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Search results

1000 results found for “hbsag”

Name

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  • View Data Sheet

    Name :

    S100b Mouse, His

    Description:

    S100 Calcium Binding Protein B Mouse Recombinant, His Tag

    Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    Product # :

    PRO-853

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    Description

    S100B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-112 a.a.) and having a molecular mass of 12.8 kDa. The Mouse S100B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100B Mouse solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100B faintly binds calcium but binds zinc extremely strongly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. S100B binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction participates in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

    • Synonyms

      Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    • 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 MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVAM VTTACHEFFE HE.

    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.

    S100B Mouse
  • View Data Sheet

    Name :

    SH3BGRL2 Human

    Description:

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 2 Human Recombinant

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 2, Fovea-Associated SH3 Domain-Binding Protein, FASH3. 

    Product # :

    PRO-1215

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    Description

    SH3BGRL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 130 amino acids (1-107) and having a molecular mass of 14.7 kDa.SH3BGRL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SH3BGRL2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH3 domain-binding glutamic acid-rich-like protein 2 (SH3BGRL2) belongs to the human SH3BGR family. SH3BGRL2 is a protein of 107 amino acids, which, like SH3BGRL and SH3BGRL3 proteins, is highly homologous to the N-terminal region of the SH3BGR protein and seems to be related to Glutaredoxins and to PKC-interacting cousin of thioredoxin homology domain. SH3BGRL2 is highly expressed in the brain, placenta, liver and kidney and it is also expressed in the retina. The SH3BGRL2 gene is located to chromosome 6q13-15 and its messenger RNA has a large 3' untranslated region containing several AUUUA repeats.

    • Synonyms

      SH3 Domain Binding Glutamic Acid-Rich Protein Like 2, Fovea-Associated SH3 Domain-Binding Protein, FASH3.

    • 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 MGSMVIRVFI ASSSGFVAIK KKQQDVVRFL EANKIEFEEV DITMSEEQRQ WMYKNVPPEK KPTQGNPLPP QIFNGDRYCG DYDSFFESKE SNTVFSFLGL KPRLASKAEP

    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.

    Sh3Bgrl2 Human
  • View Data Sheet

    Name :

    SHH Human, His

    Description:

    Sonic HedgeHog Human Recombinant, His Tag

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-717

    Price :

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    Description

    Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids and having a molecular mass of 20.7kDa. The Sonic HedgeHog is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHH Human solution containing 20mM Tris HCL pH-8, 0.1M NaCl, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • 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). Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MCGPGRGFGK RRHPKKLTPL AYKQFIPNVA EKTLGASGRY EGKISRNSER FKELTPNYNP DIIFKDEENT GADRLMTQRC KDKLNALAIS VMNQWPGVKL RVTEGWDEDG HHSEESLHYE GRAVDITTSD RDRSKYGMLA RLAVEAGFDW VYYESKAHIH CSVKAENSVA AKSGGLEHHH HHH.

    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.

    Shh Human His
  • View Data Sheet

    Name :

    SHMT1 Human

    Description:

    Serine Hydroxymethyltransferase 1 Human Recombinant

    Serine hydroxymethyltransferase 1 (soluble), CSHMT, Glycine hydroxymethyltransferase, Serine methylase, 14 kDa protein, cytoplasmic serine hydroxymethyltransferase, serine hydroxymethyltransferase cytosolic, EC 2.1.2.1.

    Product # :

    ENZ-199

    Price :

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    Description

    SHMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483 a.a.) and having a molecular mass of 55.2kDa.SHMT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHMT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SHMT1 is a member of the SHMT family. SHMT1 is the cellular form of serine hydroxymethyltransferase, a pyridoxal phosphate-containing enzyme which catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5 10-methylene tetrahydrofolate. In addition, SHMT1 specifically provides one-carbon units for thymidylate biosynthesis, reduces methylenetetrahydrofolate pools for S-adenosylmethionine (SAM) synthesis by synthesizing serine, sequesters 5-methyltetrahydrofolate and inhibits SAM synthesis.

    • Synonyms

      Serine hydroxymethyltransferase 1 (soluble), CSHMT, Glycine hydroxymethyltransferase, Serine methylase, 14 kDa protein, cytoplasmic serine hydroxymethyltransferase, serine hydroxymethyltransferase cytosolic, EC 2.1.2.1.

    • 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 MTMPVNGAHK DADLWSSHDK MLAQPLKDSD VEVYNIIKKE SNRQRVGLEL IASENFASRA VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELETLCQKRA LQAYKLDPQC WGVNVQPYSG SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY INYDQLEENA RLFHPKLIIA GTSCYSRNLE YARLRKIADE NGAYLMADMA HISGLVAAGV VPSPFEHCHV VTTTTHKTLR GCRAGMIFYR KGVKSVDPKT GKEILYNLES LINSAVFPGL QGGPHNHAIA GVAVALKQAM TLEFKVYQHQ VVANCRALSE ALTELGYKIV TGGSDNHLIL VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDRSALRPSG LRLGTPALTS RGLLEKDFQK VAHFIHRGIE LTLQIQSDTG VRATLKEFKE RLAGDKYQAA VQALREEVES FASFFPLPGL PDF.

    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.

    Shmt1 Human
  • View Data Sheet

    Name :

    ATOH1 Human

    Description:

    Atonal Homolog 1 Human Recombinant

    Atonal homolog 1 (Drosophila), Helix-loop-helix protein hATH-1, Class A basic helix-loop-helix protein 14, bHLHa14, HATH1, Math1.

    Product # :

    PRO-1073

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    Description

    ATOH1 Human Recombinant produced in E. coli is a single polypeptide chain containing 198 amino acids (158-354) and having a molecular mass of 21.3kDa.ATOH1 is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ATOH1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ATOH1 activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is entirely provoked by the negative regulator of neurogenesis HES1. ATOH1 takes part in the differentiation of divisions of neural cells by activating E box-dependent transcription.

    • Synonyms

      Atonal homolog 1 (Drosophila), Helix-loop-helix protein hATH-1, Class A basic helix-loop-helix protein 14, bHLHa14, HATH1, Math1.

    • 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

      MKQRRLAANA RERRRMHGLN HAFDQLRNVI PSFNNDKKLS KYETLQMAQI YINALSELLQ TPSGGEQPPP PPASCKSDHH HLRTAASYEG GAGNATAAGA QQASGGSQRP TPPGSCRTRF SAPASAGGYS VQLDALHFST FEDSALTAMM AQKNLSPSLP GSILQPVQEE NSKTSPRSHR SDGEFSPHSH YSDSDEAS

    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.

    Atoh1 Human
  • View Data Sheet

    Name :

    B9D1 Human

    Description:

    B9 Protein Domain 1 Human Recombinant

    B9 Protein Domain 1, MKSR1, Endothelial Precursor Protein B9, MKS1-Related Protein 1, MKS9, B9 Domain-Containing Protein 1, EPPB9, B9, B9 domain-containing protein 1.

    Product # :

    PRO-2073

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    Description

    B9D1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a) and having a molecular mass of 25.2kDa. B9D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    B9D1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      B9 domain-containing protein (B9D1) is one of the numerous proteins which take part in ciliogenesis. Alterations in expression of B9D1 have been found in a family with Meckel syndrome. The Meckel syndrome has been associated with at least six different genes. B9D1 is placed within the Smith-Magenis syndrome region on chromosome 17. Three alternatively spliced transcript variants which encode dissimilar proteins have been found for B9D1.

    • Synonyms

      B9 Protein Domain 1, MKSR1, Endothelial Precursor Protein B9, MKS1-Related Protein 1, MKS9, B9 Domain-Containing Protein 1, EPPB9, B9, B9 domain-containing protein 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 MGSMATASPS VFLLMVNGQV ESAQFPEYDD LYCKYCFVYG QDWAPTAGLE EGISQITSKS QDVRQALVWN FPIDVTFKST NPYGWPQIVL SVYGPDVFGN DVVRGYGAVH VPFSPGRHKR TIPMFVPEST SKLQKFTSWF MGRRPEYTDP KVVAQGEGRE VTRVRSQGFV TLLFNVVTKD MRKLGYDTGP SDTQGVLGPS PPQSFPQ.

    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.

    B9D1 Human
  • View Data Sheet

    Name :

    EREG Human, His

    Description:

    Epiregulin Human Recombinant, His Tag

    Epiregulin, Proepiregulin, ER, ERP.

    Product # :

    CYT-859

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    Description

    EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE

    sds-page

    EREG-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      Epiregulin, Proepiregulin, ER, ERP.

    • 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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 7.7kDa.

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

      What is the Purity of EREG Protein?
      EREG Protein is >80% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EREG Protein?
      MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

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

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

    Ereg Human His
  • View Data Sheet

    Name :

    PAICS Human

    Description:

    Phosphoribosylaminoimidazole Carboxylase Human Recombinant

    PAICS, Phosphoribosylaminoimidazole Carboxylase Phosphoribosylaminoimidazole, Succinocarboxamide Synthetase, PAIS, AIRC, ADE2, ADE2H1, AIR Carboxylase, Multifunctional Protein ADE2, Multifunctional Protein ADE2H1, SAICAR Synthetase.

    Product # :

    ENZ-786

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    Description

    PAICS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425) and having a molecular mass of 49.5kDa.PAICS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PAICS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.

    • Synonyms

      PAICS, Phosphoribosylaminoimidazole Carboxylase Phosphoribosylaminoimidazole, Succinocarboxamide Synthetase, PAIS, AIRC, ADE2, ADE2H1, AIR Carboxylase, Multifunctional Protein ADE2, Multifunctional Protein ADE2H1, SAICAR Synthetase.

    • 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 MGSMATAEVL NIGKKLYEGK TKEVYELLDS PGKVLLQSKD QITAGNAARK NHLEGKAAIS NKITSCIFQL LQEAGIKTAF TRKCGETAFI APQCEMIPIE WVCRRIATGS FLKRNPGVKE GYKFYPPKVE LFFKDDANND PQWSEEQLIA AKFCFAGLLI GQTEVDIMSH ATQAIFEILE KSWLPQNCTL VDMKIEFGVD VTTKEIVLAD VIDNDSWRLW PSGDRSQQKD KQSYRDLKEV TPEGLQMVKK NFEWVAERVE LLLKSESQCR VVVLMGSTSD LGHCEKIKKA CGNFGIPCEL RVTSAHKGPD ETLRIKAEYE GDGIPTVFVA VAGRSNGLGP VMSGNTAYPV ISCPPLTPDW GVQDVWSSLR LPSGLGCSTV LSPEGSAQFA AQIFGLSNHL VWSKLRASIL NTWISLKQAD KKIRECNL.

    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.

    Paics Human
  • View Data Sheet

    Name :

    SULT2A1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    Product # :

    ENZ-141

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    Description

    SULT2A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-285a.a) and having a molecular mass of 35.9kDa.SULT2A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT2A1 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.

    • Synonyms

      Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    • 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 MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE

    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.

    Sult2A1 Human
  • View Data Sheet

    Name :

    FABP6 Human, His

    Description:

    Fatty Acid Binding Protein 6 Human Recombinant, His Tag

    I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.

    Product # :

    PRO-667

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    Description

    FABP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids and having a molecular mass of 18 kDa. FABP6 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP6 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FABP6 also called ileal fatty acid binding protein, is part of the small family of highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 cytosolic protein binds bile acid. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. Alternate transcription promoters generate 2 transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is acetylated on Ala2. FABP6 binds together fatty acids and bile acids and is directly involved in fatty acid transport and metabolism.

    • Synonyms

      I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

    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.

    Fabp6 Human His
  • View Data Sheet

    Name :

    GLUL Human

    Description:

    Glutamine Synthetase Human Recombinant

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ENZ-544

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    • 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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human
  • View Data Sheet

    Name :

    CIB1 Human

    Description:

    Calcium and Integrin Binding 1 Human Recombinant

    Calcium and integrin-binding protein 1, Calmyrin, DNA-PKcs-interacting protein, Kinase-interacting protein, SNK-interacting protein 2-28, SIP2-28, CIB1, CIB, KIP, PRKDCIP.

    Product # :

    PKA-345

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    Description

    CIB1 Human Recombinant is a single, non-glycosylated polypeptide chain (aa 1-191) containing a total of 211 amino acids and having a molecular mass of 23 kDa.CIB1 is fused to a 20 a.a His-tag and it was purified by conventional column chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CIB1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8 & 5mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CIB1 (Calcium and integrin binding 1) is regulatory protein with 50% homology to calmodulin and calcineurin B, that encodes a member of the calcium-binding protein family. CIB1 interacts with DNA-dependent protein kinase and may play a role in kinase-phosphatase regulation of DNA end joining. Also CIB1 is widely expressed and binds to a number of effectors, such as integrin ?IIb, PAK1, and polo-like kinases, in different tissues.

    • Synonyms

      Calcium and integrin-binding protein 1, Calmyrin, DNA-PKcs-interacting protein, Kinase-interacting protein, SNK-interacting protein 2-28, SIP2-28, CIB1, CIB, KIP, PRKDCIP.

    • 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 0.1% HSA or BSA. Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPQ EQRTVESSLR AQVPFEQILS LPELKANPFK ERICRVFSTS PAKDSLSFED FLDLLSVFSD TATPDIKSHY AFRIFDFDDD GTLNREDLSR LVNCLTGEGE DTRLSASEMK QLIDNILEES DIDRDGTINL SEFQHVISRS PDFASSFKIV L.

    • Patent Protected Countries

      The Sale of recombinant Human CIB1 by ProSpec is prohibited in the United States of America.

    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.

    Cib1 Human
  • View Data Sheet

    Name :

    SARS Nucleocapsid Biotin Antibody

    Description:

    Mouse Anti SARS Nucleocapsid Biotinylated

    Product # :

    ANT-764

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    Description

    SARS Nucleoprotein Biotinylated antibody clone PT3851 is specific for the nucleocapsid SARS-CoV protein and recognizes the nucleoprotein of SARS-CoV-2 by ELISA.

    Formulation

    1mg/ml in DPBS, 1% BSA and 0.1% Proclin 950.

    Purity

    Greater than 90% as determined by SDS-PAGE gel.

    Citations

    More Info

    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

      Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.

    • Immunogen

      Recombinant protein fragment 1-49 a.a. of the SARS nucleoprotein.

    • Clone

      PT3851

    • Applications

      ELISA.

    • Isotype

      Mouse IgG2b.

    • Type

      Mouse antibody Monoclonal.

    • Purification Method

      Protein A affinity purified.

    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.

    Cov Nucleocprotein Antibody
  • View Data Sheet

    Name :

    Heparanase 1 Clone HP3/17

    Description:

    Heparanase 1 (HPA1), Monoclonal Anti-Human Antibody

    Product # :

    ANT-154

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    Source

    Mab HP3/17 is a Protein G affinity purified monoclonal antibody raised against a polypeptide from the 50 kDa subunit of Heparanase.

    Formulation

    Each vial contains 50, 100 or 150 μg in 14, 28 or 42 μl respectively, of 0.22 micron filtered solution of 20 mM Sodium Phosphate; 150 mM NaCl; pH 7.2, containing 0.01% Thimerosal.

    Purity

    >98% on SDS-PAGE when loaded 50 μg/lane.

    Citations

    More Info

    • Introduction

      Heparanase is an endo-β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).

    • Stability

      Store at 4°C. Stable for six months from the date of shipment. For extended storage, freeze in working aliquots at -20°C. Avoid repeated freeze-thaw cycles.

    • Ig Subclass

      Mouse IgG2Bκ

    • Applications

      Western blot
      Immunohistochemistry

    • Data Sheet

      To view the FULL VERSION click Monoclonal Anti-Human Heparanase 1:

    • Patent Protected Countries

      Anti-heparanase antibodies and their uses, including HP3/17 and its uses, are protected by US. Patents No. 6,177,545; 6,531,129, additional US patent applications and patents and patent applications worldwide.

    • Specificity

      HP3/17 reacts with the 50 kDa subunit and with the 65 kDa precursor of human or mouse Heparanase by Western blotting and immunohistochemistry.Recommended dilution range for Western blot analysis: 1:4000.Recommended dilution range for immunohistochemistry: 1:40.

    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.

    Heparanase 1 Clone Hp3 17 Antibody
  • View Data Sheet

    Name :

    SARS MERS, Sf9

    Description:

    SARS MERS Spike Recombinant

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

    Product # :

    SARS-051

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    Description

    SARS MERS Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1285 amino acids (18-1296aa) and having a molecular mass of 141.6kDa.SARS MERS 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 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    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 SP, Spike glycoprotein, S glycoprotein, S, Spike protein, 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

      YVDVGPDSVK SACIEVDIQQ TFFDKTWPRP IDVSKADGII YPQGRTYSNI TITYQGLFPY QGDHGDMYVY SAGHATGTTP QKLFVANYSQ DVKQFANGFV VRIGAAANST GTVIISPSTS ATIRKIYPAF MLGSSVGNFS DGKMGRFFNH TLVLLPDGCG TLLRAFYCIL EPRSGNHCPA GNSYTSFATY HTPATDCSDG NYNRNASLNS FKEYFNLRNC TFMYTYNITE DEILEWFGIT QTAQGVHLFS SRYVDLYGGN MFQFATLPVY DTIKYYSIIP HSIRSIQSDR KAWAAFYVYK LQPLTFLLDF SVDGYIRRAI DCGFNDLSQL HCSYESFDVE SGVYSVSSFE AKPSGSVVEQ AEGVECDFSP LLSGTPPQVY NFKRLVFTNC NYNLTKLLSL FSVNDFTCSQ ISPAAIASNC YSSLILDYFS YPLSMKSDLS VSSAGPISQF NYKQSFSNPT CLILATVPHN LTTITKPLKY SYINKCSRLL SDDRTEVPQL VNANQYSPCV SIVPSTVWED GDYYRKQLSP LEGGGWLVAS GSTVAMTEQL QMGFGITVQY GTDTNSVCPK LEFANDTKIA SQLGNCVEYS LYGVSGRGVF QNCTAVGVRQ QRFVYDAYQN LVGYYSDDGN YYCLRACVSV PVSVIYDKET KTHATLFGSV ACEHISSTMS QYSRSTRSML KRRDSTYGPL QTPVGCVLGL VNSSLFVEDC KLPLGQSLCA LPDTPSTLTP RSVRSVPGEM RLASIAFNHP IQVDQLNSSY FKLSIPTNFS FGVTQEYIQT TIQKVTVDCK QYVCNGFQKC EQLLREYGQF CSKINQALHG ANLRQDDSVR NLFASVKSSQ SSPIIPGFGG DFNLTLLEPV SISTGSRSAR SAIEDLLFDK VTIADPGYMQ GYDDCMQQGP ASARDLICAQ YVAGYKVLPP LMDVNMEAAY TSSLLGSIAG VGWTAGLSSF AAIPFAQSIF YRLNGVGITQ QVLSENQKLI ANKFNQALGA MQTGFTTTNE AFQKVQDAVN NNAQALSKLA SELSNTFGAI SASIGDIIQR LDVLEQDAQI DRLINGRLTT LNAFVAQQLV RSESAALSAQ LAKDKVNECV KAQSKRSGFC GQGTHIVSFV VNAPNGLYFM HVGYYPSNHI EVVSAYGLCD AANPTNCIAP VNGYFIKTNN TRIVDEWSYT GSSFYAPEPI TSLNTKYVAP QVTYQNISTN LPPPLLGNST GIDFQDELDE FFKNVSTSIP NFGSLTQINT TLLDLTYEML SLQQVVKALN ESYIDLKELG NYTYYNKWPH HHHHH

    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.

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  • View Data Sheet

    Name :

    HDHD3 Human

    Description:

    Haloacid Dehalogenase-Like Hydrolase Domain Containing 3 Human Recombinant

    Haloacid dehalogenase-like hydrolase domain-containing protein 3, HDHD3, C9orf158, MGC12904, 2810435D12Rik.

    Product # :

    ENZ-089

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    Description

    HDHD3 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 287 amino acids (1-251 a.a.) and having a molecular mass of 32.2kDa. The HDHD3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDHD3 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Haloacid dehalogenase-like hydrolase domain-containing protein 3 (HDHD3) is a member of the HAD-like hydrolase superfamily. This family of hydrolase enzymes includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases.

    • Synonyms

      Haloacid dehalogenase-like hydrolase domain-containing protein 3, HDHD3, C9orf158, MGC12904, 2810435D12Rik.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAHR LQIRLLTWDV KDTLLRLRHP LGEAYATKAR AHGLEVEPSA LEQGFRQAYR AQSHSFPNYG LSHGLTSRQW WLDVVLQTFH LAGVQDAQAV APIAEQLYKD FSHPCTWQVL DGAEDTLREC RTRGLRLAVI SNFDRRLEGI LEGLGLREHF DFVLTSEAAG WPKPDPRIFQ EALRLAHMEP VVAAHVGDNY LCDYQGPRAV GMHSFLVVGP QALDPVVRDS VPKEHILPSL AHLLPALDCL EGSTPGL.

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    Hdhd3 Human
  • View Data Sheet

    Name :

    HINT2 Human

    Description:

    Histidine Triad Nucleotide Binding Protein 2 Human Recombinant

    Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.

    Product # :

    PRO-1455

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    Description

    HINT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (18-163 a.a) and having a molecular mass of 17.9kDa.HINT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HINT2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Histidine triad nucleotide-binding protein 2 (HINT2) belongs to the triad proteins, which are nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides. Hydrolase is most likely involved in steroid biosynthesis, furthermore it might play a role in apoptosis. HINT2 shows high expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients.

    • Synonyms

      Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.

    • 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 MGSVAATGVR GGQVRGAAGV TDGNEVAKAQ QATPGGAAPT IFSRILDKSL PADILYEDQQ CLVFRDVAPQ APVHFLVIPK KPIPRISQAE EEDQQLLGHL LLVAKQTAKA EGLGDGYRLV INDGKLGAQS VYHLHIHVLG GRQLQWPPG.

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    Hint2 Human
  • View Data Sheet

    Name :

    NARS Human, Sf9

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant, Sf9

    Asparagine--tRNA ligase, cytoplasmic, EC 6.1.1.22, Asparaginyl-tRNA synthetase, AsnRS, NARS, NARS1.

    Product # :

    ENZ-716

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    Description

    NARS Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 63,853 Dalton. NARS is expressed with a -6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NARS 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

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      Asparagine--tRNA ligase, cytoplasmic, EC 6.1.1.22, Asparaginyl-tRNA synthetase, AsnRS, NARS, NARS1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Nars Human
  • View Data Sheet

    Name :

    TREM2 Human, HEK

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

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    PRO-2773

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    Description

    TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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

      HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.

    • Background

      TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.

      The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.

      Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.

      Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.

      Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.

      Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.

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    Trem2 Human Hek
  • View Data Sheet

    Name :

    SCGB1A1 Rat

    Description:

    Uteroglobin Rat Recombinant

    Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    Product # :

    CYT-820

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    Description

    SCGB1A1 Rat Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 77 amino acids and having a molecular mass of 17.0kDa.

    Source

    Escherichia Coli.

    Formulation

    SCGB1A1 protein was lyophilized from a 0.2 µm filtered concentrated 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

    Fully biologically active when compared to standard. The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0 ?g/ml, corresponding to a specific activity of >200IU/mg.

    Citations

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    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SCGB1A1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SSDICPGFLQ VLEALLLGSE SNYEAALKPF NPASDLQNAG TQLKRLVDTL PQETRINIVK LTEKILTSPL CEQDLRV

    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.

    Scgb1A1 Rat
  • View Data Sheet

    Name :

    SSX2 Human

    Description:

    Synovial Sarcoma, X Breakpoint 2 Human Recombinant

    Cancer/testis antigen family 5, member 2b, CT5.2b, Protein SSX2, Cancer/testis antigen 5.2, Synovial sarcoma, X breakpoint 2, CT5.2, Tumor antigen HOM-MEL-40, SSX2, SSX2A, SSX2B.

    Product # :

    PRO-1996

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    Description

    SSX2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-188a.a) and having a molecular mass of 24.0kDa. SSX2 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SSX2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synovial Sarcoma, X Breakpoint 2 (SSX2) is a part of the family of highly homologous synovial sarcoma X breakpoint proteins which play a role as transcriptional repressors. Homologous synovial sarcoma X breakpoint proteins are also able to bring out spontaneous humoral and cellular immune responses in cancer patients, and are effective targets in cancer vaccine-based immunotherapy.

    • Synonyms

      Cancer/testis antigen family 5, member 2b, CT5.2b, Protein SSX2, Cancer/testis antigen 5.2, Synovial sarcoma, X breakpoint 2, CT5.2, Tumor antigen HOM-MEL-40, SSX2, SSX2A, SSX2B.

    • 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 RSMNGDDAFA RRPTVGAQIP EKIQKAFDDI AKYFSKEEWE KMKASEKIFY VYMKRKYEAM TKLGFKATLP PFMCNKRAED FQGNDLDNDP NRGNQVERPQ MTFGRLQGIS PKIMPKKPAE EGNDSEEVPE ASGPQNDGKE LCPPGKPTTS EKIHERSGPK RGEHAWTHRL RERKQLVIYE EISDPEEDDE.

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    Ssx2 Human
  • View Data Sheet

    Name :

    Apolipoprotein A1 Human, His

    Description:

    Apolipoprotein A-I Human Recombinant, His Tag

    Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

    Product # :

    CYT-661

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    Description

    APOA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (25-267 a.a.) and having a molecular mass of 30.3kDa. APOA1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The APOA1 solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Apolipoprotein A1-sds-page - Product image 1

    Citations

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    • Introduction

      APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.

    • Synonyms

      Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

    • 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 MDEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.

    • Background

      What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
      APOLIPOPROTEIN A1 Protein has a total Mw of 30.3kDa.

      What is the source or expression system of APOLIPOPROTEIN A1 Protein?
      Escherichia Coli.

      What is the Purity of APOLIPOPROTEIN A1 Protein?
      APOLIPOPROTEIN A1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
      The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.

      What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
      MGSSHHHHHH SSGLVPRGSH MDEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ

      What applications can APOLIPOPROTEIN A1 Protein be used in?
      APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
      The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.

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    Apoa1 Human
  • View Data Sheet

    Name :

    HTLV-1 Envelope

    Description:

    HTLV-1 Envelope Recombinant

    Product # :

    HIV-107

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    Description

    The E.Coli derived recombinant protein contains the C- terminus of gp46 and most of p21E of HTLV-1. This non-fusion, E. coli-derived protein, starts from HTLV-1 env. Amino acid 165, and is ending in amino acid 440, Mw 27 kDa.

    Formulation

    10mM Na-PO4 pH 6.0, 0.1% SDS and 1mM DTT.

    Purity

    HTLV-1 Envelope protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

    Citations

    More Info

    • Introduction

      Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).

    • 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.

    • Purification Method

      HTLV-1 Envelope was purified by proprietary chromatographic technique.

    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.

    Htlv 1 Envelope
  • View Data Sheet

    Name :

    Prealbumin Human

    Description:

    Transthyretin Human

    TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    Product # :

    PRO-2740

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

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

    Description

    Human Transthyretin dimer protein produced in Human plasma having a molecular mass of 30kD. Under certain conditions it may be shown as a monomer (15kD) or a tetramer (60kD).

    Source

    Human serum.

    Formulation

    The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.

    Purity

    Greater than 96.0%.

    Citations

    More Info

    • Introduction

      Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.

    • Synonyms

      TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Prealbumin Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Prealbumin Human in phosphate buffer pH > 7 containing 0.15M NaCl.

    • Human Virus Test

      Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).

    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.

    Prealbumin Protein
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