causing Charcot-Marie-Tooth disease type 1C is a mild form of Charcot-Marie-Tooth disease. PMID: 28164329
An aberrant LITAF-phosphoethanolamine interaction on the surface of intracellular membranes contributes to the molecular pathogenesis that underlies Charcot-Marie-Tooth disease type 1C. PMID: 27927196
Study conclude that LITAF is a monotopic membrane protein whose membrane integration is stabilised by a zinc finger. The related human protein, CDIP1 (cell death involved p53 target 1), displays identical membrane topology, suggesting that this mode of membrane integration is conserved in LITAF family proteins. PMID: 27582497
PIG7 promotes leukemia cell chemosensitivity via lysosomal membrane permeabilization. PMID: 26716897
Suggest LITAF as regulatory of pro-inflammatory and pro-fibrogenic pattern in non-alcoholic fatty liver disease. PMID: 26573228
LITAF may serve as a switch in the balance between classical and alternative activation in tumor-associated inflammation. (Review) PMID: 26324337
Results show that LITAF mutants in Charcot-Marie-Tooth 1C have an altered intracellular localization. They localize either completely or partially in the mitochondria depending on the mutation site. This can explain the different severity of the disease. PMID: 25058650
Study shows that the I92V LITAF sequence variant would be a good candidate for a biomarker in the case of the CMT1A/HNPP disorders. PMID: 25342198
The results of this study findings confirm that the genetic analysis of LITAF/SIMPLE should be considered for the diagnostic flow-chart of CMT1 patient, especially when nerve conduction studies show the presence of conduction blocks. PMID: 24880540
Early-onset hereditary neuropathy with liability to pressure palsy (HNPP) was associated frequently with isoleucine92valine LITAF polymorphism. PMID: 24668782
It is concluded that PA can induce insulin resistance in liver cells and knockdown of LITAF expression can reduce insulin resistance in liver cells. PMID: 22282245
Mutation of SIMPLE (Litaf) in Charcot-Marie-Tooth 1C disease alters production of exosomes. PMID: 23576546
LITAF, a BCL6 target gene, regulates autophagy in mature B-cell lymphomas. PMID: 23795761
The findings indicate a function of SIMPLE as a regulator of endosomal trafficking and provide evidence linking dysregulated endosomal trafficking to CMT pathogenesis. PMID: 23166352
Two sequence variations c.269G-->A and c.274A-->G were detected in LITAF gene and two sequence variations c.1243G-->A and c.1910C-->T were detected in LMNA gene in Chinese Charcot-Marie-Tooth disease. PMID: 20709679
Lipopolysaccharide-induced tumor necrosis factor (LITAF) interacted with CIDE-3 in hepatic cells. PMID: 20957525
PIG7 could be transactivated by AML1, which subsequently induces differentiation and apoptosis of leukemia cells, especially those with AML1-ETO fusion gene PMID: 21836606
Our findings suggest that SIMPLE mutations cause Charcot-Marie-Tooth type 1 C peripheral neuropathy by a combination of loss-of-function and toxic gain-of-function mechanisms PMID: 21896645
Itch protein re-localization is dependent upon the interaction with the PPXY sequences of LITAF, since disruption of these binding motifs completely abrogates Itch re-localization. PMID: 21326863
LITAF is associated with obesity and insulin resistance, as well as inflammatory cytokine secretion. The results indicate LITAF to be a new mediator between inflammation and the obesity related disorders. PMID: 21362361
studies for the first time establish the regulatory axis of AMPK-LITAF-TNFSF15 and also suggest that LITAF may function as a tumor suppressor PMID: 21217782
New gene for CMT is located on chrosome 16. PMID: 14641644
The expression of SIMPLE is reported in various cell types of the sciatic nerve, including Schwann cells, the affected cell type in Charcot-Marie-Tooth neuropathy type 1C. PMID: 15122712
the potential E3 ubiquitin ligase activity of SIMPLE, alteration in its interactions with NEDD4 or TSG101, or changes in its properties as a clathrin coat adaptor may underlie the pathogenesis of Charcot-Marie-Tooth disease PMID: 15776429
This study identified a LITAF/SIMPLE substitution (T49M), absent in 1000 control chromosomes, but which was thought to be a polymorphism in Charcot-Marie-Tooth neuropathy. PMID: 16373087
The mutation Gly112Ser was found in two families confirming its frequent occurrence in SIMPLE mutations. Three novel mutations were also identified: Ala111Gly (two families), Pro135Ser, and Pro135Thr. PMID: 16787513
LITAF has a role in the pathophysiological regulation of the TNF-alpha gene PMID: 16804395
results suggest that the consensus sequence for hepatocyte nuclear factor-3alpha, or a nuclear binding protein to the CTCCC motif, may play an important role in regulating LPS-dependent LITAF transcription PMID: 16872372
Hypermethylation of pig7 promoter was identified in K562 and HL-60 cells, in contrast to non-methylation predominant in U937 cells. pig7 expression was markedly decreased in AL patients. PMID: 18078129

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.