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Search results

1000 results found for “Transforming Growth Factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CFB Human, Native

    Description:

    Complement Factor B Human

    CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.

    Product # :

    PRO-2698

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    Description

    Human Complement Factor B produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 93kDa.

    Source

    Human Plasma.

    Formulation

    CFB protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Complement Factor B Protein
  • View Data Sheet

    Name :

    CTSF Human

    Description:

    Cathepsin-F Human Recombinant

    800x600 CATSF, CLN13, Cathepsin F, EC=3.4.22.41. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    ENZ-738

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    Description

    800x600 CTSF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa.CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTSF solution (1mg/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.

    More Info

    • Introduction

      Cathepsin F ( CTSF) is a member of the peptidase C1 family. Cathepsins are papain familycysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.

    • Synonyms

      CATSF, CLN13, Cathepsin F, EC=3.4.22.41.

    • 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 MGSAPPEWDW RSKGAVTKVK DQGMCGSCWA FSVTGNVEGQ WFLNQGTLLS LSEQELLDCD KMDKACMGGL PSNAYSAIKN LGGLETEDDY SYQGHMQSCN FSAEKAKVYI NDSVELSQNE QKLAAWLAKR GPISVAINAF GMQFYRHGIS RPLRPLCSPW LIDHAVLLVG YGNRSDVPFW AIKNSWGTDW GEKGYYYLHR GSGACGVNTM ASSAVVD.

    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.

    Ctsf Human
  • View Data Sheet

    Name :

    TFRC Human

    Description:

    Transferrin Receptor Human Recombinant

    Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.

    Product # :

    PRO-2180

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    Description

    TFRC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 696 amino acids (89-760 a.a) and having a molecular mass of 77.7 kDa.TFRC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFRC protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

    • Synonyms

      Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.

    • 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 MGSMCKGVEP KTECERLAGT ESPVREEPGE DFPAARRLYW DDLKRKLSEK LDSTDFTGTI KLLNENSYVP REAGSQKDEN LALYVENQFR EFKLSKVWRD QHFVKIQVKD SAQNSVIIVD KNGRLVYLVE NPGGYVAYSK AATVTGKLVH ANFGTKKDFE DLYTPVNGSI VIVRAGKITF AEKVANAESL NAIGVLIYMD QTKFPIVNAE LSFFGHAHLG TGDPYTPGFP SFNHTQFPPS RSSGLPNIPV QTISRAAAEK LFGNMEGDCP SDWKTDSTCR MVTSESKNVK LTVSNVLKEI KILNIFGVIK GFVEPDHYVV VGAQRDAWGP GAAKSGVGTA LLLKLAQMFS DMVLKDGFQP SRSIIFASWS AGDFGSVGAT EWLEGYLSSL HLKAFTYINL DKAVLGTSNF KVSASPLLYT LIEKTMQNVK HPVTGQFLYQ DSNWASKVEK LTLDNAAFPF LAYSGIPAVS FCFCEDTDYP YLGTTMDTYK ELIERIPELN KVARAAAEVA GQFVIKLTHD VELNLDYERY NSQLLSFVRD LNQYRADIKE MGLSLQWLYS ARGDFFRATS RLTTDFGNAE KTDRFVMKKL NDRVMRVEYH FLSPYVSPKE SPFRHVFWGS GSHTLPALLE NLKLRKQNNG AFNETLFRNQ LALATWTIQG AANALSGDVW DIDNEF.

    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.

    Tfrc Human
  • View Data Sheet

    Name :

    PRTFDC1 Human

    Description:

    Phosphoribosyl Transferase Domain Containing 1 Human Recombinant

    Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    Product # :

    ENZ-142

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    Description

    PRTFDC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa.PRTFDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRTFDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

    • Synonyms

      Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      PRTFDC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGSSEE APDYGRGVVI MDDWPGYDLN LFTYPQHYYG DLEYVLIPHG IIVDRIERLA KDIMKDIGYS DIMVLCVLKG GYKFCADLVE HLKNISRNSD RFVSMKVDFI RLKSYRNDQS MGEMQIIGGD DLSTLAGKNV LIVEDVVGTG RTMKALLSNI EKYKPNMIKV ASLLVKRTSR SDGFRPDYAG FEIPNLFVVG YALDYNEYFR DLNHICVINE HGKEKYRV.

    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.

    Prtfdc1 Human
  • View Data Sheet

    Name :

    GSTP1 Human

    Description:

    Glutathione S-Transferase pi 1 Human Recombinant

    Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.

    Product # :

    ENZ-427

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    Description

    GSTP1 Human Recombinant fused with 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-210 a.a.) And having a molecular mass of 27.4kDa. The GSTP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol, 1mM EDTA and 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
      The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

    • Synonyms

      Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.

    • 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 KDRWGSMPPY TVVYFPVRGR CAALRMLLAD QGQSWKEEVV TVETWQEGSL KASCLYGQLP KFQDGDLTLY QSNTILRHLG RTLGLYGKDQ QEAALVDMVN DGVEDLRCKY ISLIYTNYEA GKDDYVKALP GQLKPFETLL SQNQGGKTFI VGDQISFADY NLLDLLLIHE VLAPGCLDAF PLLSAYVGRL SARPKLKAFL ASPEYVNLPI NGNGKQ.

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    Gstp1 Human
  • View Data Sheet

    Name :

    IL-2 Canine

    Description:

    Interleukin-2 Canine Recombinant

    Interleukin-2, IL-2, T-cell growth factor, TCGF.

    Product # :

    CYT-1096

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    Description

    Interleukin-2 Canine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 136 amino acids and having a molecular mass of 15.6kDa. IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 20 mM sodium bicarbonate, pH 8.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as determined by CTLL-2 cell proliferation is <5ng/ml corresponding to a specific activity which is ≥ 2.0 x 10^5 units/mg.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is essential 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 and interleukin 7. The expression of IL2in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the exact expression of a single gene.

    • Synonyms

      Interleukin-2, IL-2, T-cell growth factor, TCGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized IL-2 in Sterile 10 mM sodium bicarbonate, pH 8.5 at 0.1 mg/mL, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPITSSSTK ETEQQMEQLL LDLQLLLNGV NNYENPQLSR MLTFKFYTPK KATEFTHLQC LAEELKNLEE VLGLPQSKNV HLTDTKELIS NMNVTLLKLK GSETSYNCEY DDETATITEF LNKWITFSQS IFSTLT.

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    Canine Il2
  • View Data Sheet

    Name :

    GADD45G Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant

    DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    Product # :

    PRO-570

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    Description

    GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45G protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.

    • Synonyms

      DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    • 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

      MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDIDIVRVGDVQR LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND WVPSITLPE.

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    Gadd45G Human
  • View Data Sheet

    Name :

    MTHFD2 Human

    Description:

    MTHFD2 Human Recombinant

    Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    Product # :

    ENZ-853

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    Description

    MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.

    • Synonyms

      Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    • 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 MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.

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    Mthfd2 Human
  • View Data Sheet

    Name :

    HS3ST1 Human

    Description:

    Heparan Sulfate 3-O-Sulfotransferase 1 Human Recombinant

    Heparan sulfate glucosamine 3-O-sulfotransferase 1, Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1, 3-OST-1, Heparan sulfate 3-O-sulfotransferase 1, h3-OST-1, HS3ST1, 3OST, 3OST1, HS3S1.

    Product # :

    ENZ-744

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    Description

    HS3ST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (21-307 a.a) and having a molecular mass of 36.2kDa.HS3ST1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HS3ST1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heparan Sulfate 3-O-Sulfotransferase 1 (HS3ST1), is sulfotransferase which uses 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. HS3ST1 catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a vital part in the biosynthesis of anticoagulant heparan sulfate since it concludes the structure of the antithrombin pentasaccharide binding site.

    • Synonyms

      Heparan sulfate glucosamine 3-O-sulfotransferase 1, Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1, 3-OST-1, Heparan sulfate 3-O-sulfotransferase 1,
      h3-OST-1, HS3ST1, 3OST, 3OST1, HS3S1.

    • 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 MGSRPAELGQ QELLRKAGTL QDDVRDGVAP NGSAQQLPQT IIIGVRKGGT RALLEMLSLH PDVAAAENEV HFFDWEEHYS HGLGWYLSQM PFSWPHQLTV EKTPAYFTSP KVPERVYSMN PSIRLLLILR DPSERVLSDY TQVFYNHMQK HKPYPSIEEF LVRDGRLNVD YKALNRSLYH VHMQNWLRFF PLRHIHIVDG DRLIRDPFPE IQKVERFLKL SPQINASNFY FNKTKGFYCL RDSGRDRCLH ESKGRAHPQV DPKLLNKLHE YFHEPNKKFF ELVGRTFDWH.

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    Hs3St1 Human
  • View Data Sheet

    Name :

    Transferrin Human, CHO

    Description:

    Transferrin Human Recombinant, CHO

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

    Product # :

    PRO-2782

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    Description

    Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

    Source

    Chinese Hamster Ovary cells.

    Formulation

    Transferrin solution contains 0.05% NaN3 and PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

    • 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.

    • Applications

      Immunoassay, cell culture.

    • Background

      Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.

      The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.

      The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.

      The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.

      By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

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    Transferrin Protein
  • View Data Sheet

    Name :

    IL 3 Mouse

    Description:

    Interleukin-3 Mouse Recombinant

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-371

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    Description

    Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

    More Info

    • Introduction

      Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
      IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 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 IL3 as a Reference Standard.

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    Il 3 Mouse
  • View Data Sheet

    Name :

    KLF12 Human

    Description:

    Kruppel-Like Factor 12 Human Recombinant

    AP-2rep, AP2REP, HSPC122, Krueppel-like factor 12, Transcriptional repressor AP-2rep.

    Product # :

    PRO-2090

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    Description

    KLF12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a) and having a molecular mass of 46.6kDa.KLF12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLF12 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH8.0) ,10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Krueppel-like factor 12 (KLF12) belongs to the Kruppel-like zinc finger protein family and can repress expression of the AP-2 alpha gene by binding to a particular site in the AP-2 alpha gene promoter. AP-2 alpha (Activator protein-2 alpha) is a developmentally-regulated transcription factor and vital regulator of gene expression during vertebrate development and carcinogenesis. KLF12 gene repression entails binding with a corepressor, CtBP1.

    • Synonyms

      AP-2rep, AP2REP, HSPC122, Krueppel-like factor 12, Transcriptional repressor AP-2rep.

    • 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 MGSMNIHMKR KTIKNINTFE NRMLMLDGMP AVRVKTELLE SEQGSPNVHN YPDMEAVPLL LNNVKGEPPE DSLSVDHFQT QTEPVDLSIN KARTSPTAVS SSPVSMTASA SSPSSTSTSS SSSSRLASSP TVITSVSSAS SSSTVLTPGP LVASASGVGG QQFLHIIHPV PPSSPMNLQS NKLSHVHRIP VVVQSVPVVY TAVRSPGNVN NTIVVPLLED GRGHGKAQMD PRGLSPRQSK SDSDDDDLPN VTLDSVNETG STALSIARAV QEVHPSPVSR VRGNRMNNQK FPCSISPFSI ESTRRQRRSE SPDSRKRRIH RCDFEGCNKV YTKSSHLKAH RRTHTGEKPY KCTWEGCTWK FARSDELTRH YRKHTGVKPF KCADCDRSFS RSDHLALHRR RHMLV.

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    Klf12 Human
  • View Data Sheet

    Name :

    TPGS2 Human

    Description:

    Tubulin Polyglutamylase Complex Subunit 2 Human Recombinant

    Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

    Product # :

    PRO-1668

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    Description

    TPGS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 35.7kDa.TPGS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPGS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Tubulin Polyglutamylase Complex Subunit 2 (TPGS2) is a component of the neuronal polyglutamylase complex, which takes part in post-translational addition of glutamate residues to C-terminal tubulin tails. Alternatively spliced transcript variants encoding multiple isoforms have been monitored for TPGS2.

    • Synonyms

      Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

    • 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 MGSMEEEASS PGLGCSKPHL EKLTLGITRI LESSPGVTEV TIIEKPPAER HMISSWEQKN NCVMPEDVKN FYLMTNGFHM TWSVKLDEHI IPLGSMAINS ISKLTQLTQS SMYSLPNAPT LADLEDDTHE ASDDQPEKPH FDSRSVIFEL DSCNGSGKVC LVYKSGKPAL AEDTEIWFLD RALYWHFLTD TFTAYYRLLI THLGLPQWQY AFTSYGISPQ AKQWFSMYKP ITYNTNLLTE ETDSFVNKLD PSKVFKSKNK IVIPKKKGPV QPAGGQKGPS GPSGPSTSST SKSSSGSGNP TRK.

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    Tpgs2 Human
  • View Data Sheet

    Name :

    Leptin tA Mouse, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

    Product # :

    CYT-566

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP 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 Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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 Mouse Peg
  • View Data Sheet

    Name :

    REG1A Human

    Description:

    Regenerating Islet-Derived 1 Alpha Human Recombinant

    Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    Product # :

    PRO-289

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    Description

    The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
      Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

    • Synonyms

      Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.

    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.

    Reg1A Human
  • View Data Sheet

    Name :

    GGCT Human

    Description:

    Gamma-Glutamylcyclotransferase Human Recombinant

    Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.

    Product # :

    ENZ-062

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    Description

    GGCT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188a.a.) and having a molecular mass of 23.2kDa.GGCT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GGCT protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.

    • Synonyms

      Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSHMANSGCKDVT GPDEESFLYF AYGSNLLTER IHLRNPSAAF FCVARLQDFK LDFGNSQGKT SQTWHGGIAT IFQSPGDEVW GVVWKMNKSN LNSLDEQEGV KSGMYVVIEV KVATQEGKEI TCRSYLMTNY ESAPPSPQYK KIICMGAKEN GLPLEYQEKL KAIEPNDYTG KVSEEIEDII KKGETQTL

    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.

    Ggct Human
  • View Data Sheet

    Name :

    Transthyretin Human

    Description:

    Prealbumin Human Recombinant

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

    Product # :

    PRO-771

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    Description

    Transthyertin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (21-147 a.a.) and having a molecular weight of 13.8kDa. The Transthyertin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Transthyertin protein solution contains 1x PBS, pH-7.4, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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, HsT2651.

    • 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

      MGPTGTGESK CPLMVKVLDA VRGSPAINVA VHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA LLSPYSYSTT AVVTNPKE.

    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 Human
  • View Data Sheet

    Name :

    RBP4 Mouse

    Description:

    Retinol Binding Protein-4 Mouse Recombinant, BioActive

    Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    Product # :

    CYT-1158

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    Description

    RBP4 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 191 amino acids (19-201 a.a) and having a molecular mass of 22.4kDa. RBP4 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The RBP4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinol Binding Protein-4 or RBP4, is the retinol currier protein in the plasma. RBP4 takes part on the conversion of retinol to the stable and soluble retinol complex in the plasma. RBP4 carries retinol from the liver tissue where its store to peripheral tissues. RBP-retinol complex has interactions with transthyretin in the plasma, thus prevents its loss by filtration in the kidney.

    • Synonyms

      Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    • 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

      ERDCRVSSFR VKENFDKARF SGLWYAIAKK DPEGLFLQDN IIAEFSVDEK GHMSATAKGR VRLLSNWEVC ADMVGTFTDT EDPAKFKMKY WGVASFLQRG NDDHWIIDTD YDTFALQYSC RLQNLDGTCA DSYSFVFSRD PNGLSPETRR LVRQRQEELC LERQYRWIEH NGYCQSRPSR NSLLEHHHHH H.

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

    Rbp4 Mouse
  • View Data Sheet

    Name :

    C1QTNF6 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 6 Human Recombinant

    CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 6.

    Product # :

    PRO-655

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    Description

    C1QTNF6 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 242 amino acids and having a molecular mass of 27 kDa. The protein contains an extra His tag at N-terminus. The C1QTNF6 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXI9 amino acids 29–259.The C1QTNF6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.23mg/ml in 30mM Acetate Buffer pH-4.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      C1QTNF6 is a collagen type-IV specific for basement membranes. C1QTNF6 is vital for embryonic development.

    • Synonyms

      CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 6.

    • 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.

    • Amino Acid Sequence

      MKHHHHHHAS TFDRAVASGC QRCCDSEDPL DPAHVSSASS SGRPHALPEI RPYINITILK GDKGDPGPMG LPGYMGREGP QGEPGPQGSK GDKGEMGSPG APCQKRFFAF SVGRKTALHS GEDFQTLLFE RVFVNLDGCF DMATGQFAAP LRGIYFFSLN VHSWNYKETY VHIMHNQKEA VILYAQPSER SIMQSQSVML DLAYGDRVWV RLFKRQRENA IYSNDFDTYI TFSGHLIKAEDD.

    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.

    C1Qtnf6 Human
  • View Data Sheet

    Name :

    ARF5 Human

    Description:

    ADP-Ribosylation Factor 5 Human Recombinant

    ADP-ribosylation factor 5, ARF5.

    Product # :

    PRO-245

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    Description

    ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARF5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor 5 (ARF5) is a small guanine nucleotide-binding protein which enhances the enzymatic activities of cholera toxin. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the connection of actin to the golgi via rho family-dependent G-protein localization and WASP/Arp2/3 complexes. ARF5 is involved in vesicular transport and functioning via phospholipase D activation.

    • Synonyms

      ADP-ribosylation factor 5, ARF5.

    • 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 MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
      TQGTGLYDGL DWLSHELSKR.

    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.

    Arf5 Human
  • View Data Sheet

    Name :

    TROVE2 Bovine, Biotin

    Description:

    TROVE Domain Family Member 2 Human Recombinant, Biotinlyated

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-2561

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    Description

    TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

    Source

    Bovine tissues.

    Formulation

    TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 83.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • 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.

    Ro60 Bovine
  • View Data Sheet

    Name :

    IL 2 Porcine

    Description:

    Interleukin-2 Porcine Recombinant

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

    Product # :

    CYT-397

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    Description

    Interleukin2 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 15217 Dalton. The IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

    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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-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 IL 2 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APTSSSTKNT KKQLEPLLLD LQLLLKEVKN YENADLSRML TFKFYMPKQA TELKHLQCLV EELKALEGVL NLGQSKNSDS ANIKESMNNI NVTVLELKGS ETSFKCEYDD ETVTAVEFLN KWITFCQSIY STLT.

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

    Il 2 Porcine
  • View Data Sheet

    Name :

    ATF Bovine

    Description:

    Apo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    Product # :

    PRO-511

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    Description

    Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.

    Source

    Bovine Serum.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    • Physical Appearance

      Sterile Filtered off-white lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.

    • Solubility

      It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.

    • Iron Content

      The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.

    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.

    Apo Transferrin Bovine
  • View Data Sheet

    Name :

    INSR Human

    Description:

    Insulin Receptor Human Recombinant

    Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.

    Product # :

    CYT-777

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    Description

    Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.The Human INSR is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    INSR was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Insulin Receptor (INSR) is a receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Once the precursor signal peptide is removed, the insulin receptor precursor is post-translationally cleaved into 2 chains (alpha and beta) which are covalently linked. Insulin binding initiates phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins function as docking proteins for other signaling proteins which contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2.

    • Synonyms

      Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.

    • 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.

    • Solubility

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

    • Amino Acid Sequence

      ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK LHHHHHH.

    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.

    Insr Human
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