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Search results

1000 results found for “Dynactin”

Name

Description

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  • View Data Sheet

    Name :

    GDF15 Human

    Description:

    Growth and Differentiation Factor 15 Human Recombinant

    GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    Product # :

    CYT-335

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    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN Protein?
      GDF15 HUMAN Protein has a total Mw of 24.8kDa.

      What is the source or expression system of GDF15 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN Protein?
      GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN Protein?
      The biological functionality of GDF15 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF15 HUMAN Protein?
      MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

      What applications can GDF15 HUMAN Protein be used in?
      GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN Protein?
      The endotoxin level is minimal, GDF15 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.

    Gdf15 H Human
  • View Data Sheet

    Name :

    DSIP

    Description:

    Delta Sleep Inducing Peptide

    Product # :

    HOR-030

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH

    • Background

      Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.

      DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.

      In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

      Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.

      While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

    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.

    Dsip
  • View Data Sheet

    Name :

    PDIA6 Human, Active

    Description:

    Protein Disulfide Isomerase A6 Human Recombinant, Active

    Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    Product # :

    ENZ-994

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
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    • More Info

    Description

    PDIA6 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 442 amino acids (20-440 a.a.) and having a molecular mass of 48.5kDa. The PDIA6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDIA6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 10 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of INS in the presence of DTT.

    More Info

    • Introduction

      PDIA6 belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6, also has a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

    • Synonyms

      Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    • 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 MLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL.

    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.

    Pdia6 Human Active
  • View Data Sheet

    Name :

    IL-9 Human, Sf9 Active

    Description:

    Interleukin 9 Human Recombinant, Sf9, Active

    Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

    Product # :

    CYT-1143

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    IL-9 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 132 amino acids (19-144 aa) and having a molecular mass of 14.9kDa.IL-9 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL-9 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

    More Info

    • Introduction

      Interleukin-9 is a protein that acts as one of the regulators of hematopoiesis. IL-9 is an enhancer of cells and megakaryoblastic leukemic cells’ growth. Among this protein’s producers we can find cells like mast cells, Treg, NKT cells, Th17, Th2, ILC2, and Th9 cells in various amounts. Th9 are the primary CD4 cells (T cells) that IL-9 is produced in.

    • Synonyms

      Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

    • 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

      QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
      TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH 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.

    Interleukin 9 Human
  • View Data Sheet

    Name :

    LYVE1 Human 25-235 a.a.

    Description:

    Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 (25-235 a.a) Human Recombinant

    HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.

    Product # :

    PKA-349

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    Description

    LYVE1 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 229 amino acids and having a molecular mass of 24.8 kDa. As a result of glycosylation, the LYVE1 migrates on SDS-PAGE at approximately 50 kDa. LYVE1 is expressed with 15 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    High Five insect cells.

    Formulation

    The LYVE1 protein solution contains 20mM Tris buffer pH-7.5 and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      LYVE1 is a selective marker of the lymphatic endothelium & a surface endocytic receptor for both soluble and immobilized hyaluronan, LYVE1 is an extracellular glycosaminoglycan that plays a role in cell adhesion and migration. LYVE1 functions in lympathic hyaluronan transport and is involved in tumor metastasis. Recombinant human LYVE1 was expressed in and purified by conventional chromatography techniques. The normal adult human choroid is endowed with a significant number of LYVE-1 positive macrophages. LYVE-1 is expressed in a reticulum cell neoplasm in an axillary lymph node. This reticulum cell sarcoma is a lymphatic sinus lining cell sarcoma which might represent another subtype of reticulum cell sarcomas.
      LYVE-1 immunohistochemistry is a functional method for detecting lymphatics invaded by cancer cells, and detailed examination of the submucosa around the tumor is important for predicting LN metastasis.

    • Synonyms

      HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.

    • 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

      DPLRAEELS IQVSCRIMGI TLVSKKANQQ LNFTEAKEAC RLLGLSLAGK DQVETALKAS FETCSYGWVG DGFVVISRIS PNPKCGKNGV GVLIRKVPVS RQFAAYCYNS SDTWTNSCIP EIITTKDPIF NTQTATQTTE FIVSDSTYSV ASPYSTIPAP TTTPPAPAST SIPRRKKLIC VTEVFMETST MSTETEPFVE NKAAFKNEAA GFGGSGRLVP RGSHHHHHH.

    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.

    Lyve1 Human 25 235 Aa
  • View Data Sheet

    Name :

    FAM50A Human

    Description:

    Family with Sequence Similarity 50, Member A Human Recombinant

    9F, DXS9928E, HXC-26, HXC26, XAP5, XAP-5.

    Product # :

    PRO-1477

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    Description

    FAM50A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (150-339 a.a.) and having a molecular mass of 25.2kDa.FAM50A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FAM50A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      FAM50A is a member of the FAM50 family. FAM50A is highly conserved in length and sequence among numerous species. FAM50A is a basic protein comprised of a nuclear localization signal, and can function as a DNA-binding protein or a transcriptional factor. FAM50A expressed in all tissues mainly abundant in fetal brain, liver and kidney. High levels of FAM50A were observed in the adult's skeletal muscle, spleen, thymus, prostate and the small intestine.

    • Synonyms

      9F, DXS9928E, HXC-26, HXC26, XAP5, XAP-5.

    • 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 MGSTTKKRKL GKNPDVDTSF LPDRDREEEE NRLREELRQE WEAKQEKIKS EEIEITFSYW DGSGHRRTVK MRKGNTMQQF LQKALEILRK DFSELRSAGV EQLMYIKEDL IIPHHHSFYD FIVTKARGKS GPLFNFDVHD DVRLLSDATV EKDESHAGKV VLRSWYEKNK HIFPASRWEP YDPEKKWDKY TIR.

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    Fam50A Human
  • View Data Sheet

    Name :

    PFDN5 Human

    Description:

    Prefoldin Subunit 5 Human Recombinant

    Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    Product # :

    PRO-901

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    Description

    PFDN5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 19.5kDa.PFDN5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFDN5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFDN5 is a member of the prefoldin alpha subunit family. Prefoldin (PFDN) being a ubiquitously expressed heterohexameric co-chaperone, is required for proper folding of nascent proteins, in particular, tubulin and actin. PFDN5 is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold properly. The PFDN5 protein may also limit the transcriptional activity of the proto-oncogene c-Myc.

    • Synonyms

      Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-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 MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA.

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    Pfdn5 Human
  • View Data Sheet

    Name :

    CANX Human

    Description:

    Calnexin Human Recombinant

    Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    Product # :

    PRO-725

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    Description

    CANX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 462 amino acids (21-481 a.a.) and having a molecular mass of 52.5kDa.The CANX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CANX protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.

    • Synonyms

      Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    • 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

      MHDGHDDDVI DIEDDLDDVI EEVEDSKPDT TAPPSSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVEEM KESKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGIYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIPDPEAV KPDDWDEDAP AKIPDEEATK PEGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPR CESAPGCGVW QRPVIDNPNY KGKWKPPMID NPSYQGIWKP RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ICADRRIVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE RP.

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    Canx Human
  • View Data Sheet

    Name :

    CDC37 Human

    Description:

    Cell Division Cycle 37 Human Recombinant

    P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.

    Product # :

    PRO-464

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    Description

    CDC37 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids and having a molecular mass of 44.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    The CDC37 protein solution contains 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.

    • Synonyms

      P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.

    • 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

      MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV.

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    Cdc37 Human
  • View Data Sheet

    Name :

    TSNAX Human

    Description:

    Translin-Associated Factor X Human Recombinant

    TRAX, Translin-associated protein X, Translin-associated factor X.

    Product # :

    PRO-1292

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    Description

    TSNAX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-290 a.a.) and having a molecular mass of 35kDa.TSNAX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TSNAX protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TSNAX is a member of translin family. TSNAX particularly interacts with translin, a DNA-binding protein that binds consensus sequences at breakpoint junctions of chromosomal translocations. TSNAX works in combination with TSN as an endonuclease involves in the activation of the RNA-induced silencing complex (RISC). TSNAX has bipartite nuclear targeting sequences that afford nuclear transport for translin, which lacks any nuclear targeting motifs.

    • Synonyms

      TRAX, Translin-associated protein X, Translin-associated factor X.

    • 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 MGSMSNKEGS GGFRKRKHDN FPHNQRREGK DVNSSSPVML AFKSFQQELD ARHDKYERLV KLSRDITVES KRTIFLLHRI TSAPDMEDIL TESEIKLDGV RQKIFQVAQE LSGEDMHQFH RAITTGLQEY VEAVSFQHFI KTRSLISMDE INKQLIFTTE DNGKENKTPS SDAQDKQFGT WRLRVTPVDY LLGVADLTGE LMRMCINSVG NGDIDTPFEV SQFLRQVYDG FSFIGNTGPY EVSKKLYTLK QSLAKVENAC YALKVRGSEI PKHMLADVFS VKTEMIDQEE GIS.

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    Tsnax Human
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

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    Vaspin Human
  • View Data Sheet

    Name :

    YWHAQ Human

    Description:

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

    14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    Product # :

    PKA-254

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    Description

    YWHAQ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 27 kDa. YWHAQ is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAQ solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, ?, ?, ?, ?, ?, ? and ? that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

    • Synonyms

      14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      YWHAQ Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWRVISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLKMKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYEILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN.

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    Ywhaq Human
  • View Data Sheet

    Name :

    LGALS2 Mouse, Active

    Description:

    Galectin-2, BioActive Mouse Recombinant

    Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    Product # :

    CYT-1155

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    Description

    LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

    More Info

    • Introduction

      Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.

    • Synonyms

      Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    • 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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE

    • Background

      What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
      Escherichia Coli.

      What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
      Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

      What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

      What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
      LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
      The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE Protein was purified using conventional chromatography techniques.


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    Galectin 2 Mouse
  • View Data Sheet

    Name :

    PDIA4 Human, Active

    Description:

    Protein Disulfide Isomerase A4 Human Recombinant, Active

    Endoplasmic reticulum resident protein 72, ERP70, ERP72.

    Product # :

    ENZ-993

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    Description

    PDIA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (21-645 a.a.) and having a molecular weight of 72.9kDa. The PDIA4 is fused to 21 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDIA4 1mg/ml protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 10 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of insulin in the presence of DTT.

    More Info

    • Introduction

      PDIA4 is an endoplasmic reticulum luminal protein that is a stress protein as well as a member of the protein disulfide isomerase family of proteins. PDIA4 participates in the catalysis of protein-S-S-bond rearrangement. PDIA4 and PDIA3 function as proteases, protein disulfide isomerases, phospholipases or an arrangement of these.

    • Synonyms

      Endoplasmic reticulum resident protein 72, ERP70, ERP72.

    • 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 MVAGAEGPDE DSSNRENAIE DEEEEEEEDD DEEEDDLEVK EENGVLVLND ANFDNFVADK DTVLLEFYAP WCGHCKQFAP EYEKIANILK DKDPPIPVAK IDATSASVLA SRFDVSGYPT IKILKKGQAV DYEGSRTQEE IVAKVREVSQ PDWTPPPEVT LVLTKENFDE VVNDADIILV EFYAPWCGHC KKLAPEYEKA AKELSKRSPP IPLAKVDATA ETDLAKRFDV SGYPTLKIFR KGRPYDYNGP REKYGIVDYM IEQSGPPSKE ILTLKQVQEF LKDGDDVIII GVFKGESDPA YQQYQDAANN LREDYKFHHT FSTEIAKFLK VSQGQLVVMQ PEKFQSKYEP RSHMMDVQGS TQDSAIKDFV LKYALPLVGH RKVSNDAKRY TRRPLVVVYY SVDFSFDYRA ATQFWRSKVL EVAKDFPEYT FAIADEEDYA GEVKDLGLSE SGEDVNAAIL DESGKKFAME PEEFDSDTLR EFVTAFKKGK LKPVIKSQPV PKNNKGPVKV VVGKTFDSIV MDPKKDVLIE FYAPWCGHCK QLEPVYNSLA KKYKGQKGLV IAKMDATAND VPSDRYKVEG FPTIYFAPSG DKKNPVKFEG GDRDLEHLSK FIEEHATKLS RTKEEL.

    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.

    Pdia4 Human Active
  • View Data Sheet

    Name :

    VAMP2 Human, (1-94)

    Description:

    Synaptobrevin-2 Human Recombinant, (1-94)

    Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.

    Product # :

    PRO-2644

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    Description

    VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The VAMP2 solution (0.5mg/1ml) contains 0.1mM PMSF, 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin-2 or VAMP2 is a protein that has a proline-rich N-terminal part, highly conserved hydrophilic domain, a transmembrane anchor and a C-terminal.VAMP2 found in the transmembrane region of the cell, in the cytoplasmic surface of the synaptic vesicle. The protein is mainly found in the Langerhans islets in the pancreas and glomerular cells in the kidney. A SNARE complex is created within the protein’s N-terminal domain and the target membrane-associated T.

    • Synonyms

      Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.

    • 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 MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.

    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.

    Synaptobrevin 2 Human
  • View Data Sheet

    Name :

    OX40L Human

    Description:

    OX40 Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

    Product # :

    CYT-1226

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    Description

    OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.

    More Info

    • Synonyms

      Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

    • 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

      QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.

    • Background

      OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.

      Structural Insights into OX40L Human Recombinant:

      OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.

      Immunomodulatory Signaling Pathways:

      OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.

      Applications in Immunotherapy:

      The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.

      OX40L in Autoimmune Diseases:

      Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.

      While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.

      OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.

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    Ox40L Human
  • View Data Sheet

    Name :

    TRAIL Human (114-281 a.a.), Active

    Description:

    TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant, Active

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    Product # :

    CYT-1014

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    Description

    Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRAIL protein solution (1mg/ml) containing 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 1 ng/ml.

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
      In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
      TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • 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

      MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

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    Trail Human 114 281 Aa Active
  • View Data Sheet

    Name :

    PARK7 Antibody

    Description:

    Parkinson Disease Protein 7, Mouse Anti Human

    Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    Product # :

    ANT-317

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    Formulation

    1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.

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    • Introduction

      The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

    • Synonyms

      Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    • Immunogen

      Anti-human PARK7 mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PARK7 amino acids 1-189 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1B11AT.

    • Applications

      PARK7 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PARK7 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Park7 Antibody
  • View Data Sheet

    Name :

    Activin B Human Active

    Description:

    Activin-B Human Recombinant, Active

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-057

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

    More Info

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

    • Background

      An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active

      1. Abstract

      Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.

      2. Introduction

      The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.

      3. Structure and Synthesis of Activin-B

      Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.

      4. Biological Functions of Activin-B

      Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.

      5. Activin-B in Regenerative Medicine

      Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.

      6. Activin-B and Reproductive Health

      Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.

      7. Activin-B in Cancer

      Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.

      8. Conclusion and Future Perspectives

      Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

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

      What is the Biological Activity of Activin B Protein?
      The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

    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.

    Activin B Human Active
  • View Data Sheet

    Name :

    PSMD10 Antibody

    Description:

    Gankyrin, Mouse Anti Human

    26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

    Product # :

    ANT-609

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.

    • Synonyms

      26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PSMD10 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PSMD10 protein 1-226 amino acids purified from E.coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1F4AT.

    • Applications

      PSMD10 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PSMD10 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Psmd10 Antibody
  • View Data Sheet

    Name :

    CJC-1295 DAC

    Description:

    CJC-1295 DAC

    Product # :

    HOR-065

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    Description

    CJC-1295 DAC is a synthetic single, non-glycosylated polypeptide chain containing 30 amino acids, having a molecular mass of 3647.18 Dalton and a Molecular formula of C165H269N47O46.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CJC-1295 DAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CJC-1295 DAC 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 CJC-1295 DAC in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-D-Ala-Asp-Ala-Ile-PheThr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-LeuLeu-Gln-Asp-Ile-Leu-Ser-Arg-Lys(Mal)-NH2.

    • Background

      CJC-1295 DAC owns a Drug Affinity Complex (DAC), which allows it to bind to serum albumin, extending its half-life to 6–8 days. CJC-1295 DAC normalizes growth and metabolism while maintaining natural hormone pulsatility.

    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.

    CJC-1295-DAC
  • View Data Sheet

    Name :

    NPPC Human

    Description:

    Natriuretic Peptide C Human Recombinant

    Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    Product # :

    CYT-760

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    Description

    NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.

    • Synonyms

      Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    • 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 MGSKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS MSGLGC

    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.

    Nppc Human
  • View Data Sheet

    Name :

    NCL Human

    Description:

    Nucleolin Human Recombinant

    Nucleolin, Protein C23, NCL, C23.

    Product # :

    PRO-1508

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    • description
    • source
    • formulation
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    Description

    Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.

    • Synonyms

      Nucleolin, Protein C23, NCL, C23.

    • 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.

    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.

    Ncl Human
  • View Data Sheet

    Name :

    MAPK3 Human, Active

    Description:

    Mitogen-Activated Protein Kinase 3 Human Recombinant, Active

    Mitogen-activated protein kinase 3, EC 2.7.11.24, Extracellular signal-regulated kinase 1, ERK-1, Insulin-stimulated MAP2 kinase, MAP kinase 1, MAPK 1, p44-ERK1, ERT2, p44-MAPK, Microtubule-associated protein 2 kinase, ERK1, PRKM3, P44ERK1, P44MAPK, HS44KDAP, HUMKER1A, MGC20180.

    Product # :

    PKA-212

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    Description

    ERK1/MAPK3 Recombinant is a highly active form produced by phosphorylation of the purified ERK1/MAPK3 in vitro with MEK1 is a non-glycosylated polypeptide having a molecular mass of 43.6 kDa. ERK1/MAPK3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ERK1/MAPK3 is supplied as 0.15mg/ml containing 50mM Tris-HCl, 150mM NaCl, 1mM DTT, 50% glycerol, pH 8.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinaseintracellular signalingmolecules which are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virusinfection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.
      The term, "extracellular signal-regulated kinases", is sometimes used as a synonym for mitogen-activated protein kinase(MAPK), but has more recently been adopted for a specific subset of the mammalianMAPK family. In the MAPK/ERK pathway, Rasactivates c-Raf, followed by MEKand then MAPK1/2 (below). Ras is typically activated by growth hormones through receptor tyrosine kinasesand GRB2/SOS, but may also receive other signals. ERKs are known to activate many transcription factors and some downstream protein kinases. Disruption of the ERK pathway is common in cancers, especially Ras, c-Raf and receptors such as HER2.Mitogen-activated protein kinase 3 (MAPK3) is also known as "extracellular signal-regulated kinase 1" (ERK1). Transgenic gene knockoutmice lacking MAPK3 are viable and it is thought that MAPK1 can fulfill most MAPK3 functions in most cells. The main exception is in T cells. Mice lacking MAPK3 have reduced T cell development past the CD4+CD8+ stage.

    • Synonyms

      Mitogen-activated protein kinase 3, EC 2.7.11.24, Extracellular signal-regulated kinase 1, ERK-1, Insulin-stimulated MAP2 kinase, MAP kinase 1, MAPK 1, p44-ERK1, ERT2, p44-MAPK, Microtubule-associated protein 2 kinase, ERK1, PRKM3, P44ERK1, P44MAPK, HS44KDAP, HUMKER1A, MGC20180.

    • 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.

    • Unit Definition

      No protease activity detectable, specific activity > 15.000 U*/mg (*1 U = 1 pmol/min transferred to myelin basic protein at 30 degree C).

    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.

    Erk1 Human Active Enzyme
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