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Search results

910 results found for “cellular retinoic acid binding protein”

Name

Description

Product #

Price

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  • View Data Sheet

    Name :

    KRT18 Human

    Description:

    Cytokeratin 18 Human Recombinant

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-349

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    Description

    Cytokeratin 18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 48,201 Dalton, showing a 45kDa band on SDS-page, pI-5.7.The KRT18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CK-18 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Upon reconstitution CK-18 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 1mg CK-18 in sterile 18MΩ-cm H2O not less than 700µl, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    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.

    Krt18 Human
  • View Data Sheet

    Name :

    DYNLT3 Human

    Description:

    Dynein, Light Chain, Tctex-Type 3 Human Recombinant

    Dynein light chain Tctex-type 3, t-complex-associated-testis-expressed 1-like, TCTE1XL, Protein 91/23, TCTEX1L, TCTE1L, RP3.

    Product # :

    PRO-1197

    Price :

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    Description

    DYNLT3 Human Recombinant produced in E. coli is a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.5 kDa.DYNLT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DYNLT3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      DYNLT3 belongs to a subclass of dynein light chains. The DYNLT3 protein homodimerizes and forms the light chain component of the cytoplasmic dynein motor protein complex. DYNLT3 functions as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex which are believed to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. DYNLT3 may also work independently of dynein as a transcriptional modulator. DYNLT3 is required for the effective progression through mitosis.

    • Synonyms

      Dynein light chain Tctex-type 3, t-complex-associated-testis-expressed 1-like, TCTE1XL, Protein 91/23, TCTEX1L, TCTE1L, RP3.

    • 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 MGSMEEYHRH CDEVGFNAEE AHNIVKECVD GVLGGEDYNH NNINQWTASI VEQSLTHLVK LGKAYKYIVT CAVVQKSAYG FHTASSCFWD TTSDGTCTVR WENRTMNCIV NVFAIAIVL

    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.

    Dynlt3 Human
  • View Data Sheet

    Name :

    SIRT3 Human

    Description:

    Sirtuin 3 Human Recombinant

    Sirtuin 3, SIR2-like protein 3, Sir2-like 3, NAD-dependent deacetylase sirtuin-3, mitochondrial.

    Product # :

    PRO-462

    Price :

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    Description

    SIRT3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (118-399a.a.) and having a molecular mass of 33.5kDa.SIRT3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SIRT3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 0.1M NaCl, 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SIRT3 is a member of a family of proteins called Sirtuin. Proteins of the Sirtuin family are characterized by a Sirtuin core domain and grouped into four classes. The roles of human Sirtuins are numerous and are important in aging prosseses, stress resistance and metabolic regulation. SIRT3 shows NAD+-dependent deacetylase activity in the mitochondria. Over-expression of SIRT3 causes increased levels of the mitochondrial uncoupling protein 1. Also, in certain breast cancers the levels of SIRT3 protein are found to be extremely high.

    • Synonyms

      Sirtuin 3, SIR2-like protein 3, Sir2-like 3, NAD-dependent deacetylase sirtuin-3, mitochondrial.

    • 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 MSDKGKLSLQ DVAELIRARA CQRVVVMVGA GISTPSGIPD FRSPGSGLYS NLQQYDLPYP EAIFELPFFF
      HNPKPFFTLA KELYPGNYKP NVTHYFLRLL HDKGLLLRLY TQNIDGLERV SGIPASKLVE AHGTFASATC TVCQRPFPGE DIRADVMADR
      VPRCPVCTGV VKPDIVFFGE PLPQRFLLHV VDFPMADLLL ILGTSLEVEP FASLTEAVRS SVPRLLINRD LVGPLAWHPR SRDVAQLGDV
      VHGVESLVEL LGWTEEMRDL VQRETGKLDG PDK.

    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.

    Sirt3 Human
  • View Data Sheet

    Name :

    CYTH1 Human

    Description:

    Cytohesin 1 Human Recombinant

    Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-1.

    Product # :

    PRO-2215

    Price :

    Quantity :

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    Description

    CYTH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-398 a.a) and having a molecular mass of 48.8kDa. CYTH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CYTH1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytohesin 1 also known as CYTH1 belongs to the PSCD family. CYTH1 is responsible for promoting guanine-nucleotide exchange on ARF1 and ARF5 and also promotes the activation of ARF factors by the replacement of GDP with GTP.

    • Synonyms

      Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEEDDSY VPSDLTAEER QELENIRRRK QELLADIQRL KDEIAEVANE IENLGSTEER KNMQRNKQVA MGRKKFNMDP KKGIQFLIEN DLLKNTCEDI AQFLYKGEGL NKTAIGDYLG ERDEFNIQVL HAFVELHEFT DLNLVQALRQ FLWSFRLPGE AQKIDRMMEA FAQRYCQCNN GVFQSTDTCY VLSFAIIMLN TSLHNPNVKD KPTVERFIAM NRGINDGGDL PEELLRNLYE SIKNEPFKIP EDDGNDLTHT FFNPDREGWL LKLGGGRVKT WKRRWFILTD NCLYYFEYTT DKEPRGIIPL ENLSIREVED SKKPNCFELY IPDNKDQVIK ACKTEADGRV VEGNHTVYRI SAPTPEEKEE WIKCIKAAIS RDPFYEMLAA RKKKVSSTKR H.

    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.

    Cyth1 Human
  • View Data Sheet

    Name :

    SARS MERS RBD

    Description:

    SARS MERS Spike Receptor Binding Domain Recombinant

    Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

    Product # :

    SARS-054

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    Description

    SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa.SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SARS MERS RBD solution (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

    • Synonyms

      Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer 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

      ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH

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  • View Data Sheet

    Name :

    SIRT2 Human

    Description:

    Sirtuin 2 Human Recombinant

    Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 2.

    Product # :

    PRO-033

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    Description

    SIRT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352a.a.) and having a molecular mass of 41.7kDa.SIRT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SIRT2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 2mM DTT, 200mM NaCl, 0.5mM EDTA and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SIRT2 belongs to the sirtuin family of proteins, homologs to the yeast Sir2 protein. Proteins of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes and take part in various processes, including transcriptional regulation, cell cycle progression, DNA-damage repair and aging. SIRT2 is a NAD-dependent deacetylase, which deacetylates the 'Lys-40' of alpha-tubulin.

    • Synonyms

      Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDFLRNLFSQ TLSLGSQKER LLDELTLEGV ARYMQSERCR RVICLVGAGI STSAGIPDFR SPSTGLYDNL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFMRLLKD KGLLLRCYTQ NIDTLERIAG LEQEDLVEAH GTFYTSHCVS ASCRHEYPLS WMKEKIFSEV TPKCEDCQSL VKPDIVFFGE SLPARFFSCM QSDFLKVDLL LVMGTSLQVQ PFASLISKAP LSTPRLLINK EKAGQSDPFL GMIMGLGGGM DFDSKKAYRD VAWLGECDQG CLALAELLGW KKELEDLVRR EHASIDAQSG AGVPNPSTSA SPKKSPPPAK DEARTTEREK PQ

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    Sirt2 Human
  • View Data Sheet

    Name :

    WWC1 Human

    Description:

    WW And C2 Domain Containing 1 Human Recombinant

    WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.

    Product # :

    PRO-1863

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    Description

    WWC1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 152 amino acids (655-783) and having a molecular mass of 17kDa. WWC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWC1 solution (0.25mg/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

      WW and C2 Domain Containing 1 (WWC1) is a cytoplasmic phosphoprotein which interacts with PRKC-zeta and dynein light chain-1. WWC1 takes part in cognition and memory performance. In some individuals, alleles of WWC1 have enhanced memory.

    • Synonyms

      WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.

    • 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 MGSEAVGATR IQIALKYDEK NKQFAILIIQ LSNLSALLQQ QDQKVNIRVA VLPCSESTTC LFRTRPLDAS DTLVFNEVFW VSMSYPALHQ KTLRVDVCTT DRSHLEECLG GAQISLAEVC RSGERSTRWY NL.

    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.

    Wwc1 Human
  • View Data Sheet

    Name :

    CLEC10A Human

    Description:

    C-Type Lectin Domain Family 10, Member A Human Recombinant

    C-Type Lectin Domain Containing 10A, C-Type Lectin Domain Family 10 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 14 (Macrophage-Derived), Macrophage Lectin 2 (Calcium Dependent), CLECSF13, CLECSF14, HML, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 13 (Macrophage-Derived), C-Type Lectin Domain Family 10, Member A, C-Type Lectin Superfamily Member 14, Macrophage Lectin 2, CD301 Antigen, CD301, HML2, MGL.

    Product # :

    PRO-2425

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    Description

    CLEC10A Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 241 amino acids (61-292a.a.) and having a molecular mass of 27.3kDa. (Molecular size on SDS-PAGE under reducing conditions 28-40kDa).CLEC10A is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CLEC10A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-Type Lectin Domain Family 10, Member A (CLEC10A) is a part of the C-type lectin superfamily. CLEC10A is expressed in immature myeloid dendritic cells and alternatively activated macrophages. CLEC10A takes part in regulating adaptive and innate immune responses and also binds in a calcium dependent way to terminal galactose and N-acetylgalactosamine, linked to serine or threonine.

    • Synonyms

      C-Type Lectin Domain Containing 10A, C-Type Lectin Domain Family 10 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 14 (Macrophage-Derived), Macrophage Lectin 2 (Calcium Dependent), CLECSF13, CLECSF14, HML, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 13 (Macrophage-Derived), C-Type Lectin Domain Family 10, Member A, C-Type Lectin Superfamily Member 14, Macrophage Lectin 2, CD301 Antigen, CD301, HML2, MGL.

    • 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

      ADPQNSKFQR DLVTLRTDFS NFTSNTVAEI QALTSQGSSL EETIASLKAE VEGFKQERQA VHSEMLLRVQ QLVQDLKKLT CQVATLNNNG EEASTEGTCC PVNWVEHQDS CYWFSHSGMS WAEAEKYCQL KNAHLVVINS REEQNFVQKY LGSAYTWMGL SDPEGAWKWV DGTDYATGFQ NWKPGQPDDW QGHGLGGGED CAHFHPDGRW NDDVCQRPYH WVCEAGLGQT SQESHHHHHH H.

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    Clec10A Human
  • View Data Sheet

    Name :

    RSPO3 Human

    Description:

    R-Spondin-3 Human Recombinant

    R-spondin-3, Protein with TSP type-1 repeat, hPWTSR, Roof plate-specific spondin-3, hRspo3, Thrombospondin type-1 domain-containing protein 2, RSPO3, PWTSR, THSD2, THSD2, CRISTIN1.

    Product # :

    PRO-1646

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    Description

    Recombinant Human R-Spondin-3 produced in HEK293 cells is a polypeptide chain starting at amino acid Gln at position 22 to amino acid Val at position 201, fused to an FC, 6 x His-tag at C-terminus, containing a total of 498 amino acids and having a Mw of 47.9 kDa. The protein migrates at 61kDa on SDS-PAGE. RSPO3 is a truncated protein that lacks amino acid Gln at position 201 to amino acid H at position 272 and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    RSPO3 was lyophilized from a 0.2µm filtered solution in 20mM PB, and 150mM NaCl pH-7.2.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      R-spondin-3 (RSPO3) belongs to the thrombospondin type 1 repeat supergene family. RSPO3 is a secreted protein which is widely expressed in many tissues. RSPO3 contains 2 Furin-like repeats which have been found in various eukaryotic proteins involved in the mechanism of signal transduction by receptor tyrosine kinases, and one TSP type-1 domain. RSPO3 acts as an activator of the beta-catenin signaling cascade, initiating TCF-dependent gene activation.

    • Synonyms

      R-spondin-3, Protein with TSP type-1 repeat, hPWTSR, Roof plate-specific spondin-3, hRspo3, Thrombospondin type-1 domain-containing protein 2, RSPO3, PWTSR, THSD2, THSD2, CRISTIN1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RSPO3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RSPO3 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 quick spin followed by reconstitution of RSPO3 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QNASRGRRQR RMHPNVSQGC QGGCATCSDY NGCLSCKPRL FFALERIGMK QIGVCLSSCP SGYYGTRYPD INKCTKCKAD CDTCFNKNFC TKCKSGFYLH LGKCLDNCPE GLEANNHTME CVSIVHCEVS EWNPWSPCTK KGKTCGFKRG TETRVREIIQ HPSAKGNLCP PTNETRKCTV DDIEGRMDEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSREE MTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

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    Rspo3 Human
  • View Data Sheet

    Name :

    CCBL1 Human

    Description:

    Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant

    Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.

    Product # :

    ENZ-878

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    Description

    CCBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-422 a.a) and having a molecular mass of 50.3kDa. CCBL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCBL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cysteine Conjugate-Beta Lyase Cytoplasmic also known as CCBL1 is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family. CCBL1 catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) it also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Furthermore, CCBL1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno) cysteine, resulting in the cleavage of the C-S or C-Se bond.

    • Synonyms

      Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAKQLQA RRLDGIDYNP WVEFVKLASE HDVVNLGQGF PDFPPPDFAV EAFQHAVSGD FMLNQYTKTF GYPPLTKILA SFFGELLGQE IDPLRNVLVT VGGYGALFTA FQALVDEGDE VIIIEPFFDC YEPMTMMAGG RPVFVSLKPG PIQNGELGSS SNWQLDPMEL AGKFTSRTKA LVLNTPNNPL GKVFSREELE LVASLCQQHD VVCITDEVYQ WMVYDGHQHI SIASLPGMWE RTLTIGSAGK TFSATGWKVG WVLGPDHIMK HLRTVHQNSV FHCPTQSQAA VAESFEREQL LFRQPSSYFV QFPQAMQRCR DHMIRSLQSV GLKPIIPQGS YFLITDISDF KRKMPDLPGA VDEPYDRRFV KWMIKNKGLV AIPVSIFYSV PHQKHFDHYI RFCFVKDEAT LQAMDEKLRK WKVEL.

    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.

    Ccbl1 Human
  • View Data Sheet

    Name :

    LYVE1 Antibody

    Description:

    Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1, Mouse Anti Human

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

    Product # :

    ANT-322

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    • More Info

    Formulation

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

    More Info

    • Introduction

      LYVE-1 has been identified as a major receptor for HA (extracellular matrix glycosaminoglycan hyaluronan) on the lymph vessel wall. The deduced amino acid sequence of LYVE-1 predicts a 322-residue type I integral membrane polypeptide 41% similar to the CD44 HA receptor with a 212-residue extracellular domain containing a single Link module the prototypic HA binding domain of the Link protein superfamily. Like CD44, the LYVE-1 molecule binds both soluble and immobilized HA. However, unlike CD44, the LYVE-1 molecule colocalizes with HA on the luminal face of the lymph vessel wall and is completely absent from blood vessels. Hence, LYVE-1 is the first lymph-specific HA receptor to be characterized and is a uniquely powerful marker for lymph vessels themselves.

    • Synonyms

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

    • Immunogen

      Anti-human LYVE1 mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LYVE1 amino acids 25-235 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P4G1AT.

    • Applications

      LYVE1 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 ~ 1,000. 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

      LYVE1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Lyve1 Antibody
  • View Data Sheet

    Name :

    GHBP Human

    Description:

    GHBP Human Recombinant

    Product # :

    CYT-238

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    Description

    GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton. GHR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GHBP was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    GHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with G.H.

    More Info

    • Introduction

      GHBP is a transmembrane receptor for GH. Binding of GH to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the GH insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AFSGSEATAAILSRAPWSLQSVNPGLKTNS SKEPKFTKCRSPERETFSCHWTDEVHHGTK
      NLGPIQLFYTRRNTQEWTQEWKECPDYVSA GENSCYFNSSFTSIWIPYCIKLTSNGGTVD
      EKCFSVDEIVQPDPPIALNWTLLNVSLTGI HADIQVRWEAPRNADIQKGWMVLEYELQYK
      EVNETKWKMMDPILTTSVPVYSLKVDKEYE VRVRSKQRNSGNYGEFSEVLYVTLPQMSQF
      TCEEDFYF.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GHBP as a Reference Standard.

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    Ghbp Human
  • View Data Sheet

    Name :

    Activin-A Human Active

    Description:

    Activin-A Human Recombinant, Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-145

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    Description

    Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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

      Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential

      Introduction:

      Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.

      Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.

      Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.

      Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.

      The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.

      In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

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    Inhba Human
  • View Data Sheet

    Name :

    GDI1 Human

    Description:

    GDP Dissociation Inhibitor 1 Human Recombinant

    Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.

    Product # :

    PRO-2023

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    Description

    GDI1 Human Recombinant produced in E. coli is a single polypeptide chain containing 470 amino acids (1-447) and having a molecular mass of 53 kDa.GDI1 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDP Dissociation Inhibitor 1 (GDI1) is expressed mainly in neural and sensory tissues. GDI1 regulates the GDP/GTP exchange reaction of nearly all Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. GDI1 is also promoting the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Mutations in GDI1 have been associated with X-linked nonspecific mental retardation.

    • Synonyms

      Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.

    • 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 MGSMDEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESSSIT PLEELYKRFQ LLEGPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVVEG SFVYKGGKIY KVPSTETEAL ASNLMGMFEK RRFRKFLVFV ANFDENDPKT FEGVDPQTTS MRDVYRKFDL GQDVIDFTGH ALALYRTDDY LDQPCLETVN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPVDD IIMENGKVVG VKSEGEVARC KQLICDPSYI PDRVRKAGQV IRIICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SYAHNVAAQG KYIAIASTTV ETTDPEKEVE PALELLEPID QKFVAISDLY EPIDDGCESQ VFCSCSYDAT THFETTCNDI KDIYKRMAGT AFDFENMKRK QNDVFGEAEQ.

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    Gdi1 Human
  • View Data Sheet

    Name :

    Activin-A Human Plant-Active

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

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

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

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

      What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      What applications can ACTIVIN-A Protein be used in?

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

       

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    Activin A Active
  • View Data Sheet

    Name :

    SYT13 Human

    Description:

    Synaptotagmin XIII Human Recombinant

    Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    Product # :

    PRO-1550

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Syt13 Human
  • View Data Sheet

    Name :

    TCEA2 Human

    Description:

    Transcription Elongation Factor A (SII)-2 Human Recombinant

    Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 2.

    Product # :

    PRO-1489

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    Description

    TCEA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 36kDa.TCEA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TCEA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.25M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)- 2 (TCEA2) is located in the nucleus, where it serves as an SII class transcription elongation factor. Elongation factors in this class are responsible for discharging RNA polymerase II ternary complexes from transcriptional arrest at template-encoded arresting sites. TCEA2 interacts with general transcription factor IIB, a basal transcription factor.

    • Synonyms

      Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 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 MGSMMGKEEE IARIARRLDK MVTKKSAEGA MDLLRELKAM PITLHLLQST RVGMSVNALR KQSSDEEVIA LAKSLIKSWK KLLDASDAKA RERGRGMPLP TSSRDASEAP DPSRKRPELP RAPSTPRITT FPPVPVTCDA VRNKCREMLT AALQTDHDHV AIGADCERLS AQIEECIFRD VGNTDMKYKN RVRSRISNLK DAKNPDLRRN VLCGAITPQQ IAVMTSEEMA SDELKEIRKA MTKEAIREHQ MARTGGTQTD LFTCGKCRKK NCTYTQVQTR SSDEPMTTFV VCNECGNRWK FC.

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    Tcea2 Human
  • View Data Sheet

    Name :

    MAPT Human 412a.a.

    Description:

    Microtubule-Associated Protein Tau 412 a.a. Human Recombinant

    Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    Product # :

    PRO-210

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    Description

    MAPT Human Recombinant (Isoform 5) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 45.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.

    • Synonyms

      Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    • 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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS KCGSKDNIKH VPGGGSVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.

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    Mapt Human 412Aa
  • View Data Sheet

    Name :

    COPE Human

    Description:

    Coatomer Protein Complex Subunit Epsilon Human Recombinant

    Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.

    Product # :

    PRO-2120

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    Description

    COPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 36.9kDa. COPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COPE protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Coatomer Protein Complex SubunitEpsilon, also known as COPE is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex which binds to dilysine motifs and reversibly links with Golgi non-clathrin-coated vesicles. COPE is necessary forbudding from Golgi membranes, and is also essential for the retrograde Golgi-to-ER transport of dilysine-taggedproteins. Coatomer complex contain at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding dissimilar isoforms have been identifiedfor COPE.

    • Synonyms

      Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.

    • 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 MGSMAPPAPG PASGGSGEVD ELFDVKNAFY IGSYQQCINE AQRVKLSSPE RDVERDVFLY RAYLAQRKFG VVLDEIKPSS APELQAVRMF ADYLAHESRR DSIVAELDRE MSRSVDVTNT TFLLMAASIY LHDQNPDAAL RALHQGDSLE CTAMTVQILL KLDRLDLARK ELKRMQDLDE DATLTQLATA WVSLATGGEK LQDAYYIFQE MADKCSPTLL LLNGQAACHM AQGRWEAAEG LLQEALDKDS GYPETLVNLI VLSQHLGKPP EVTNRYLSQL KDAHRSHPFI KEYQAKENDF DRLVLQYAPS A.

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    Cope Human
  • View Data Sheet

    Name :

    p53 Human

    Description:

    p53 Protein Human Recombinant

    Cellular tumor antigen p53, Tumor suppressor p53, Phosphoprotein p53, Antigen NY-CO-13, TP53, P53, LFS1, TRP53, FLJ92943.

    Product # :

    PRO-742

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    Description

    p53 Human Recombinant full length produced in E.Coli is a non-glycosylated, polypeptide chain having a total Mw of 81kDa. p53 Human Recombinant is fused to GST tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Purified human p53 in 50mM Tris-HCl, pH-7.5 and 10mM L-glutathione (reduced).

    More Info

    • Introduction

      Tumor protein p53 responds to various cellular stresses by regulating target genes that induce cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. p53 is a tumor suppressor gene expressed in a wide variety of tissue types and is involved in regulating cell growth, replication, and apoptosis. p53 is a DNA-binding protein containing transcription activation, DNA-binding & oligomerization domains.
      p53 binds to mdm2, SV40 T antigen and human papilloma virus E6 protein p53 senses DNA damage and possibly facilitating repair. p53 protein is a transcription factor which is encoded in humans by the TP53 gene. Alterations of TP53 occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome. p53 mutants that often occur in many different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Mutation involving p53 is found in a wide variety of malignant tumors, including breast, ovarian, bladder, colon, lung, and melanoma. The p53 expression in normal cells is low and in an assortment of transformed cell lines is high, which may contribute to transformation and malignancy. Multiple p53 variants encode distinct isoforms, which can regulate p53 transcriptional activity. p53’s significance in multicellular organisms is in cell cycle regulation therefore it functions as a tumor suppressor that is involved in preventing cancer. p53’s role in conserving stability by preventing genome mutation has earned it descriptions such as "the guardian of the genome," "the guardian angel gene," and the "master watchman.” The name p53 refers to its evident molecular mass: it migrates as a 53kDa protein on SDS-PAGE. However, based on calculations from its amino acid residues, p53's mass is in fact only 43.7kDa. This difference is attributed to the high number of proline residues in the protein which slow its migration on SDS-PAGE, consequently making it appear larger than it actually is.

    • Synonyms

      Cellular tumor antigen p53, Tumor suppressor p53, Phosphoprotein p53, Antigen NY-CO-13, TP53, P53, LFS1, TRP53, FLJ92943.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      For long term storage store at -20°C. Avoid freeze/thaw cycles.

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    P53 Human Gst
  • View Data Sheet

    Name :

    DnaK SBD

    Description:

    DnaK Substrate Binding Domain E.Coli Recombinant

    HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    Product # :

    HSP-008

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    Description

    Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 25mM Tris-HCl, pH7.5, 2mM B-ME and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

    • Synonyms

      HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    • 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

      MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST.

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    Dnak Sbd
  • View Data Sheet

    Name :

    PPP1R3B Human

    Description:

    Protein Phosphatase 1, Regulatory Subunit 3B Human Recombinant

    Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    Product # :

    PRO-1700

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    Description

    PPP1R3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 35.1 kDa.PPP1R3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP1R3B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Phosphatase 1, Regulatory Subunit 3B (PPP1R3B) is the catalytic subunit of the serine/theonine phosphatase, protein phosphatase-1. PPP1R3B, which is expressed both in liver and in skeletal muscle tissue, regulates glycogen synthesis in these tissues. PPP1R3B is involved in type 2 diabetes and maturity-onset diabetes of the young.

    • Synonyms

      Protein phosphatase 1 regulatory subunit 3B, Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, Protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, Protein phosphatase 1 subunit GL, PTG, PPP1R4, PPP1R3B, Protein Phosphatase 1, Regulatory Subunit 3B, GL.

    • 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 MGSMMAVDIE YRYNCMAPSL RQERFAFKIS PKPSKPLRPC IQLSSKNEAS GMVAPAVQEK KVKKRVSFAD NQGLALTMVK VFSEFDDPLD MPFNITELLD NIVSLTTAES ESFVLDFSQP SADYLDFRNR LQADHVCLEN CVLKDKAIAG TVKVQNLAFE KTVKIRMTFD TWKSYTDFPC QYVKDTYAGS DRDTFSFDIS LPEKIQSYER MEFAVYYECN GQTYWDSNRG KNYRIIRAEL KSTQGMTKPH SGPDLGISFD QFGSPRCSYG LFPEWPSYLG YEKLGPYY.

    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.

    Ppp1R3B Human
  • View Data Sheet

    Name :

    SET Human

    Description:

    SET Human Recombinant

    2PP2A, I2PP2A, IGAAD, IPP2A2, PHAPII, TAF-I, TAF-IBETA, Protein SET, HLA-DR-associated protein II, Inhibitor of granzyme A-activated DNase, Template-activating factor I, SET.

    Product # :

    PRO-1540

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SET Human Recombinant produced in E. coli is a single polypeptide chain containing 313 amino acids (1-290) and having a molecular mass of 35.9kDa. SET is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SET 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

      SET is part of a complex localized to the endoplasmic reticulum however is found in the nucleus. SET inhibits apoptosis following attack by cytotoxic T lymphocytes and can also enhance DNA replication of the adenovirus genome. SET inhibits acetylation of nucleosomes, particularly histone H4, by histone acetylases (HAT). This inhibition is accomplished by masking histone lysines from being acetylated.

    • Synonyms

      2PP2A, I2PP2A, IGAAD, IPP2A2, PHAPII, TAF-I, TAF-IBETA, Protein SET, HLA-DR-associated protein II, Inhibitor of granzyme A-activated DNase, Template-activating factor I, SET.

    • 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 MGSMAPKRQS PLPPQKKKPR PPPALGPEET SASAGLPKKG EKEQQEAIEH IDEVQNEIDR LNEQASEEIL KVEQKYNKLR QPFFQKRSEL IAKIPNFWVT TFVNHPQVSA LLGEEDEEAL HYLTRVEVTE FEDIKSGYRI DFYFDENPYF ENKVLSKEFH LNESGDPSSK STEIKWKSGK DLTKRSSQTQ NKASRKRQHE EPESFFTWFT DHSDAGADEL GEVIKDDIWP NPLQYYLVPD MDDEEGEGEE DDDDDEEEEG LEDIDEEGDE DEGEEDEDDD EGEEGEEDEG EDD.

    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.

    Set Human
  • View Data Sheet

    Name :

    CRP Rat

    Description:

    C-Reactive Protein Rat Recombinant

    Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    Product # :

    PRO-1421

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
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    • More Info

    Description

    CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    • 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

      HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.

    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.

    Crp Rat
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