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Search results

1000 results found for “lhrh”

Name

Description

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  • View Data Sheet

    Name :

    FGFR4 Human, His

    Description:

    Fibroblast Growth Factor Receptor-4 Human Recombinant, His Tag

    Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

    Product # :

    PKA-090

    Price :

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    • source
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    Description

    Fibroblast Growth Factor Receptor-4 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (22-369a.a.) and having a molecular mass of 39.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).FGFR4 is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FGFR4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.

    • Synonyms

      Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

    • 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

      LEASEEVELE PCLAPSLEQQ EQELTVALGQ PVRLCCGRAE RGGHWYKEGS RLAPAGRVRG WRGRLEIASF LPEDAGRYLC LARGSMIVLQ NLTLITGDSL TSSNDDEDPK SHRDPSNRHS YPQQAPYWTH PQRMEKKLHA VPAGNTVKFR CPAAGNPTPT IRWLKDGQAF HGENRIGGIR LRHQHWSLVM ESVVPSDRGT YTCLVENAVG SIRYNYLLDV LERSPHRPIL QAGLPANTTA VVGSDVELLC KVYSDAQPHI QWLKHIVING SSFGADGFPY VQVLKTADIN SSEVEVLYLR NVSAEDAGEY TCLAGNSIGL SYQSAWLTVL PEEDPTWTAA APEARYTDLE HHHHHH.

    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.

    Fgfr4 Human His
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

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    • description
    • source
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    • biological activity
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    • Citations

    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Human
  • View Data Sheet

    Name :

    LIN28B Human

    Description:

    LIN28B Human Recombinant

    Lin-28 Homolog B (C. Elegans), Protein Lin-28 Homolog B, CSDD2, Lin-28B, Lin-28.2, FLJ16517.

    Product # :

    PRO-1249

    Price :

    Quantity :

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    Description

    LIN28B Human Recombinant produced in E. coli is a single polypeptide chain containing 273 amino acids (1-250) and having a molecular mass of 29.5 kDa. LIN28B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LIN28B solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lin28B is a member of the lin-28 family. LIN28 protein is a microRNA-binding protein that binds to and enhances the translation of the IGF-2 mRNA. Lin28B acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. LIN28 is highly expressed in testis, fetal liver, placenta, and in primary human tumors and cancer cell lines.

    • Synonyms

      Lin-28 Homolog B (C. Elegans), Protein Lin-28 Homolog B, CSDD2, Lin-28B, Lin-28.2, FLJ16517.

    • 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 MGSMAEGGAS KGGGEEPGKL PEPAEEESQV LRGTGHCKWF NVRMGFGFIS MINREGSPLD IPVDVFVHQS KLFMEGFRSL KEGEPVEFTF KKSSKGLESI RVTGPGGSPC LGSERRPKGK TLQKRKPKGD RCYNCGGLDH HAKECSLPPQ PKKCHYCQSI MHMVANCPHK NVAQPPASSQ GRQEAESQPC TSTLPREVGG GHGCTSPPFP QEARAEISER SGRSPQEASS TKSSIAPEEQ SKKGPSVQKR KKT.

    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.

    Lin28B Human
  • View Data Sheet

    Name :

    LPCAT1 Human

    Description:

    Lysophosphatidylcholine Acyltransferase Human Recombinant

    AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 3.

    Product # :

    ENZ-695

    Price :

    Quantity :

    Shipping Method :

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    Description

    LPCAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 479 amino acids (79-534a.a) and having a molecular mass of 53.4kDa. LPCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LPCAT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysophosphatidylcholine acyltransferase 1 (LPCAT1) is a part of the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. LPCAT1 is a key enzyme for remodeling phospholipids, including phosphatidylcholine. LPCAT1 possesses both acyltransferase and acetyltransferase activities and also mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). LPCAT1 presents a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. LPCAT1 synthesizes phosphatidylcholine in pulmonary surfactant and therefore playing an important role in respiratory physiology.

    • Synonyms

      AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSAEKEPE QPPALWRKVV DFLLKAIMRT MWFAGGFHRV AVKGRQALPT EAAILTLAPH SSYFDAIPVT MTMSSIVMKA ESRDIPIWGT LIQYIRPVFV SRSDQDSRRK TVEEIKRRAQ SNGKWPQIMI FPEGTCTNRT CLITFKPGAF IPGAPVQPVV LRYPNKLDTI TWTWQGPGAL EILWLTLCQF HNQVEIEFLP VYSPSEEEKR NPALYASNVR RVMAEALGVS VTDYTFEDCQ LALAEGQLRL PADTCLLEFA RLVRGLGLKP EKLEKDLDRY SERARMKGGE KIGIAEFAAS LEVPVSDLLE DMFSLFDESG SGEVDLRECV VALSVVCRPA RTLDTIQLAF KMYGAQEDGS VGEGDLSCIL KTALGVAELT VTDLFRAIDQ EEKGKITFAD FHRFAEMYPA FAEEYLYPDQ THFESCAETS PAPIPNGFCA DFSPENSDAG RKPVRKKLD.

    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.

    Lpcat1 Human
  • View Data Sheet

    Name :

    RARRES2 Human, Sf9

    Description:

    Retinoic Acid Receptor Responder 2 Human Recombinant, Sf9

    Retinoic Acid Receptor Responder 2, Chemerin, Retinoic Acid Receptor Responder (Tazarotene Induced) 2, Tazarotene-Induced Gene 2 Protein, RAR-Responsive Protein TIG2, TIG2, Retinoic Acid Receptor Responder Protein 2, HP10433, Retinoic acid receptor responder protein 2, Chemerin, RAR-responsive protein TIG2, Tazarotene-induced gene 2 protein.

    Product # :

    PRO-2382

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    Description

    RARRES2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (21-157a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). RARRES2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RARRES2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

    • Synonyms

      Retinoic Acid Receptor Responder 2, Chemerin, Retinoic Acid Receptor Responder (Tazarotene Induced) 2, Tazarotene-Induced Gene 2 Protein, RAR-Responsive Protein TIG2, TIG2, Retinoic Acid Receptor Responder Protein 2, HP10433, Retinoic acid receptor responder protein 2, Chemerin, RAR-responsive protein TIG2, Tazarotene-induced gene 2 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

      ADPELTEAQR RGLQVALEEF HKHPPVQWAF QETSVESAVD TPFPAGIFVR LEFKLQQTSC RKRDWKKPEC KVRPNGRKRK CLACIKLGSE DKVLGRLVHC PIETQVLREA EEHQETQCLR VQRAGEDPHS FYFPGQFAFS HHHHHH.

    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.

    Rarres2 Human Sf9
  • View Data Sheet

    Name :

    RPL35 Human

    Description:

    Ribosomal Protein L35 Human Recombinant

    Ribosomal Protein L35, 60S Ribosomal Protein L35, RPL35A, DBA5, L35, 60S ribosomal protein L35.

    Product # :

    PRO-2097

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    Description

    RPL35 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 16.9kDa. RPL35 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPL35 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ribosomal Protein L35, also known as RPL35 is a ribosomal protein which is a component of the 60S subunit. Ribosomes are the organelles which catalyze protein synthesis, they consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and about 80 structurally different proteins. RPL35 is a member of the L29P family of ribosomal proteins. RPL35 is located in the cytoplasm. As typicaly for genes encoding ribosomal proteins, there are multiple processed pseudogenes of RPL35 dispersed through the genome.

    • Synonyms

      Ribosomal Protein L35, 60S Ribosomal Protein L35, RPL35A, DBA5, L35, 60S ribosomal protein L35.

    • 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 MGSMAKIKAR DLRGKKKEEL LKQLDDLKVE LSQLRVAKVT GGAASKLSKI RVVRKSIARV LTVINQTQKE NLRKFYKGKK YKPLDLRPKK TRAMRRRLNK HEENLKTKKQ QRKERLYPLR KYAVKA.

    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.

    Rpl35 Human
  • View Data Sheet

    Name :

    Thymopentin

    Description:

    Thymopentin

    Product # :

    HOR-241

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    Description

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

    Formulation

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

    Purity

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

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

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

    Thymopentin
  • View Data Sheet

    Name :

    Borrelia p100

    Description:

    Borrelia Burgdorferi p100 Recombinant

    Product # :

    BOR-003

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    Description

    Recombinant Borrelia Burgdorferi p100 (p100/p83) produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 77,813 Dalton. Borrelia p100 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Borrelia p100 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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.

    • Applications

      Western blot with Lyme positive plasma.

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

    Borrelia P100
  • View Data Sheet

    Name :

    Adipotide

    Description:

    Adipotide

    Product # :

    HOR-060

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    Description

    Adipotide is a synthetic single, non-glycosylated polypeptide chain containing 25 amino acids, having a molecular mass of 2555 Dalton and a Molecular formula of C111H204N36O28S2.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Cys-Lys-Gly-Gly-Arg-Ala-Lys-AspCys-Gly-Gly-d-Lys-d-Leu-d-Ala-d-Lys-d-Leu-d-Ala-d-Lys-d-Lys-d-Leud-Ala-d-Lys-d-Leu-d-Ala-d-Lys-OH (disulfide bond).

    • Background

      Adipotide is a proapoptotic peptidomimetic which selectively destroy the blood vessels supplying white adipose tissue. Adipotide plays a main role in translational metabolic research. Adipotide is the most potent proof-of-concept for non-hormonal, vascular-targeted fat reduction.

    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.

    Adipotide
  • View Data Sheet

    Name :

    PGLYRP1 Human, HEK

    Description:

    Peptidoglycan Recognition Protein 1 Human Recombinant, HEK

    PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.

    Product # :

    PRO-2726

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    Description

    PGLYRP1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 184 amino acids (22-196 a.a) and having a molecular mass of 20.5 kDa.PGLYRP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PGLYRP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Peptidoglycan. The ED50 range ≤ 30 ng/ml.

    Citations

    More Info

    • Introduction

      Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.

    • Synonyms

      PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.

    • 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

      DGSQETEDPA CCSPIVPRNE WKALASECAQ HLSLPLRYVV VSHTAGSSCN TPASCQQQAR NVQHYHMKTL GWCDVGYNFL IGEDGLVYEG RGWNFTGAHS GHLWNPMSIG ISFMGNYMDR VPTPQAIRAA QGLLACGVAQ GALRSNYVLK GHRDVQRTLS PGNQLYHLIQ NWPHYRSPHH HHHH

    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.

    Pglyrp1 Protein
  • View Data Sheet

    Name :

    NT 3 Human

    Description:

    Neurotrophin-3 Human Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    Product # :

    CYT-257

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    Description

    Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

    Citations

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.

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

    Neurotrophin 3 Human
  • View Data Sheet

    Name :

    HTLV-1 mosaic

    Description:

    HTLV-1 Mosaic Recombinant

    Product # :

    HIV-144

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    Description

    The E.Coli derived recombinant mosiac protein contains the gp21 and gp46 immunodominant regions, 374-400 amino acids and 190-201 amino acids. The protein is fused with GST at N-terminus.

    Formulation

    20mM Phosphate buffer PH 7.5.

    Purity

    Protein is >95% pure as determined by SDS-PAGE.

    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).

    • Stability

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

    • Applications

      HTLV-1 Mosaic can be used as an antigen in ELISA and Western Blots. Excellent reagent for correct detection of HTLV infections, with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HTLV-I infected individuals

    • Purification Method

      HTLV-1 Mosaic 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 Mosaic
  • 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 :

    Elamipretide

    Description:

    Elamipretide

    SS-31, MTP-131, Bendavia.

    Product # :

    HOR-040

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    Description

    Elamipretide Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 639.79 Dalton and a Molecular formula of C32H49N9O5
    .

    Source

    Synthetic Peptide

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    HPLC, MS

    Elamipretide hplc - Product image 1
    elamipretide mass spec - Product image 2

    Citations

    More Info

    • Synonyms

      SS-31, MTP-131, Bendavia.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

    • Background

      What is the molecular weight/Mw of Elamipretide Protein?
      Elamipretide Protein has a total Mw of 639Da.
      What is the source or expression system of Elamipretide Protein?
      Synthetic peptide

      What is the Purity of Elamipretide Protein?

      Elamipretide Protein is >97% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of Elamipretide Protein?
      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

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

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

      Elamipretide (also known as SS-31) is a novel mitochondrial-targeted peptide with immense promise as a therapeutic agent in mitochondrial dysfunction-related disorders. This research paper aims to provide a comprehensive analysis of Elamipretide, delving into its biochemical properties, mechanisms of action, and potential applications in various disease conditions.

      Elamipretide, a mitochondria-targeting tetrapeptide, has garnered attention for its unique ability to protect mitochondria from oxidative stress and attenuate mitochondrial dysfunction (Siegel et al., 2013). This paper endeavors to explore Elamipretide's biochemical basis and its potential as a therapeutic agent in various diseases linked to mitochondrial impairment.

      Elamipretide selectively accumulates within the inner mitochondrial membrane, where it exerts its cytoprotective effects. By reducing reactive oxygen species (ROS) production and enhancing electron transport chain efficiency, Elamipretide plays a crucial role in mitochondrial homeostasis (Kloner et al., 2015).

      The mitochondrial protective actions of Elamipretide arise from its interaction with cardiolipin, a phospholipid predominantly localized in the inner mitochondrial membrane. By binding to cardiolipin, Elamipretide stabilizes mitochondrial cristae, improves membrane integrity, and enhances oxidative phosphorylation (Minkler et al., 2015).

      Elamipretide's potential applications extend to a myriad of disease conditions characterized by mitochondrial dysfunction. In preclinical studies, Elamipretide has shown promise in mitigating tissue damage following ischemia-reperfusion injury, preserving cardiac function after myocardial infarction, and ameliorating neurodegenerative processes (Birk et al., 2017; Cho et al., 2015).

      As the research on Elamipretide progresses, further investigation is warranted to better understand its pharmacokinetics, long-term safety, and potential off-target effects. Clinical trials exploring its therapeutic efficacy in human diseases offer exciting prospects for the future.

      Elamipretide, a mitochondria-targeting peptide, emerges as a promising candidate in combating mitochondrial dysfunction-related disorders. Its unique ability to stabilize mitochondrial membranes and enhance cellular bioenergetics positions Elamipretide as a novel therapeutic option for a diverse range of diseases.

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

    Elamipretide
  • View Data Sheet

    Name :

    ACADL Human

    Description:

    Acyl-CoA Dehydrogenase, Long Chain, Human Recombinant

    Acyl-CoA dehydrogenase long chain, Acyl-Coenzyme A dehydrogenase long chain, LCAD, ong-chain specific acyl-CoA dehydrogenase mitochondrial, ACAD4, EC 1.3.99.13.

    Product # :

    ENZ-190

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    Description

    ACADL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (31-430) and having a molecular mass of 46.7 kDa.ACADL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ACADL is a homotetramer belonging to the acyl-CoA dehydrogenase family. ACADL takes part in the catabolism of fatty acids and amino acids and is a key source of energy for the heart and skeletal muscle. Mutation in the ACADL gene results in non-ketotic hypoglycemia and hypotonia (muscle weakness).

    • Synonyms

      Acyl-CoA dehydrogenase long chain, Acyl-Coenzyme A dehydrogenase long chain, LCAD, ong-chain specific acyl-CoA dehydrogenase mitochondrial, ACAD4, EC 1.3.99.13.

    • 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 MGGEERLETP SAKKLTDIGI RRIFSPEHDI FRKSVRKFFQ EEVIPHHSEW EKAGEVSREV WEKAGKQGLL GVNIAEHLGG IGGDLYSAAI VWEEQAYSNC SGPGFSIHSG IVMSYITNHG SEEQIKHFIP QMTAGKCIGA IAMTEPGAGS DLQGIKTNAK KDGSDWILNG SKVFISNGSL SDVVIVVAVT NHEAPSPAHG ISLFLVENGM KGFIKGRKLH KMGLKAQDTA ELFFEDIRLP ASALLGEENK GFYYIMKELP QERLLIADVA ISASEFMFEE TRNYVKQRKA FGKTVAHLQT VQHKLAELKT HICVTRAFVD NCLQLHEAKR LDSATACMAK YWASELQNSV AYDCVQLHGG WGYMWEYPIA KAYVDARVQP IYGGTNEIMK ELIAREIVFD K

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    Acadl Human
  • View Data Sheet

    Name :

    HGFR Mouse

    Description:

    Hepatocyte Growth Factor Receptor Mouse Recombinant

    hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

    Product # :

    CYT-1139

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    Description

    HGF Receptor Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 1146 amino acids (25-931aa) and having a molecular mass of 127.8kDa. HGF is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    HGF Receptor protein (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    HGFR Mouse - Product image 1

    Citations

    More Info

    • Introduction

      HGF, also known as scatter factor (SF) and Hepatocyte growth factor, is secreted from mesenchymal cells, targets and acts mainly on epithelial and endothelial cells. The protein is a paracrine cellular growth, motility and morphogenic factor. HGF can also be part of haemopoietic progenitor cells and T cells. HGF has a crucial role in embryonic organ development, mainly in myogenesis. In adults HGF takes part in organ regeneration and wound healing.

    • Synonyms

      hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

    • 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

      ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

    • Background

      What is the molecular weight/Mw of HGFR MOUSE Protein?
      HGFR MOUSE Protein has a total Mw of 127.8kDa.

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

      What is the Purity of HGFR MOUSE Protein?
      HGFR MOUSE Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of HGFR MOUSE Protein?
      ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
      What applications can HGFR MOUSE Protein be used in?
      HGFR MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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


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    Hgf Mouse
  • View Data Sheet

    Name :

    HIBCH Human

    Description:

    3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant

    3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

    Product # :

    ENZ-594

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    Description

    HIBCH Recombinant produced in E. coli is a single polypeptide chain containing 379 amino acids (33-386) and having a molecular mass of 42.1kDa.HIBCH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HIBCH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

    • Synonyms

      3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

    • 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 MGSHMDAAEE VLLEKKGCTG VITLNRPKFL NALTLNMIRQ IYPQLKKWEQ DPETFLIIIK GAGGKAFCAG GDIRVISEAE KAKQKIAPVF FREEYMLNNA VGSCQKPYVA LIHGITMGGG VGLSVHGQFR VATEKCLFAM PETAIGLFPD VGGGYFLPRL QGKLGYFLAL TGFRLKGRDV YRAGIATHFV DSEKLAMLEE DLLALKSPSK ENIASVLENY HTESKIDRDK SFILEEHMDK INSCFSANTV EEIIENLQQD GSSFALEQLK VINKMSPTSL KITLRQLMEG SSKTLQEVLT MEYRLSQACM RGHDFHEGVR AVLIDKDQSP KWKPADLKEV TEEDLNNHFK SLGSSDLKF.

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    Hibch Human
  • View Data Sheet

    Name :

    AKR7A3 Human, His

    Description:

    Aldo-Keto Reductase Family 7 Member A3 Human Recombinant, His Tag

    AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    Product # :

    ENZ-484

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    Description

    AKR7A3 Human Recombinant fused to a 39 amino acids His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 370 amino acids (1-331 a.a.) and having a molecular mass of 41.6 kDa. The AKR7A3 is fused to a 39 amino acid His tag at n-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A3 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately < 0.1 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    Citations

    More Info

    • Introduction

      AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    • Physical Appearance

      Sterile Filtered clear 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 KDRWGSELEM SRQLSRARPA TVLGAMEMGR RMDAPTSAAV TRAFLERGHT EIDTAFVYSE GQSETILGGL GLRLGGSDCR VKIDTKAIPL FGNSLKPDSL RFQLETSLKR LQCPRVDLFY LHMPDHSTPV EETLRACHQL HQEGKFVELG LSNYAAWEVA EICTLCKSNG WILPTVYQGM YNAITRQVET ELFPCLRHFG LRFYAFNPLA GGLLTGKYKY EDKDGKQPVG RFFGNTWAEM YRNRYWKEHH FEGIALVEKA LQAAYGASAP SMTSATLRWM YHHSQLQGAH GDAVILGMSS LEQLEQNLAA AEEGPLEPAV VDAFNQAWHL VAHECPNYFR.

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    Akr7A3 Human
  • View Data Sheet

    Name :

    HP-NAP

    Description:

    Neutrophil-activating protein A Helicobacter Pylori Recombinant

    DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    Product # :

    PRO-2035

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    Description

    HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

    HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

    • Synonyms

      DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.

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    Hp Nap
  • View Data Sheet

    Name :

    NDUFB9 Human

    Description:

    NADH Dehydrogenase 1 Beta Subcomplex 9 Human Recombinant

    NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9, B22, LYRM3, UQOR22, Complex I-B22, CI-B22, LYR motif-containing protein 3, NADH-ubiquinone oxidoreductase B22 subunit, NDUFB9.

    Product # :

    ENZ-740

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    Description

    NDUFB9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-179) and having a molecular mass of 24.2kDa.NDUFB9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFB9 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9 (NDUFB9) which is a part of the complex I LYR family is localized to the internal mitochondrial membrane, as well as to the matrix side of the peripheral membrane. NDUFB9 serves as an accessory subunit of the multi-subunit mitochondrial membrane respiratory chain NADH dehydrogenase complex I. Complex I takes a crucial part in the transfer of electrons from NADH to the respiratory chain, a process which is vital for cellular respiration.

    • Synonyms

      NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9, B22, LYRM3, UQOR22, Complex I-B22, CI-B22, LYR motif-containing protein 3, NADH-ubiquinone oxidoreductase B22 subunit, NDUFB9.

    • 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 MGSMAFLASG PYLTHQQKVL RLYKRALRHL ESWCVQRDKY RYFACLMRAR FEEHKNEKDM AKATQLLKEA EEEFWYRQHP QPYIFPDSPG GTSYERYDCY KVPEWCLDDW HPSEKAMYPD YFAKREQWKK LRRESWEREV KQLQEETPPG GPLTEALPPA RKEGDLPPLW WYIVTRPRER PM.

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    Ndufb9 Human
  • View Data Sheet

    Name :

    NRAS Human

    Description:

    Neuroblastoma RAS Viral Oncogene Homolog Human Recombinant

    GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    Product # :

    PRO-794

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    Description

    NRAS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-186 a.a.) and having a molecular mass of 20.8kDa. The NRAS is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The NRAS protein solution contains 20mM Tris-HCl pH-7.5, 100mM NaCl, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.

    • Synonyms

      GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    • 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

      MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG CMGLPC.

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    Nras Human
  • View Data Sheet

    Name :

    IL2 Human, His

    Description:

    Interleukin-2 Human Recombinant, His Tag

    T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

    Product # :

    CYT-666

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    Description

    Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-2 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-2 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Background

      What is the molecular weight/Mw of IL 2 HUMAN, HIS Protein?
      IL 2 HUMAN, HIS Protein has a total Mw of 20kDa.

      What is the source or expression system of IL 2 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL 2 HUMAN, HIS Protein?
      IL 2 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 HUMAN, HIS Protein?
      The biological functionality of IL 2 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL 2 HUMAN, HIS Protein?
      T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

      What applications can IL 2 HUMAN, HIS Protein be used in?
      IL 2 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 2 HUMAN, HIS Protein?
      The endotoxin level is minimal, IL 2 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 2 HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 2 HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Interleukin 2 Human His
  • View Data Sheet

    Name :

    C19ORF80 Mouse

    Description:

    Chromosome 19 Open Reading Frame 80 Mouse Recombinant

    Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.

    Product # :

    PRO-1576

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    C19ORF80 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 16-198) containing 193 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer, pH-4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.

    • Synonyms

      Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYRA TEARLTEAGH SLGLYDRALE FLGTEVRQGQ DATQELRTSL SEIQVEEDAL HLRAEATARS LGEVARAQQA LRDTVRRLQV QLRGAWLGQA HQEFETLKAR ADKQSHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHTAA LPA.

    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.

    C19Orf80 Mouse
  • View Data Sheet

    Name :

    C19ORF80 Rat

    Description:

    Chromosome 19 Open Reading Frame 80 Rat Recombinant

    Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.

    Product # :

    PRO-2024

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.

    • Synonyms

      Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA

    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.

    C19Orf80 Rat
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