Recombinant Human Tumor Susceptibility Gene 101 Protein (TSG101) Protein (His)

Name: Recombinant Human Tumor Susceptibility Gene 101 Protein (TSG101) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07619P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Tumor Susceptibility Gene 101 Protein (TSG101) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99816
Target Symbol	TSG101
Synonyms	(ESCRT-I complex subunit TSG101)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRP
Expression Range	1-145aa
Protein Length	Partial
Mol. Weight	20.7 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	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan. It may also play a role in the extracellular release of microvesicles that differ from the exosomes.
Subcellular Location	Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody, Midbody ring. Nucleus.
Protein Families	Ubiquitin-conjugating enzyme family, UEV subfamily
Database References	HGNC: 15971 OMIM: 601387 KEGG: hsa:7251 STRING: 9606.ENSP00000251968 UniGene: Hs.523512
Tissue Specificity	Heart, brain, placenta, lung, liver, skeletal, kidney and pancreas.

Gene Functions References

this is the first study that implicates the importance of TSG101 in anoikis resistance of thyroid cancer. PMID: 30343281
In LNCaP prostate cancer cells, TSG101 overexpression recruits the androgen receptor (AR) to TSG101-containing cytoplasmic vesicles resulting in reduced AR protein level and AR transactivation activity downregulation. Immunofluorescence microscopy demonstrated that TSG101-decorated cytoplasmic vesicles are associated with late endosomes/lysosomes. PMID: 29859188
The authors provide evidence that the ubiquitin (Ub) E2 variant domain of Tsg101 provides chaperone function to HIV-1 Gag that is independent of its interaction with the Pro-Thr-Ala-Pro motif, supporting the hypothesis that the domain provides a function in addition to its well-established role in cellular endosomal sorting complex required for transport factor recruitment. PMID: 29123089
In this review, HIV-infected cells have TSG101 on their surface and thus can be used in antibody-based therapies. The development of a monoclonal antibody CB8-2 lessens the assembly of viruses from infected cells PMID: 29199609
Results indicate that Vpr overcomes the effects of TSG101 overexpression to support viral production by competing with TSG101 to bind Gag. PMID: 27648839
our studies reveal that Tsg101 plays a role in the trafficking of macropinocytosed Kaposi's sarcoma-associated herpesvirus in the endothelial cells PMID: 27764233
Knockdown of LAMP2A, a CMA-related protein, and TSG101, an mA-related protein, significantly but only partially decreased the punctate accumulation of GAPDH-HT in AD293 cells and primary cultured rat cortical neurons. PMID: 27377049
the variant alleles of TSG101 rs2292179 and ATF2 rs3845744 were associated with a reduced risk of breast cancer, particularly for subjects with BMI <24 (kg/m(2)) and postmenopausal women, respectively PMID: 26729199
TSGDelta154-1054 splice variant increases TSG101 oncogenicity by inhibiting its E3-ligase-mediated proteasomal degradation. PMID: 26811492
Results show that TSG101 bidirectionally modulates cell invasion through regulating MMP-9 mRNA expression in different cell types. PMID: 26608825
TSG101 plays an important role in the development of hepatocellular carcinoma PMID: 26537625
Expression of tsg101 mRNA and of TSG101 protein were significantly higher in the oxaliplatin resistant cell line than parent HT-29 cels. PMID: 26400331
PSAP motif of OFR3 is required for hepatitis E virus exit and interaction with host TSG101. PMID: 26457367
Stress-internalized EGFR is retained intracellularly by continued p38 activity in a mechanism involving ubiquitin-independent, ESCRT/ALIX-dependent incorporation onto intraluminal vesicles (ILVs) of MVBs PMID: 26066081
Tsg101 is necessary for the efficient transport and release of nucleocapsids in marburg virus-infected cells PMID: 25330247
our findings strongly suggest that TSG101 is a cellular target for HSV-1 tegument ubiquitin specific protease activity during infection. PMID: 25510868
Our findings thus indicate that TSG101 regulation of p21 is an important factor in the cellular function of TSG101. PMID: 24244542
The ESCRT component TSG101 is required for optimal Human papillomavirus 16 infection. PMID: 25010273
These data support the interferon-induced generation of a Tsg101- and ISG15-dependent checkpoint in the secretory pathway that compromises influenza virus release. PMID: 24237697
Authors describe a novel compound (compound 0013) that blocks the JUNV Z-Tsg101 interaction and inhibits budding of virus-like particles. PMID: 24522922
Knock down of TSG101 causes the EGFR to accumulate in low density endosomes. PMID: 23933150
Data indicate tht n the Biaka, strong signal of selection was detected at CUL5 and at TSG101. PMID: 23217182
These results support a model in which both HIV-1 Gag-induced membrane curvature and Gag-ESCRT interactions promote tetherin recruitment, but the recruitment level achieved by the former is sufficient for full restriction. PMID: 23408603
The results provide evidence for a two-step splicing pathway of the TSG101 mRNA in which the initial constitutive splicing removes all 14 authentic splice sites, thereby bringing the weak alternative splice sites into close proximity. PMID: 22675076
The expression of TSG101 in HCC is higher than that in corresponding non-cancer tissues and the expression level is closely correlated with TNM stage and metastasis of HCC. PMID: 22768867
identified TSG101 as a novel FIP4-binding protein, which can also bind FIP3. alpha-helical coiled-coil regions of both TSG101 and FIP4 mediate the interaction with the cognate protein PMID: 22348143
Overexpression of PEG10 and TSG101 was detected in gallbladder adenocarcinoma. PMID: 21455631
Depletion of endogenous Tsg101 by siRNA led to a significant reduction of HEV release in cultured cells. PMID: 21880841
HIV-1 infection affects the expression of host factors TSG101 and Alix PMID: 21528537
TSG101 knockdown in breast cancer cells induces apoptosis and inhibits proliferation. TSG101 may play a biological role through modulation of the MAPK/ERK signaling pathway in breast cancer. PMID: 21117030
TSG101 may induce the malignant phenotype of cells. PMID: 19787439
Taken together, these data indicate that Marburg virus nucleoprotein enhances budding of virus-like particles by recruiting Tsg101 to the VP40-positive budding site through a PSAP late-domain motif. PMID: 20504928
Results suggest that TSG101 down-regulation in cervical cancer cells is not regulated by genetic or epigenetic events. PMID: 20372822
show that ubiquitin recognition by TSG101 is required for cSMAC formation, T cell receptor (TCR) microcluster signal termination, TCR downregulation. PMID: 20399684
recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. PMID: 11916981
Negative regulation of cell growth and differentiation by TSG101 through association with p21(Cip1/WAF1). PMID: 11943869
structure and functional interactions of its binding sites PMID: 12006492
solution structure of the UEV (ubiquitin E2 variant) binding domain of Tsg101 in complex with a PTAP peptide that spans the late domain of HIV-1 p6(Gag) PMID: 12379843
interacts specifically with human immunodeficiency virus type 2 gag polyprotein, results in increased levels of ubiquinated gag, and is incorporated into HIV-2 virions PMID: 12388682
Human ortholog TSG101 does not substitute VPS23 in its ability to rescue the phenotype of defective plasma membrane proteins PMID: 12725919
truncated and full length forms of TSG101 inhibit HIV-1 budding by interacting with the p6 L domain and by disrupting the cellular endosomal sorting machinery PMID: 12743307
the TSG101 interaction with HRS is a crucial step in endocytic down-regulation of mitogenic signaling and this interaction may have a role in linking the functions of early and late endosomes PMID: 12802020
alternative splicing and role implicated in interaction with HIV-1 PMID: 14526201
TSG101 activates androgen receptor-induced transcription by transient stabilization of the monoubiquitinated state PMID: 14761944
Reduction of TSG101 protein has a negative impact on breast and prostate tumor cell growth PMID: 14991575
molecular interactions between Daxx and TSG101 establish an efficient repressive transcription complex in the nucleus PMID: 15033475
X-ray crystallography study of the UEV domain of TSG101 and ubquitin showed the basis for the binding recognition at high resolution. PMID: 15053872
Tsg101 and Nedd4.1 act successively in the assembly process of HTLV-1 to ensure proper Gag trafficking through the endocytic pathway up to late endosomes where the late steps of retroviral release occur. PMID: 15126635
TSG101 binds GR and protects the non-phosphorylated receptor from degradation. PMID: 15657031
interaction of Gag with Tsg101 and Alix favors budding from the plasma membrane and relieves a requirement for ubiquitination by Nedd4 PMID: 15908698

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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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