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Search results

625 results found for “otoraplin”

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  • View Data Sheet

    Name :

    POP7 Human

    Description:

    Processing Of Precursor 7 Human Recombinant

    Ribonuclease P protein subunit p20, RNaseP protein p20, Ribonucleases P/MRP protein subunit POP7 homolog, hPOP7, POP7, RPP20, 0610037N12Rik, RPP2.

    Product # :

    PRO-2015

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    Description

    POP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-140 a.a.) and having a molecular mass of 18.3kDa.POP7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Processing Of Precursor 7, also known as POP7, is a part of the histone-like Alba family. POP7 is a part of ribonuclease P which is a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. POP7 is also a part of RNase MRP complex, which cleaves pre-rRNA sequences.

    • Synonyms

      Ribonuclease P protein subunit p20, RNaseP protein p20, Ribonucleases P/MRP protein subunit POP7 homolog, hPOP7, POP7, RPP20, 0610037N12Rik, RPP2.

    • 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 MGSEFMAENR EPRGAVEAEL DPVEYTLRKR LPSRLPRRPN DIYVNMKTDF KAQLARCQKL LDGGARGQNA CSEIYIHGLG LAINRAINIA LQLQAGSFGS LQVAANTSTV ELVDELEPET DTREPLTRIR NNSAIHIRVF RVTPK.

    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.

    Pop7 Human
  • View Data Sheet

    Name :

    TRAIL Mouse

    Description:

    TNF-Related Apoptosis Inducing Ligand/Apo2L Mouse Recombinant

    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-806

    Price :

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    Description

    TRAIL Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.2kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized containing PBS, pH 7.4, and 3mM DTT.

    Purity

    Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2,000,000 IU/mg in the presence of actinomycin D.

    Citations

    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 White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TRAIL although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TRAIL recombinant should be stored at 4C between 2-7 days and for future use below -18C.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 TRAIL Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPRGGRPQKV AAHITGITRR SNSALIPISK DGKTLGQKIE SWESSRKGHS FLNHVLFRNG ELVIEQEGLY YIYSQTYFRF QEAEDASKMV SKDKVRTKQL VQYIYKYTSY PDPIVLMKSA RNSCWSRDAE YGLYSIYQGG LFELKKNDRI FVSVTNEHLM DLDQEASFFG AFLIN

    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.

    Trail Mouse
  • View Data Sheet

    Name :

    LTF Holo Human

    Description:

    Lactoferrin Holo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-592

    Price :

    Quantity :

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    Description

    Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Holo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Lactoferrin Holo Human
  • View Data Sheet

    Name :

    EPO Mouse

    Description:

    Erythropoietin Mouse Recombinant

    Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    Product # :

    CYT-1171

    Price :

    Quantity :

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    • sds-page
    • Citations

    Description

    EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPO Mouse protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

    sds-page

    EPO-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

    • Synonyms

      Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    • 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

      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

    • Background

      What is the molecular weight/Mw of EPO Protein?
      EPO Protein has a total Mw of 19.8kDa.

      What is the source or expression system of EPO Protein?
      Sf9, Baculovirus cells.

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

      What is the Biological Activity of EPO Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

      What is the amino acid sequence of EPO Protein?
      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

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

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

    Epo Mouse
  • View Data Sheet

    Name :

    TANK Human

    Description:

    TRAF Family Member-Associated NFKB Activator Human Recombinant

    TRAF, TRAF2, TRAF-interacting protein, ITRAF.

    Product # :

    PRO-1348

    Price :

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    • Citations

    Description

    TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.

    • Synonyms

      TRAF, TRAF2, TRAF-interacting protein, ITRAF.

    • 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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.

    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.

    Tank Human
  • View Data Sheet

    Name :

    Adiponectin Mouse, Trimeric

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

    Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Name :

    DLL4 Mouse

    Description:

    Delta-Like 4 Mouse Recombinant

    Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.

    Product # :

    PRO-2236

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    Description

    DLL4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-532 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 512 amino acids and having a molecular mass of 55.8kDa.DLL4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DLL4 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Delta-Like4, also known as DLL4 is implicated in the Notch signaling pathway as Notch ligand. Consequently DLL4 negatively regulates endothelial cell proliferation, migration as well as angiogenic sprouting. DLL4 is vital for retinal progenitor proliferation and also required for suppressing rod fates in late retinal progenitors and for proper generation of other retinal cell types. Furthermore, at some stage in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.

    • Synonyms

      Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.

    • 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

      GSGIFQLRLQ EFVNQRGMLA NGQSCEPGCR TFFRICLKHF QATFSEGPCT FGNVSTPVLG TNSFVVRDKN SGSGRNPLQL PFNFTWPGTF SLNIQAWHTP GDDLRPETSP GNSLISQIII QGSLAVGKIW RTDEQNDTLT RLSYSYRVIC SDNYYGESCS RLCKKRDDHF GHYECQPDGS LSCLPGWTGK YCDQPICLSG CHEQNGYCSK PDECICRPGW QGRLCNECIP HNGCRHGTCS IPWQCACDEG WGGLFCDQDL NYCTHHSPCK NGSTCSNSGP KGYTCTCLPG YTGEHCELGL SKCASNPCRN GGSCKDQENS YHCLCPPGYY GQHCEHSTLT CADSPCFNGG SCRERNQGSS YACECPPNFT GSNCEKKVDR CTSNPCANGG QCQNRGPSRT CRCRPGFTGT HCELHISDCA RSPCAHGGTC HDLENGPVCT CPAGFSGRRC EVRITHDACA SGPCFNGATC YTGLSPNNFV CNCPYGFVGS RCEFPVGLPP SFPWVAHHHH 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.

    Dll4 Mouse
  • View Data Sheet

    Name :

    ATXN3 Human

    Description:

    Ataxin-3 Human Recombinant

    Ataxin-3, Machado-Joseph disease protein 1, Spinocerebellar ataxia type 3 protein, ATXN3, ATX3, MJD, MJD1, SCA3, AT3, JOS.

    Product # :

    PRO-708

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    Description

    ATXN3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (1-370 a.a.) and having a molecular mass of 42.4kDa.ATXN3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATXN3 protein solution contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ataxin 3 is otherwise known as Machado-Joseph disease protein 1. Machado–Joseph disease is a hereditary autosomal dominant neurodegenerative disorder. ATXN3 contains trinucleotide CAG repeats in the coding region, and the expansion of these repeats from the normal 13-36 to 68-79 causes the Machado-Joseph disease. ATXN3 is a poly-ubiquitin-binding protein whose cellular turnover is regulated by its catalytic activity.
      In addition, ATXN3 is a proteasome-associated factor which mediates the degradation of ubiquitinated proteins. ATXN3 folds reversibly using a single intermediate; partial destabilization of ATXN3 by chemical denaturation causes the formation of fibrillar aggregates by the non-pathological variant.
      Ataxin-3 interacts with the major histone acetyltransferases cAMP-response-element binding protein (CREB)-binding protein, p300, and p300/CREB-binding protein-associated factor and hinders transcription by these coactivators.

    • Synonyms

      Ataxin-3, Machado-Joseph disease protein 1, Spinocerebellar ataxia type 3 protein, ATXN3, ATX3, MJD, MJD1, SCA3, AT3, JOS.

    • 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

      MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLELILFNSPEYQ RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ QQQQQQQQQQ QQQQGDLSGQ SSHPCERPAT SSGALGSDLG DAMSEEDMLQ AAVTMSLETV RNDLKTEGKK.

    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.

    Atxn3 Human
  • View Data Sheet

    Name :

    NUP210 Human

    Description:

    Nucleopurin 210kDa Recombinant Human

    Nucleoporin 210kDa, KIAA0906, GP210, Nuclear envelope pore membrane protein POM 210, Nuclear pore protein gp210, nuclear pore membrane glycoprotein 210.

    Product # :

    PRO-109

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    Description

    Recombinant NUP210 protein is a construct carrying multiple concatenated copies of the short cytoplasmic gp210 C-terminus (which contains the autoreactive epitopes) and having a molecular mass of 27kDa (pH 9.8). NUP210 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    NUP210 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The NUP210 complex is a immense structure which spreads through the nuclear envelope, forming a doorway which regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the core components of the nuclear pore complex in eukaryotic cells. NUP210 is a membrane-spanning glycoprotein and is a major component of the nuclear pore complex.

    • Synonyms

      Nucleoporin 210kDa, KIAA0906, GP210, Nuclear envelope pore membrane protein POM 210, Nuclear pore protein gp210, nuclear pore membrane glycoprotein 210.

    • 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 IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test.

    • coating concentration

      0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with PBC sera or monoclonal anti-hexa-His-tag antibody.

    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.

    Nup210 Human
  • View Data Sheet

    Name :

    IL11 Mouse

    Description:

    Interleukin-11 Mouse Recombinant

    AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    Product # :

    CYT-646

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    Description

    Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

    Citations

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.

    • Background

      What is the molecular weight/Mw of IL11 MOUSE Protein?
      IL11 MOUSE Protein has a total Mw of 19.1kDa.

      What is the source or expression system of IL11 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL11 MOUSE Protein?
      IL11 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL11 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

      What is the amino acid sequence of IL11 MOUSE Protein?
      MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.
      What applications can IL11 MOUSE Protein be used in?
      IL11 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL11 MOUSE Protein?
      The endotoxin level is minimal, IL11 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL11 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL11 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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 11 Mouse
  • View Data Sheet

    Name :

    IL12p40 Human

    Description:

    Interleukin-12 p40 Human Recombinant

    NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    Product # :

    CYT-488

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    Description

    Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.

    • Synonyms

      NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 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. Please avoid freeze thaw cycles.

    • Background

      What is the source or expression system of IL12P40 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL12P40 HUMAN Protein?
      IL12P40 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12P40 HUMAN Protein?
      The biological functionality of IL12P40 HUMAN Protein will be determined in the future.

      What applications can IL12P40 HUMAN Protein be used in?
      IL12P40 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12P40 HUMAN Protein?
      The endotoxin level is minimal, IL12P40 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12P40 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12P40 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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 12 P40 Human His
  • View Data Sheet

    Name :

    Borrelia Spielmanii DbpA

    Description:

    Borrelia Spielmanii Decorin Binding Protein A Recombinant

    Product # :

    BOR-026

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    Description

    Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa. Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

    • 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 IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Spielmanii Dbpa
  • View Data Sheet

    Name :

    IL36RN Mouse

    Description:

    Interleukin-36 Receptor Antagonist Mouse Recombinant

    Product # :

    CYT-154

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    Description

    IL36RN Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.0kDa.The IL36RN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Measured by its ability to inhibit IL-36a, IL-36b or IL-36g induced IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 0.8-4ug/ml (corresponding to a specific activity of 250-125units/mg) in the presence of 15ng/ml of recombinant mouse IL-36b.

    Citations

    More Info

    • Introduction

      IL36RA belongs to the IL-1 family of proteins. IL36RA is produced as a 156 aa protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation site but, IL36RA is secreted as a 17 kDa monomer. Cells known to express IL36Ra/IL1F5 include monocytes, B cells, keratinocytes, dendritic cells/Langerhans cells and gastric fundus Parietal and Chief cells.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 36RN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 36RN should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL36RN in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAEKVIKGEE ISVVPNRALD ASLSPVILGV QGGSQCLSCG TEKGPILKLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTSPEADQPV RLTQIPEDPA WDAPITDFYF QQCD

    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.

    Il36Ra Mouse
  • View Data Sheet

    Name :

    Clusterin Canine

    Description:

    Clusterin Canine Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-549

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    • More Info
    • sds-page
    • Citations

    Description

    Apolipoprotein-J canine Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain (Asn227~Glu445) and having a molecular mass of 30 kDa.
    The protein is fused to His tag at N-Terminus.
    The Apolipoprotein-J canine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Canine Clusterin was lyophilized from 20mM Tris, 150mM NaCl, pH8.0, 0.01% skl and 5%Trehalose.

    Purity

    Greater than 90% as determined by SDS PAGE.

    sds-page

    Clusterin Canine sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Reconstitute in 20mM Tris and 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 30kDa.

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

      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.

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

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

    Clusterin Canine
  • View Data Sheet

    Name :

    Clusterin Human

    Description:

    Clusterin Human Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-278

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    Description

    Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.

    Source

    293 cell line (Human embryonic kidney).

    Formulation

    Filtered (0.4 micron) and lyophilized PBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered, White, Lyophilized powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.

    • Amino Acid Sequence

      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 51.27kDa.

      What is the source or expression system of CLUSTERIN Protein?
      293 cell line
      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

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

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

    Clusterin Human Recombinant
  • View Data Sheet

    Name :

    PTH (1-84) N15 Human

    Description:

    Parathyroid Hormone (1-84) N15 Labeled Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-002

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    Description

    PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.The PTH (1-84) N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTH (1-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 9,000 Units/mg.

    Citations

    More Info

    • Introduction

      Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
      In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
      In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
      Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.

    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.

    Pth 1 84 N15 Human
  • View Data Sheet

    Name :

    CABP7 Human

    Description:

    Calcium Binding Protein 7 Human Recombinant

    Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.

    Product # :

    PRO-211

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    Description

    CABP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188 a.a.) and having a molecular mass of 23.7kDa.CABP7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CABP7 protein solution (0.5mg/ml) containing Phosphate-buffered saline (pH 7.4).

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calcium-binding protein 7 (CABP7) contains 2 EF-hand domains. CABP7 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. The CaBP family of EF-hand containing small Ca (2+)-binding proteins has lately emerged as significant regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system.

    • Synonyms

      Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CABP7 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPFHPVTAAL MYRGIYTVPN LLSEQRPVDI PEDELEEIRE AFKVFDRDGN GFISKQELGT AMRSLGYMPN EVELEVIIQR LDMDGDGQVD FEEFVTLLGP KLSTSGIPEK FHGTDFDTVF WKCDMQKLTV DELKRLLYDT FCEHLSMKDI ENIIMTEEES HLGTAEECPV DVETCSNQQI RQTCVRKS.

    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.

    Cabp7 Human
  • View Data Sheet

    Name :

    Prolactin Ovine Antagonist, Mutant

    Description:

    Prolactin Antagonist Ovine Recombinant, Mutant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL, Prolactin.

    Product # :

    CYT-705

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    Description

    Prolactin Ovine Antagonist Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and an additional Ala at N-terminus and having a molecular mass of 23kDa. The mutant R129G is DES 9 amino acids truncated form from its N-terminus which has higher inhibitory activity. Ovine Prolactin Antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Ovine Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02%-0.03% NaHCO3.

    Purity

    Greater than 99.0% as determined by Gel Filtration & SDS-PAGE.

    Biological Activity

    Ovine Prolactin Antagonist mutant form is devoid of agonistic activity and capable of inhibiting biological activity of oPRL or other lactogenic hormones as evidenced by proliferation assay of Nb2 or other cells. The truncated form is more potent inhibitor.

    Citations

    More Info

    • Introduction

      Prolactin is a lactogenic hormone secreted by the adenohypophysis .Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation.Prolactin has been shown also to have cytokine-like activities and to have important immunoregulatory activities. It contributes to the development of lymphoid tissues and the maintenance of physiological immune function and also modulates a variety of T-cell immune responses. Prolactin has been reported to activate cellular proliferation in nonreproductive tissue, such as liver, spleen, and thymus. It induces significant proliferation in aortic smooth muscle cells and also enhances proliferation of these cells induced by PDGF . Prolactin also appears to be directly mitogenic for pancreatic beta cells. Prolactin is also mitogenic for cultured astrocytes.

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL, Prolactin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro.

    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.

    Prolactin Antagonist Ovine Mutant
  • View Data Sheet

    Name :

    Thymopentin

    Description:

    Thymopentin

    Product # :

    HOR-241

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    Description

    Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

    Citations

    More Info

    • Introduction

      Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Thymopentin
  • View Data Sheet

    Name :

    Betacellulin Human

    Description:

    Betacellulin Human Recombinant

    Product # :

    CYT-330

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    Description

    Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

    • Background

      Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine

      Introduction

      In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.

      BTC: The Architect of Cellular Revitalization

      BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.

      Crafting the Alchemist: Pioneering Methodologies

      Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.

      Unveiling the Biological Tapestry

      Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.

      A Flourish of Results

      The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.

      Charting a Transformative Future

      As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.

      What is the molecular weight/Mw of BTC Protein?
      BTC Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BTC Protein?
      The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

      What is the amino acid sequence of BTC Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

    Betacellulin Human
  • View Data Sheet

    Name :

    SPOP Human

    Description:

    Speckle-Type POZ Protein Human Recombinant

    Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    Product # :

    PRO-195

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    Description

    SPOP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.

    • Synonyms

      Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    • Physical Appearance

      SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
      VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

    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.

    Spop Human
  • View Data Sheet

    Name :

    IL33 Mouse, His

    Description:

    Interleukin-33 Mouse Recombinant, His Tag

    9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.

    Product # :

    CYT-847

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    IL33 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (109-266 a.a) and having a molecular mass of 18.1kDa.IL33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL33 protein solution (0.5mg/ml) containing Phosphate buffered saline,10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ 0.1ng/ml.

    Citations

    More Info

    • Introduction

      Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.

    • 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 MGSSIQGTSL LTQSPASLST YNDQSVSFVL ENGCYVINVD DSGKDQEQDQ VLLRYYESPC PASQSGDGVD GKKLMVNMSP IKDTDIWLHA NDKDYSVELQ RGDVSPPEQA FFVLHKKSSD FVSFECKNLP GTYIGVKDNQ LALVEEKDES CNNIMFKLSK I.

    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.

    Il33 Mouse His
  • View Data Sheet

    Name :

    IL36A Mouse

    Description:

    Interleukin-36 Alpha Mouse Recombinant

    Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    Product # :

    CYT-162

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 21.0kDa.The IL36A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA to bind recombinant mouse IL-1 Rrp2.

    Citations

    More Info

    • Introduction

      Murine IL-36a belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
      Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.

    • Synonyms

      Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36A Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL36A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH

    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.

    Il36A Mouse
  • View Data Sheet

    Name :

    TPM4 Human

    Description:

    Tropomyosin-4 Human Recombinant

    Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.

    Product # :

    PRO-187

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
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    • Citations

    Description

    TPM4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248 a.a.) and having a molecular mass of 30.7kDa.TPM4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPM4 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TPM4 is a member of the tropomyosin family. Tropomyosins exist in practically all eukaryotic cells (both muscle and nonmuscle), where they bind actin filaments and function to modulate actin-myosin interaction and stabilize actin filament structure. TPM4 binds to actin filaments in muscle and nonmuscle cells and plays a central role, in connection with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction.

    • Synonyms

      Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.

    • 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 MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI.

    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.

    Tpm4 Human
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