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Search results

1000 results found for “Calreticulin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Ara h 2.0201

    Description:

    Allergen Ara h 2.0201 (Conglutin-7) Recombinant

    Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    Product # :

    ALR-007

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    Description

    Recombinant Allergen Ara h 2.0201 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20,000 Dalton. Ara h 2.0201 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Ara h 2.0201 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.

    • Synonyms

      Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ara H 20201
  • View Data Sheet

    Name :

    CXCL8 Human, GST

    Description:

    Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag

    Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    Product # :

    CHM-047

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    Description

    Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Applications

      Immunoassay.

    • Background

      What is the source or expression system of CXCL8 HUMAN, GST Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, GST Protein?
      The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.

      What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is composed from 72 amino acids.

      What applications can CXCL8 HUMAN, GST Protein be used in?
      CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, GST Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, GST Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 8 Human
  • View Data Sheet

    Name :

    LIN28 Human

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

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    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Lin28 Human
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

    Price :

    Quantity :

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    Shipped at Room temp

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    • More Info
    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      Escherichia Coli.

      What is the Purity of BDNF Protein?
      BDNF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

      What applications can BDNF Protein be used in?
      BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Bdnf Human
  • View Data Sheet

    Name :

    Cyclophilin A Mouse

    Description:

    Cyclophilin A Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    Product # :

    ENZ-857

    Price :

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    Description

    Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cyclophilin A Mouse
  • View Data Sheet

    Name :

    DNAJC19 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 19 Human Recombinant

    Mitochondrial import inner membrane translocase subunit TIM14, DnaJ homolog subfamily C member 19, DNAJC19, TIM14, TIMM14, Pam18.

    Product # :

    HSP-039

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    Description

    DNAJC19 Human Recombinant fused with a 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids (19-116 a.a.) and having a molecular mass of 15.1kDa. The DNAJC19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DNAJC19 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNAJC19 is part of a complex involved in the ATP-dependent transport of transit peptide-containing proteins from the inner cell membrane to the mitochondrial matrix. DNAJC19 is a single-pass membrane protein which contains a J domain and is localized to the inner membrane of the mitochondrion. Expressed ubiquitously, DNAJC19 acts as a component of the mitochondrial DNAJC19 complex that is responsible for the ATP-dependent translocation of select proteins from the inner mitochondrial membrane to the mitochondrial matrix. Defects in the DNAJC19 gene are the cause of 3-methylglutaconic aciduria type 5 (MGA5), otherwise known as dilated cardiomyopathy with ataxia (DCMA).

    • Synonyms

      Mitochondrial import inner membrane translocase subunit TIM14, DnaJ homolog subfamily C member 19, DNAJC19, TIM14, TIMM14, Pam18.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGRY VLQAMKHMEP QVKQVFQSLP KSAFSGGYYR GGFEPKMTKR EAALILGVSP TANKGKIRDA HRRIMLLNHP DKGGSPYIAA KINEAKDLLE GQAKK.

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    Dnajc19 Human
  • View Data Sheet

    Name :

    NDP Human

    Description:

    Norrie Disease Human Recombinant

    800x600 Norrin, EVR2, FEVR, ND, Norrie disease protein, X-linked exudative vitreoretinopathy 2 protein, NDP, Norrie Disease. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    PRO-1674

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    Description

    NDP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (25-133) and having a molecular mass of 14.8 kDa.NDP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Source

    Escherichia Coli.

    Formulation

    The NDP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Norrie Disease (NDP) is a secreted regulatory protein which activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. NDP takes part in retinal vascularization by acting as a ligand for FZD4 which signals through stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. NDP is involved in a pathway that regulates neural cell differentiation and proliferation and also in neuroectodermal cell-cell interaction.

    • Synonyms

      Norrin, EVR2, FEVR, ND, Norrie disease protein, X-linked exudative vitreoretinopathy 2 protein, NDP, Norrie Disease.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKTDSSFI MDSDPRRCMR HHYVDSISHP LYKCSSKMVL LARCEGHCSQ ASRSEPLVSF STVLKQPFRS SCHCCRPQTS KLKALRLRCS GGMRLTATYR YILSCHCEEC NS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ndp Human
  • View Data Sheet

    Name :

    SLC3A2 Human

    Description:

    Solute Carrier Family 3 Member 2 Human Recombinant

    Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.

    Product # :

    PRO-2489

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    Description

    SLC3A2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (206-630a.a.) and having a molecular mass of 47.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).SLC3A2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SLC3A2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SLC3A2, also known as Solute Carrier Family 3 Member 2, is a single-pass type II membrane protein which is part of the SLC3A transporter family. SLC3A2 is expressed ubiquitously in all tissues tested with the highest levels detected in kidney, placenta and testis and lowest level in thymus. SLC3A2 is essential for the function of light chain amino-acid transporters and also takes part in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 participates in guiding and targeting of LAT1 and LAT2 to the plasma membrane.

    • Synonyms

      Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPRAPRCRE LPAQKWWHTG ALYRIGDLQA FQGHGAGNLA GLKGRLDYLS SLKVKGLVLG PIHKNQKDDV AQTDLLQIDP NFGSKEDFDS LLQSAKKKSI RVILDLTPNY RGENSWFSTQ VDTVATKVKD ALEFWLQAGV DGFQVRDIEN LKDASSFLAE WQNITKGFSE DRLLIAGTNS SDLQQILSLL ESNKDLLLTS SYLSDSGSTG EHTKSLVTQY LNATGNRWCS WSLSQARLLT SFLPAQLLRL YQLMLFTLPG TPVFSYGDEI GLDAAALPGQ PMEAPVMLWD ESSFPDIPGA VSANMTVKGQ SEDPGSLLSL FRRLSDQRSK ERSLLHGDFH AFSAGPGLFS YIRHWDQNER FLVVLNFGDV GLSAGLQASD LPASASLPAK ADLLLSTQPG REEGSPLELE RLKLEPHEGL LLRFPYAAHH HHHH.

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    Slc3A2 Human
  • View Data Sheet

    Name :

    BAG3 Human

    Description:

    BCL2-Associated Athanogene 3 Human Recombinant

    BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.

    Product # :

    PRO-760

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    Description

    BAG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 595 amino acids (1-575 a.a.) and having a molecular mass of 63.7 kDa. The BAG3 protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The BAG3 protein contains 20mM Tris buffer pH-8, 1mM EDTA, 10% glycerol and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BAG3 Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG3 has anti-apoptotic activity. BAG proteins participate with Hip for their binding to Hsc70/Hsp70 ATPase domain and encourage substrate release. BAG proteins have about 45 amino acid BAG domain close to the C terminus however they differ noticeably in their N-terminal regions. BAG3 includes a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact particularly with the Hsc70 ATPase domain in vitro and in mammalian cells. They bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. BAG3 plays a role as a protein-refolding cochaperone of the bcl2 binding protein BAG family and as upregulated in response to persistent stress of cellular calcium balance dysregulation. BAG3 has been shown to diminish stress-induced apoptosis.

    • Synonyms

      BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP.

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    Bag3 Human
  • View Data Sheet

    Name :

    OTC Human

    Description:

    Ornithine Carbamoyltransferase Human Recombinant

    Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    Product # :

    ENZ-596

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    Description

    OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

    • Synonyms

      Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.

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    Otc Human
  • View Data Sheet

    Name :

    ERCC1 Human

    Description:

    Excision Repair Cross-Complementing 1 Human Recombinant

    Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.

    Product # :

    PRO-1106

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    Description

    ERCC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (1-273) and having a molecular mass of 32.5kDa.ERCC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ERCC1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.

    • Synonyms

      Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMDPGKD KEGVPQPSGP PARKKFVIPL DEDEVPPGVA KPLFRSTQSL PTVDTSAQAA PQTYAEYAIS QPLEGAGATC PTGSEPLAGE TPNQALKPGA KSNSIIVSPR QRGNPVLKFV RNVPWEFGDV IPDYVLGQST CALFLSLRYH NLHPDYIHGR LQSLGKNFAL RVLLVQVDVK DPQQALKELA KMCILADCTL ILAWSPEEAG RYLETYKAYE QKPADLLMEK LEQDFVSRSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP

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    Ercc1 Human
  • View Data Sheet

    Name :

    GIP Human

    Description:

    Gastric Inhibitory Polypeptide Human Recombinant

    Gastric inhibitory polypeptide, GIP, Incretin hormone.

    Product # :

    PRO-1438

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    Description

    GIP Human Recombinant produced in E. coli is a single polypeptide chain containing 155 amino acids (22-153) and having a molecular mass of 17.3kDa. GIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.

    • Synonyms

      Gastric inhibitory polypeptide, GIP, Incretin hormone.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEKKEGHF SALPSLPVGS HAKVSSPQPR GPRYAEGTFI SDYSIAMDKI HQQDFVNWLL AQKGKKNDWK HNITQREARA LELAGQANRK EEEAVEPQSS PAKNPSDEDL LRDLLIQELL ACLLDQTNLC RLRSR.

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    Gip Human
  • View Data Sheet

    Name :

    CEACAM7 Human

    Description:

    Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 Human Recombinant

    CEA, CGM2, Carcinoembryonic antigen CGM2.

    Product # :

    PRO-1483

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    Description

    CEACAM7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (36-242 a.a.) and having a molecular mass of 25.7kDa.CEACAM7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CEACAM7 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 (CEACAM7) is a member of the immunoglobulin superfamily, CEA family. CEACAM7 contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. CEACAM7 is intensely down-regulated in colonic adenocarcinomas.

    • Synonyms

      CEA, CGM2, Carcinoembryonic antigen CGM2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSTNIDVVP FNVAEGKEVL LVVHNESQNL YGYNWYKGER VHANYRIIGY VKNISQENAP GPAHNGRETI YPNGTLLIQN VTHNDAGIYT LHVIKENLVN EEVTRQFYVF SEPPKPSITS NNFNPVENKD IVVLTCQPET QNTTYLWWVN NQSLLVSPRL LLSTDNRTLV LLSATKNDIG PYECEIQNPV GASRSDPVTL NVRYESVQAS.

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    Ceacam7 Human
  • View Data Sheet

    Name :

    CEACAM8 Human

    Description:

    Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 Human Recombinant

    Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8

    Product # :

    PRO-2716

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    Description

    CEACAM8 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (35-320 a.a) and having a molecular mass of 32.3kDa.CEACAM8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CEACAM8 solution (1mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 (CEACAM8) is a cell surface glycoprotein which takes part in cell adhesion in a calciumindependent manner.CEACAM8mediates heterophilic cell adhesion with other carcinoembryonic antigen-related celladhesion molecules (CEACAM6 for example).CEACAM8main role is cell migration,cell adhesion, and pathogen binding.CEACAM-8 isexpressed mainly on the surface of human peripheral blood eosinophils isolated from healthy individuals andused as granulocyte marker.

    • Synonyms

      Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      QLTIEAVPSN AAEGKEVLLL VHNLPQDPRG YNWYKGETVD ANRRIIGYVI SNQQITPGPA YSNRETIYPN ASLLMRNVTR NDTGSYTLQV IKLNLMSEEV TGQFSVHPET PKPSISSNNS NPVEDKDAVA FTCEPETQNT TYLWWVNGQS LPVSPRLQLS NGNRTLTLLS VTRNDVGPYE CEIQNPASAN FSDPVTLNVL YGPDAPTISP SDTYYHAGVN LNLSCHAASN PPSQYSWSVN GTFQQYTQKL FIPNITTKNS GSYACHTTNS ATGRNRTTVR MITVSDHHHH HH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ceacam8 Human
  • View Data Sheet

    Name :

    CLEC5A Human

    Description:

    C-Type Lectin Domain Family 5, Member A Human Recombinant

    C-type lectin domain family 5 member A , CLECSF5, MDL-1, MDL1, C-type lectin superfamily member 5, Myeloid DAP12-associating lectin 1.

    Product # :

    PRO-2165

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    Description

    CLEC5A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (28-188 a.a) and having a molecular mass of 20.8kDa.CLEC5A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLEC5A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-type lectin domain family 5-member A isoform 1 (CLEC5A) is part of the CTL/CTLD superfamily which carry various functions, for instance cell-cell signaling, cell adhesion, glycoprotein turnover, in addition to their inflammation & immune response abilities. CLEC5A operates as a cell attachment receptor for all 4 serotypes of Dengue virus in addition to Japanese encephalitis virus. CLEC5A binds to the dengue virus and it triggers signaling through the phosphylation of TYROBP, as a result no viral entrance occurs, however this interaction does stimulate proinflammatory cytokine release. CLEC5A preforms as a positive regulator of osteoclastogenesis and also a main regulator of synovial injury & bone erosion for the period of autoimmune joint inflammation.

    • Synonyms

      C-type lectin domain family 5 member A , CLECSF5, MDL-1, MDL1, C-type lectin superfamily member 5, Myeloid DAP12-associating lectin 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSPQIFNKS NDGFTTTRSY GTVSQIFGSS SPSPNGFITT RSYGTVCPKD WEFYQARCFF LSTSESSWNE SRDFCKGKGS TLAIVNTPEK LKFLQDITDA EKYFIGLIYH REEKRWRWIN NSVFNGNVTN QNQNFNCATI GLTKTFDAAS CDISYRRICE KNAK.

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    Clec5A Human
  • View Data Sheet

    Name :

    Fibronectin Human

    Description:

    Fibronectin Human

    Product # :

    PRO-448

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    Description

    Human Fibronectin produced purified from Human Plasma having a Molecular Weight of 440kDa.

    Source

    Human Plasma.

    Formulation

    The Fibronectin was lyophilized from a non sterile 2mg/ml buffer of 10mM sodium phosphate, pH 7.5 and 0.15M NaCl.

    Purity

    ≥ 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the extracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin also takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C.

    • Solubility

      We suggest reconstituting the 1mg Fibronectin with a chaotropic agent such as urea at room temperature at a concentration of 0.2mg/ml using sterile water. Let stand 1-2 hours. The recommended concentration is 4M-5M urea.

      When using the protein as an attachment factor, wash the urea off after attaching the fibronectin to the growth surface (plate or dish).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fibronectin Human
  • View Data Sheet

    Name :

    CCL14 Human, His

    Description:

    HCC-1 (CCL14) Human Recombinant, His Tag

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-253

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    Description

    HCC-1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids (20-93 a.a.) and having a molecular mass of 10.9kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCC-1 solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CCL14 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN, HIS Protein?
      The biological functionality of CCL14 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL14 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

      What applications can CCL14 HUMAN, HIS Protein be used in?
      CCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hcc 1 Human His
  • View Data Sheet

    Name :

    CRYAB Human, His

    Description:

    Crystallin Alpha B Human Recombinant, His Tag

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-088

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    Description

    CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.

    • Background

      Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.

      Structural Insights into CRYAB Human Recombinant:

      CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.

      Cellular Functions in Proteostasis:

      As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.

      Implications in Neurodegenerative Disorders:

      CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.

      CRYAB in Cardiovascular Health:

      The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.

      Challenges and Future Directions:

      While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.

      CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

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    Cryab Human His
  • View Data Sheet

    Name :

    CTACK Mouse

    Description:

    CTACK Mouse Recombinant (CCL27)

    C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    Product # :

    CHM-013

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    Description

    CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CTACK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

    • Background

      What is the molecular weight/Mw of CTACK MOUSE Protein?
      CTACK MOUSE Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CTACK MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CTACK MOUSE Protein?
      CTACK MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTACK MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

      What is the amino acid sequence of CTACK MOUSE Protein?
      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

      What applications can CTACK MOUSE Protein be used in?
      CTACK MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTACK MOUSE Protein?
      The endotoxin level is minimal, CTACK MOUSE Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ctack Mouse
  • View Data Sheet

    Name :

    Eotaxin Human

    Description:

    Eotaxin Human Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-256

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    Description

    Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Eotaxin Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD

      SMKYLDQKSP TPKP.

    • Background

      What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
      EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.

      What is the source or expression system of EOTAXIN HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EOTAXIN HUMAN Protein?
      EOTAXIN HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of EOTAXIN HUMAN Protein?
      The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.

      What is the amino acid sequence of EOTAXIN HUMAN Protein?
      GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
      SMKYLDQKSP TPKP.

      What applications can EOTAXIN HUMAN Protein be used in?
      EOTAXIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EOTAXIN HUMAN Protein?
      The endotoxin level is minimal, EOTAXIN HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Eotaxin Human
  • View Data Sheet

    Name :

    Stratifin Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Sigma Human Recombinant

    14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    Product # :

    PKA-357

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    Description

    Stratifin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-248) and having a molecular mass of 27.7 kDa. Stratifin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Stratifin solution containing 20mM Tris-HCl pH-8, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.

    • Synonyms

      14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Stratifin Human
  • View Data Sheet

    Name :

    SYT13 Human

    Description:

    Synaptotagmin XIII Human Recombinant

    Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    Product # :

    PRO-1550

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    Description

    SYT13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (30-426) and having a molecular mass of 46.5kDa.SYT13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SYT13 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, 1mM PMSF, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SYT13 belongs to the great synaptotagmin protein family which contain 2 domains: cytoplasmic C terminus with two tandem C2 domains (C2A and C2B) and extracellular N-terminal transmembrane domain. Synaptotogmin family members have dissimilar biochemical properties and developmental profiles, and patterns of tissue distribution. Additionally, Synaptotogmins formulate homo- and heteromeric complexes with each other. Synaptotagmins operate as membrane traffickers in multicellular organisms.

    • Synonyms

      Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSCRHMHPK KGLLPRDQDP DLEKAKPSLL GSAQQFNVKK STEPVQPRAL LKFPDIYGPR PAVTAPEVIN YADYSLRSTE EPTAPASPQP PNDSRLKRQV TEELFILPQN GVVEDVCVME TWNPEKAASW NQAPKLHYCL DYDCQKAELF VTRLEAVTSN HDGGCDCYVQ GSVANRTGSV EAQTALKKRQ LHTTWEEGLV LPLAEEELPT ATLTLTLRTC DRFSRHSVAG ELRLGLDGTS VPLGAAQWGE LKTSAKEPSA GAGEVLLSIS YLPAANRLLV VLIKAKNLHS NQSKELLGKD VSVKVTLKHQ ARKLKKKQTK RAKHKINPVW NEMIMFELPD DLLQASSVEL EVLGQDDSGQ SCALGHCSLG LHTSGSERSH WEEMLKNPRR QIAMWHQLHL

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Syt13 Human
  • View Data Sheet

    Name :

    TAGLN Human

    Description:

    Transgelin Human Recombinant

    SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    Product # :

    PRO-851

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.

    • Synonyms

      SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tagln Human
  • View Data Sheet

    Name :

    TCEAL1 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 1 Human Recombinant

    Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.

    Product # :

    PRO-507

    Price :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TCEAL1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-159 a.a.) and having a molecular mass of 19.7kDa. The TCEAL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TCEAL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription elongation factor A protein-like 1 (TCEAL1) is a member of the transcription elongation factor A (SII)-like (TCEAL) family, which may function as nuclear phosphoproteins that modulate transcription in a promoter context-dependent manner. TCEAL1 is involved in transcriptional regulation. TCEAL1 is expressed in all tissues, especially highly expressed in the heart, ovary, prostate and skeletal muscle.

    • Synonyms

      Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDKPRKENEE EPQSAPKTDE ERPPVEHSPE KQSPEEQSSE EQSSEEEFFP EELLPELLPE MLLSEERPPQ EGLSRKDLFE GRPPMEQPPC GVGKHKLEEG SFKERLARSR PQFRGDIHGR NLSNEEMIQA ADELEEMKRV RNKLMIMHWK AKRSRPYPIL EHHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tceal1 Human
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