Recombinant Human Lupus La Protein (SSB) Protein (His)

Name: Recombinant Human Lupus La Protein (SSB) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06376P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Lupus La Protein (SSB) 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	P05455
Target Symbol	SSB
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ
Expression Range	1-408aa
Protein Length	Full Length
Mol. Weight	52.9 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation.
Subcellular Location	Nucleus.
Database References	HGNC: 11316 OMIM: 109090 KEGG: hsa:6741 STRING: 9606.ENSP00000260956 UniGene: PMID: 28782243 our data support a novel model, whereby cancer-associated La protein contributes to cisplatin resistance by stimulating the translation of anti-apoptotic factor Bcl2 in HNSCC cells. PMID: 27105491 La protein is an important microprocessor component regulating miRNA processing efficiency by association with DGCR8 to regulate formation of the DGCR8-Drosha complex for miRNA processing. PMID: 29087193 La functions as gatekeeper ensuring correct tRNA maturation and protecting the miRNA pathway from potentially functional tRNA fragments. PMID: 27345152 Findings identified two novel SUMO acceptors sites on La and suggest that sumoylation of La alters its RNA-binding activity, which could influence a broad range of RNA processing steps where La's function has been implicated. PMID: 27224031 Binding of double-stranded RNA involves less penetration into the RNA recognition motif (RRM2) binding pocket and more engagement with the unstructured C-terminus of the La C-terminal domain (CTD). PMID: 27959512 At the 3' UTR, HUR facilitates circularization of the viral genome through interaction with another host factor, La, which is critical for replication. PMID: 26339049 expression of nuclear hLa Ag induces thymic clonal deletion and tTreg selection, and lymphocytic infiltration of the lung is a consequence of La-specific CD4(+) T cell autoimmunity PMID: 25582858 Authors provide a model whereby a novel interplay between RNA-binding, RNA chaperoning and AKT phosphorylation of La protein regulates CCND1 IRES-mediated translation. PMID: 25520193 Primary Sjogren's patients with WSP form a benign subgroup, with a lower prevalence of anti-SSB and extraglandular manifestations. PMID: 24529195 A beta turn in the human La protein is responsible for the interaction with the hepatitis C virus RNA. PMID: 24478427 Total IgG levels correlate positively with autoantibodies La, Ro60 and Ro52 but not with RING or B-box domain antibodies of Ro52. PMID: 23554036 The competition between the host factor (La) and the viral protein (NS3) for binding to HCV IRES might regulate the molecular switch from translation to replication of HCV. PMID: 22355520 Our study demonstrates that La plays a critical role in regulating HCV replication by interacting with the GCAC motif. PMID: 23552417 Sjogren syndrome antigen B (SSB)/La promotes global microRNA expression by binding microRNA precursors through stem-loop recognition PMID: 23129761 Iron promotes the translation initiation of hepatitis C virus by stimulating the expression of eIF3A and La proteins. PMID: 22634302 oxidants cause nuclear export of La/SSB protein and subsequent association of La/SSB with Nrf2 untranslated regions and ribosomes PMID: 22207702 data indicate that the JAK2(V617F) mutation affects p53 response to DNA damage through the upregulation of La antigen and accumulation of MDM2 PMID: 21785463 the structural elements required for La-mediated RNA chaperone activity PMID: 22203678 La binds to domain IV of the hepatitis C virus RNA using an RNA recognition that is quite distinct from its mode of binding to RNAs with a 3' UUU(OH) trailer. PMID: 22009680 function of the RNA-binding protein La in promoting tumor progression of head and neck squamous cell carcinoma PMID: 22016766 Autoantigen La promotes efficient RNAi, antiviral response, and transposon silencing by facilitating multiple-turnover RNA-induced silencing complex catalysis. PMID: 22055194 Overexpression of mouse or human La enhanced M-MuLV particle release in the absence of glycosylated gag. PMID: 21343359 La protein binds to and mediates interaction of the 5' and 3' noncoding ends of the Japanese encephalitis virus genome. PMID: 21294637 show elevated La protein expression in cervical cancer tissue and its correlation with aberrant CCND1 protein levels in cervical tumor tissue lysates PMID: 20856207 There is a correlation between La protein and HBV mRNA and the expression of HBV protein. PMID: 17064465 study found expression of La protein is induced by HCV infection, and this induced La protein-activated telomerase activity in a hepatoma cell line; HCV infection might be strongly related to telomerase activity in the liver through La protein induction PMID: 20497049 nuclear trafficking by La affects the normal order of pre-tRNA processing PMID: 12049746 molecular characterization of the human La protein.hepatitis B virus RNA.B interaction in vitro PMID: 12121976 La autoantigen is required for the internal ribosome entry site-mediated translation of Coxsackievirus B3 RNA PMID: 12384597 binds differentially to multiple sites within the 5' untranslated region of Coxsackievirus B3 RNA PMID: 12457960 in addition to full-length La protein, both N- and C-terminal halves were able to interact with hepatitis C virus internal ribosome entry site in vivo. PMID: 12540850 Dengue 4 virus minus strand 3'UTR RNA binds with La protein in human monocytes PMID: 12584332 Results suggest that La ribonucleoproteins (RNP) exist in distinct states that differ in subcellular localization, serine 366 phosphorylation, and associated RNAs. PMID: 14636586 La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices PMID: 15004549 La protein binds to the 5' end and with the 3' UTR of Dengue virus RNA; interacts with the dengue virus nonstructural proteins NS5 and NS3 PMID: 15084396 NMR assignment and secondary structure of the La motif PMID: 15213463 Composition of La/hepatitis B virus ribonucleoprotein particles as well as interacting cellular factors, are critical determinants in the regulation of the stability of the HBV RNA. PMID: 15302879 RRM1 and La motifs bind pre-tRNA PMID: 15371415 CK2 is responsible for La S(366) phosphorylation in vivo PMID: 15485924 Nonphosphorylated SSB interacts with nucleolin at nucleolar sites involved in rRNA biogenesis. PMID: 15572691 This protein is s host factors responsible for the regulation of the hepatitis C virus internal ribosome entry site. PMID: 15685555 essential for efficient hepatitis C virus replication PMID: 15823607 In vitro RNA chaperone activity pf SSB was studied. PMID: 15928345 nuclear retention of peptidylglycine alpha-amidating monooxygenase (PAM) mRNA is lost upon expressing the La proteins that lack a conserved nuclear retention element, suggesting a direct association between PAM mRNA and La protein in vivo PMID: 16107699 Anti-La antibodies bound to immunodominant epitopes of La within the NH(2)-terminus and the RNA recognition motif (RRM) region of apoptotic human cells PMID: 16320341 Here, we show by chromatin immunoprecipitation (ChIP) that La is associated with pol III-transcribed genes in vivo PMID: 16344466 Results report the crystal structure of the N-terminal domain of human La, consisting of La and RRM1 motifs, bound to RNA. PMID: 16387655 Changes in salivary production rate are associated with aging and SSB antibodies. PMID: 16467037 La protein undergoes nucleocytoplasmic shuttling whereas EBER1 and EBER2 noncoding RNA's are confined to the nucleus. PMID: 16682524

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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.