Recombinant Human Protocadherin Fat 1 (FAT1) Protein (His)

Name: Recombinant Human Protocadherin Fat 1 (FAT1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06558P
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 Protocadherin Fat 1 (FAT1) 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	Q14517
Target Symbol	FAT1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	RKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRNRQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV
Expression Range	4203-4588aa
Protein Length	Partial
Mol. Weight	49.2 kDa
Research Area	Others
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 an essential role for cellular polarization, directed cell migration and modulating cell-cell contact.
Subcellular Location	[Protocadherin Fat 1]: Cell membrane; Single-pass type I membrane protein.; [Protocadherin Fat 1, nuclear form]: Nucleus.
Database References	HGNC: 3595 OMIM: 600976 KEGG: hsa:2195 STRING: 9606.ENSP00000406229 UniGene: PMID: 29985391 Study showed that FAT1 exhibits a high frequency of mutations and a downregulated expression in esophageal squamous cell carcinoma (ESCC) leading to cell migration and invasion by affecting the cellular mechanical properties of ESCC cells. PMID: 29565465 FAT1 has a novel regulatory effect on EMT/stemness markers both via or independent of HIF-1alpha. The functional relevance of this study was corroborated by significant reduction in the number of soft-agar colonies formed in hypoxic-siFAT1 treated U87MG cells. PMID: 28994107 FAT1 mutational status is a strong independent prognostic factor in patients with HPV-negative head and neck squamous cell carcinoma; FAT1 mutation was significantly associated with better overall survival PMID: 26876381 Disruption of MAPK/ERK pathway by FAT1 contributes the epithelial mesenchymal transformation in esophageal squamous cell carcinomas. PMID: 28366557 Loss of function mutations in FAT1 and CASP8 prevent cell adhesion and promote cell migration and proliferation in oral squamous cell carcinoma cell lines. PMID: 27693639 We identified recurrent mutations in the novel penile cancer tumor suppressor genes CSN1(GPS1) and FAT1 PMID: 27325650 FAT1 and mAb198.3 may offer new therapeutic opportunities for CRC. PMID: 27328312 Data show that the two N-terminal SH3 domains of SH3 domain containing ring finger 1 (SH3RF1) protein interact with FAT1 protein. PMID: 28129444 At the molecular level, under hypoxia the FAT1 depletion-associated reduction in HIF1alpha was due to compromised EGFR-Akt signaling as well as increased VHL-dependent proteasomal degradation of HIF1alpha. PMID: 27536856 Low FAT1 expression was associated with poor prognosis in children with medulloblastoma. Furthermore, FAT1 may act on Wnt signaling pathway to exert its antitumor effect PMID: 27834469 Recessive mutations in FAT1 cause a distinct renal disease entity in four families with a combination of steroid-resistance nephrotic syndrome, tubular ectasia, haematuria and facultative neurological involvement. PMID: 26905694 that loss of FAT1 and beta-catenin are associated with breast cancer progression, aggressive behavior, and poor prognosis PMID: 26721716 FAT1 protein acts upstream of Hippo signalling through TAZ protein to regulate neuronal differentiation. PMID: 26104008 Fat1 is released from pancreatic cancer cells in its soluble form by ADAM10 mediated ectodomain shedding PMID: 24625754 our data suggest that defective FAT1 is associated with an FSHD-like phenotype. PMID: 25615407 FAT1 is expressed at lower levels in muscles that are affected at early stages of facioscapulohumeral muscular dystrophy progression. PMID: 26018399 Analysis revealed an aberrant expression of FAT1 predominantly in mature BCP-ALL and thymic T-ALL and a high rate of FAT1 mutations. PMID: 24972153 FJX1 does not influence the levels of FAT1 ectodomain phosphorylation. PMID: 25150169 FAT1 expression in HCC is regulated via promotor methylation. PMID: 24590895 Fat1 may therefore provide a new marker of MRD for patients with ALL lacking known genomic aberrations or within a multiplex approach to MRD detection. PMID: 23433465 This work establishes S1-processing as a clear functional prerequisite for ectodomain shedding of FAT1 with general implications for the shedding of other transmembrane receptors. PMID: 24560745 frequency of FAT1-mutated cases was significantly higher in drug resistant chronic lymphocytic leukemia than in unselected chronic lymphocytic leukemia PMID: 24550227 There is a mechanism to regulate death receptor-mediated apoptosis via an interaction between FAT1 and procaspase-8. PMID: 24442637 this study identifies a novel signaling mechanism mediated by FAT1 in regulating the activity of PDCD4 in gliomas. PMID: 22986533 Our study identifies FAT1 as a critical determinant of muscle form, misregulation of which associates with facioscapulohumeral dystrophy . PMID: 23785297 Taken together, these data strongly point to FAT1 as a tumor suppressor gene driving loss of chromosome 4q35, a prevalent region of deletion in cancer PMID: 23354438 FAT1 suppression in activated hepatic stellate cells caused a downregulation of NFkappaB activity PMID: 22959770 Lipid accumulation in myotubes derived from obese type 2 diabetic patients arises from abnormal FAT/CD36 cycling. PMID: 22194967 data presented demonstrate that Fat1 expression in preB-ALL has a role in the emergence of relapse and could provide a suitable therapeutic target in high-risk preB-ALL PMID: 22116550 In vitro localization studies of FAT1 showed that melanoma cells display high levels of cytosolic FAT1 protein, whereas keratinocytes, despite comparable FAT1 expression levels, exhibited mainly cell-cell junctional staining PMID: 21680732 FAT1 may be involved in the migration and invasion mechanisms of oral squamous cell carcinoma cells PMID: 21617878 Processing of FAT1 and the translocation of its cytoplasmic domain to the nucleus were studied. PMID: 15922730 A cadherin gene, FAT, confers susceptibility to bipolar disorder in four independent cohorts. In mice, Fat was shown to be significantly downregulated and Catnb and Enah were significantly upregulated in response to therapeutic doses of lithium. PMID: 16402135 Fat1 exhibit co-localisation with Homer-3 in cellular protrusions and at the plasma membrane of HeLa cells PMID: 16979624 results identify mutations in FAT as an important factor in the development of oral cancer and indicate the importance of FATs function in some squamous cell carcinomas PMID: 17325662 FAT1(WT) is up-regulated in migration, induces cellular process formation when overexpressed, and is necessary for efficient wound healing PMID: 17500054 This study did not support the two FAT polymorphism in the affectve disorder. PMID: 17895925 The results of this study supports an involvement of variation at the FAT gene in the etiology of BPAD. PMID: 17938632 Results point to a role of the FAT in astrocytic tumorigenesis and demonstrate the use of RAPD analysis in identifying specific alterations in astrocytic tumors. PMID: 19126244

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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.