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    Betacellulin

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Search results

1000 results found for “sirtuin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    NPL Human

    Description:

    N-acetylneuraminate Pyruvate Lyase Human Recombinant

    N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    Product # :

    ENZ-125

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    Description

    NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.

    • Synonyms

      N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    • 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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.

    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.

    Npl Human
  • View Data Sheet

    Name :

    STAR Human

    Description:

    Steroidogenic Acute Regulatory Protein Human Recombinant

    Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.

    Product # :

    PRO-979

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    Description

    STAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (64-285) and having a molecular mass of 27.1 kDa.STAR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STAR facilitates the fast increase in pregnenolone synthesis stimulated by tropic hormones. STAR increases pregnenolone synthesis more than four-fold and a major STAR transcription of 1.6 kb is observed in ovary and testis. Throughout the growth and differentiation period of the ovary follicle, the immunoreactivity is likely to move from the granulosa cells of early antral follicles to the theca cell layers in the adult.

    • Synonyms

      Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEETLYSDQE LAYLQQGEEA MQKALGILSN QEGWKKESQQ DNGDKVMSKV VPDVGKVFRL EVVVDQPMER LYEELVERME AMGEWNPNVK EIKVLQKIGK DTFITHELAA EAAGNLVGPR DFVSVRCAKR RGSTCVLAGM ATDFGNMPEQ KGVIRAEHGP TCMVLHPLAG SPSKTKLTWL LSIDLKGWLP KSIINQVLSQ TQVDFANHLR KRLESHPASE ARC

    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.

    Star Human
  • View Data Sheet

    Name :

    IMP3 Human

    Description:

    IMP3 Human Recombinant

    BRMS2, C15orf12, MRPS4, U3 snoRNP protein IMP3.

    Product # :

    PRO-015

    Price :

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    • description
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    Description

    IMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184 a.a) and having a molecular mass of 24kDa. IMP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IMP3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      IMP3 is the human homolog of the yeast Imp3 protein and Essential for the early cleavages during pre-18S ribosomal RNA processing. IMP3 is a Part of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). IMP3 is a member of to the ribosomal protein S4P family and localizes to the nucleoli and interacts with the U3 snoRNP complex. IMP3 contains an S4 domain. U3 small nucleolar ribonucleoprotein protein IMP3 is a protein which in humans is encoded by the IMP3 gene.

    • Synonyms

      BRMS2, C15orf12, MRPS4, U3 snoRNP protein IMP3.

    • 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 MGSMVRKLKF HEQKLLKQVD FLNWEVTDHN LHELRVLRRY RLQRREDYTR YNQLSRAVRE LARRLRDLPE RDQFRVRASA ALLDKLYALG LVPTRGSLEL CDFVTASSFC RRRLPTVLLK LRMAQHLQAA VAFVEQGHVR VGPDVVTDPA FLVTRSMEDF VTWVDSSKIK RHVLEYNEER DDFDLEA.

    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.

    Imp3 Human
  • View Data Sheet

    Name :

    KRT16 Human

    Description:

    Cytokeratin 16 Human Recombinant

    Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    Product # :

    PRO-1899

    Price :

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    • description
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    Description

    KRT16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-473) and having a molecular mass of 53.7 kDa.KRT16 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT16 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

      Cytokeratin 16, also known as KRT16, is a member of the keratin gene family. KRT16 which acts as a regulator of innate immunity in response to skin barrier breach is required for some inflammatory checkpoint for the skin barrier maintenance. KRT16 is coexpressed with keratin 14 in a few epithelial tissues as esophagus, tongue, and hair follicles.

    • Synonyms

      Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    • 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 MGSMTTCSRQ FTSSSSMKGS CGIGGGIGGG SSRISSVLAG GSCRAPSTYG GGLSVSSRFS SGGACGLGGG YGGGFSSSSS FGSGFGGGYG GGLGAGFGGG LGAGFGGGFA GGDGLLVGSE KVTMQNLNDR LASYLDKVRA LEEANADLEV KIRDWYQRQR PSEIKDYSPY FKTIEDLRNK IIAATIENAQ PILQIDNARL AADDFRTKYE HELALRQTVE ADVNGLRRVL DELTLARTDL EMQIEGLKEE LAYLRKNHEE EMLALRGQTG GDVNVEMDAA PGVDLSRILN EMRDQYEQMA EKNRRDAETW FLSKTEELNK EVASNSELVQ SSRSEVTELR RVLQGLEIEL QSQLSMKASL ENSLEETKGR YCMQLSQIQG LIGSVEEQLA QLRCEMEQQS QEYQILLDVK TRLEQEIATY RRLLEGEDAH LSSQQASGQS YSSREVFTSS SSSSSRQTRP ILKEQSSSSF SQGQSS.

    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.

    Krt16 Human
  • View Data Sheet

    Name :

    KRT17 Human

    Description:

    Cytokeratin 17 Human Recombinant

    Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    Product # :

    PRO-1883

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    Description

    KRT17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432 a.a) and having a molecular mass of 50.5kDa.KRT17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 17 also known as KRT17 is a type I cytokeratin. KRT17 is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in KRT17 lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex. KRT17 takes part in the formation and maintenance of a variety of skin appendages, particularly in determining shape and orientation of hair. KRT17 also modulates the function of TNF-alpha in the precise context of hair cycling. Moreover, KRT17 regulates protein synthesis and epithelial cell growth all through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.

    • Synonyms

      Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTTSIRQ FTSSSSIKGS SGLGGGSSRT SCRLSGGLGA GSCRLGSAGG LGSTLGGSSY SSCYSFGSGG GYGSSFGGVD GLLAGGEKAT MQNLNDRLAS YLDKVRALEE ANTELEVKIR DWYQRQAPGP ARDYSQYYRT IEELQNKILT ATVDNANILL QIDNARLAAD DFRTKFETEQ ALRLSVEADI NGLRRVLDEL TLARADLEMQ IENLKEELAY LKKNHEEEMN ALRGQVGGEI NVEMDAAPGV DLSRILNEMR DQYEKMAEKN RKDAEDWFFS KTEELNREVA TNSELVQSGK SEISELRRTM QALEIELQSQ LSMKASLEGN LAETENRYCV QLSQIQGLIG SVEEQLAQLR CEMEQQNQEY KILLDVKTRL EQEIATYRRL LEGEDAHLTQ YKKEPVTTRQ VRTIVEEVQD GKVISSREQV HQTTR

    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.

    Krt17 Human
  • View Data Sheet

    Name :

    Leptin Super Antagonist Human

    Description:

    Leptin Super Antagonist Human Recombinant

    Product # :

    CYT-1238

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    Description

    Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C 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 Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, 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.

    • Background

      Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    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 Antagonist Super Human
  • View Data Sheet

    Name :

    CEBP Gamma Human

    Description:

    CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human

    CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    Product # :

    PRO-434

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    Description

    CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.

    • Synonyms

      CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.

    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.

    Cebpg 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.

    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.

    Gstp1 Human
  • View Data Sheet

    Name :

    GSTT1 Human

    Description:

    Glutathione S-Transferase Theta-1 Human Recombinant

    Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    Product # :

    ENZ-429

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    Description

    GSTT1 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 277 amino acids (1-240 a.a.) and having a molecular mass of 31.5kDa.The GSTT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTT1 solution contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung.
      The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer.

    • Synonyms

      Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    • 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 KDRWGSHMGL ELYLDLLSQP CRAVYIFAKK NDIPFELRIV DLIKGQHLSD ACAQVNPLKK VPALKDGDFT LTESVAILLY LTRKYKVPDY WYPQDLQARA RVDEYLAWQH TTLRRSCLRA LWHKVMFPVF LGEPVSPQTL AATLAELDVT LQLLEDKFLQ NKAFLTGPHI SLADLVAITE LMHPVGAGCQ VFEGRPKLAT WRQRVEAAVG EDLFQEAHEV ILKAKDFPPA DPTIKQKLMP WVLAMIR.

    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.

    Gstt1 Human
  • View Data Sheet

    Name :

    GSTZ1 Human

    Description:

    Glutathione Transferase Zeta 1 Human Recombinant

    MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    Product # :

    ENZ-494

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    Description

    GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.

    • Synonyms

      MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    • 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 MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.

    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.

    Gstz1 Human
  • View Data Sheet

    Name :

    GTSF1 Human

    Description:

    Gametocyte Specific Factor 1 Human Recombinant

    Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    Product # :

    PRO-561

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    Description

    GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.

    • Synonyms

      Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    • 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 MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.

    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.

    Gtsf1 Human
  • View Data Sheet

    Name :

    MCTS1 Human

    Description:

    Malignant T-Cell-Amplified Sequence 1 Human Recombinant

    MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    Product # :

    PRO-1387

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    Description

    MCTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 204 amino acids (1-181 a.a.) and having a molecular mass of 22.9kDa. MCTF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MCTF1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Malignant T cell amplified sequence 1 (MCTS1) is an Anti-oncogene which takes part in cell cycle regulation by means of decreasing cell doubling time and encouraging-dependent growth and also by shorting the duration of G1 transit time and G1/S transition. MCTS1 also plays a role as translation enhancer. MCTS1 recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, thereupon altering the mRNA translation profile; Up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant.

    • Synonyms

      MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    • 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 MGSMFKKFDE KENVSNCIQL KTSVIKGIKN QLIEQFPGIE PWLNQIMPKK DPVKIVRCHE HIEILTVNGE LLFFRQREGP FYPTLRLLHK YPFILPHQQV DKGAIKFVLS GANIMCPGLT SPGAKLYPAA VDTIVAIMAE GKQHALCVGV MKMSAEDIEK VNKGIGIENI HYLNDGLWHM KTYK.

    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.

    Mcts1 Human
  • View Data Sheet

    Name :

    WWTR1 Human

    Description:

    WW Domain Containing Transcription Regulator 1 Human Recombinant

    WW domain-containing transcription regulator protein 1, Transcriptional coactivator with PDZ-binding motif, WWTR1, WW Domain Containing Transcription Regulator 1, TAZ.

    Product # :

    PRO-1814

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    Description

    WWTR1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 46.5 kDa.WWTR1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWTR1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      WW Domain Containing Transcription Regulator 1 (WWTR1) is a transcriptional coactivator that plays a role as a downstream regulatory target in the Hippo signaling pathway which participates in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. WWTR1 regulates the nuclear accumulation of SMADS and has a main part in coupling them to the transcriptional machinery like the mediator complex. WWTR1 is also regulates embryonic stem-cell self-renewal.

    • Synonyms

      WW domain-containing transcription regulator protein 1, Transcriptional coactivator with PDZ-binding motif, WWTR1, WW Domain Containing Transcription Regulator 1, TAZ.

    • 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 MGSMNPASAP PPLPPPGQQV IHVTQDLDTD LEALFNSVMN PKPSSWRKKI LPESFFKEPD SGSHSRQSST DSSGGHPGPR LAGGAQHVRS HSSPASLQLG TGAGAAGSPA QQHAHLRQQS YDVTDELPLP PGWEMTFTAT GQRYFLNHIE KITTWQDPRK AMNQPLNHMN LHPAVSSTPV PQRSMAVSQP NLVMNHQHQQ QMAPSTLSQQ NHPTQNPPAG LMSMPNALTT QQQQQQKLRL QRIQMERERI RMRQEELMRQ EAALCRQLPM EAETLAPVQA AVNPPTMTPD MRSITNNSSD PFLNGGPYHS REQSTDSGLG LGCYSVPTTP EDFLSNVDEM DTGENAGQTP MNINPQQTRF PDFLDCLPGT NVDLGTLESE DLIPLFNDVE SALNKSEPFL TWL.

    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.

    Wwtr1 Human
  • View Data Sheet

    Name :

    CRADD Human

    Description:

    Caspase and RIP Adapter with Death Domain Human Recombinant

    RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    Product # :

    PRO-465

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    Description

    CRADD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.9 kDa. CRADD is fused to a 20 amino acids His-Tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CRADD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRADD is a 22kDa, widely-expressed cytosolic adaptor/signaling protein that induces cell apoptosis/cell death in numerous tissues. CRADD is a death domain (CARD) that recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes TNFR1A, RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.

    • Synonyms

      RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    • 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 MEARDKQVLR SLRLELGAEV LVEGLVLQYL YQEGILTENH IQEINAQTTG LRKTMLMLDI LPSRGPKAFD TFLDSLQEFP WVREKLKKAR EEAMTDLPAG DRLTGIPSHI LNSSPSDRQI NQLAQRLGPE WEPMVLSLGL SQTDIYRCKA NHPHNVQSQV VEAFIRWRQR FGKQATFQSL HNGLRAVEVD PSLLLHMLE.

    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.

    Cradd Human
  • View Data Sheet

    Name :

    ZNHIT1 Human

    Description:

    Zinc Finger HIT-Type Containing 1 Human Recombinant

    Zinc Finger HIT-Type Containing 1, ZNHIT1, ZNFN4A1, Zinc Finger Protein, Subfamily 4A (HIT Domain Containing) Member 1, Zinc Finger HIT Domain Containing 1, Putative Cyclin G1 Interacting Protein, Cyclin-G1-Binding Protein 1, Zinc Finger Protein Subfamily 4A Member 1, P18 Hamlet, CG1I, H_DJ0747G18.14, p18Hamlet, Zinc Finger HIT Domain-Containing Protein 1, Zinc Finger HIT Type 1, CGBP1.

    Product # :

    PRO-1448

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    Description

    ZNHIT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-154) and having a molecular mass of 19.9kDa. ZNHIT1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The ZNHIT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zinc Finger HIT-Type Containing 1 (ZNHIT1) is a member of the ZNHIT1 family and contains 1 HIT-type zinc finger. The ZNHIT1 protein is induced by DNA damage and appears to have a role in p53-mediated apoptosis induction. ZNHIT1 interacts with MAPK11 and MAPK14 and is a component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1. ZNHIT1 binds to NR1D2 and discharges it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity.

    • Synonyms

      Zinc Finger HIT-Type Containing 1, ZNHIT1, ZNFN4A1, Zinc Finger Protein, Subfamily 4A (HIT Domain Containing) Member 1, Zinc Finger HIT Domain Containing 1, Putative Cyclin G1 Interacting Protein, Cyclin-G1-Binding Protein 1, Zinc Finger Protein Subfamily 4A Member 1, P18 Hamlet, CG1I, H_DJ0747G18.14, p18Hamlet, Zinc Finger HIT Domain-Containing Protein 1, Zinc Finger HIT Type 1, CGBP1.

    • 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 MGSMVEKKTS VRSQDPGQRR VLDRAARQRR INRQLEALEN DNFQDDPHAG LPQLGKRLPQ FDDDADTGKK KKKTRGDHFK LRFRKNFQAL LEEQNLSVAE GPNYLTACAG PPSRPQRPFC AVCGFPSPYT CVSCGARYCT VRCLGTHQET RCLKWTV.

    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.

    Znhit1 Human
  • View Data Sheet

    Name :

    S100G Rat

    Description:

    S100 Calcium Binding Protein G Rat Recombinant

    Protein S100-G, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, Calbindin-D9k, 9 kDa CaBP, Cholecalcin, S100g, Calb3, S100d, Cbpi, MGC72928, Rncalbd9.

    Product # :

    PRO-399

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    Description

    CaBP9K is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution (1mg/ml) containing 100mM Phosphate buffer, pH 7.3.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

    • Synonyms

      Protein S100-G, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, Calbindin-D9k, 9 kDa CaBP, Cholecalcin, S100g, Calb3, S100d, Cbpi, MGC72928, Rncalbd9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CABP9K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CABP9K 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 CABP9K in sterile 18MΩ-cm H2O not less than 100µg/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.

    S100G Rat
  • View Data Sheet

    Name :

    PSIP1 Human

    Description:

    PC4 And SFRS1 Interacting Protein 1 Human Recombinant

    PC4 and SFRS1 Interacting Protein 1, Lens Epithelium-Derived Growth Factor, Transcriptional Coactivator P75/P52, Dense Fine Speckles 70 KDa Protein, CLL-Associated Antigen KW-7, DFS 70, PSIP2, DFS70, LEDGF, PC4 And SFRS1 Interacting Protein 2, Transcriptional Coactivator P52/P75, PAIP, P52, P75, PSIP1.

    Product # :

    PRO-2267

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    Description

    Recombinant Human PSIP1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 71 kDa. PSIP1 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PSIP1 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 84.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PC4 and SFRS1 Interacting Protein 1 (PSIP1) is a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. PSIP1 is also involved particularly in lens epithelial cell gene regulation and stress responses. PSIP1 has a significant role in lens epithelial to fiber cell terminal differentiation. In addition, PSIP1 plays a protective role during stress-induced apoptosis. Furthermore, PSIP1 is a cellular cofactor for lentiviral integration.

    • Synonyms

      PC4 and SFRS1 Interacting Protein 1, Lens Epithelium-Derived Growth Factor, Transcriptional Coactivator P75/P52, Dense Fine Speckles 70 KDa Protein, CLL-Associated Antigen KW-7, DFS 70, PSIP2, DFS70, LEDGF, PC4 And SFRS1 Interacting Protein 2, Transcriptional Coactivator P52/P75, PAIP, P52, P75, PSIP1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG type human auto-antibodies.2. Immunodot test with positive/negative samples.

    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.

    Psip1 Human
  • View Data Sheet

    Name :

    KRT20 Human

    Description:

    Cytokeratin 20 Human Recombinant

    Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

    Product # :

    PRO-351

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    Description

    Cytokeratin 20 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain having a molecular mass of 48,553 Dalton. The KRT20 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.

    • Synonyms

      Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT20 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 KRT20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

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

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

    Krt20 Human
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor 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.

    Bdnf Human
  • View Data Sheet

    Name :

    SEPSECS Mouse

    Description:

    Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant

    AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS. 

    Product # :

    ENZ-1081

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    Description

    SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 527 amino acids (1-504 a.a.) and having a molecular mass of 57.7kDa.SEPSECS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEPSECS protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 0.2M NaCl and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.

    • Synonyms

      AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.

    • 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 MGSMNPESFA AGERRVSPAY VRQGCEARRA HEHLIRLLLE QGKCPEDGWD ESTLELFLHE LAVMDSNNFL GNCGVGEREG RVASALVARR HYRFIHGIGR SGDISAVQPK AAGSSLLNKI TNSLVLNVIK LAGVHSVASC FVVPMATGMS LTLCFLTLRH

      KRPKAKYIIW PRIDQKSCFK SMVTAGFEPV VIENVLEGDE LRTDLKAVEA KIQELGPEHI LCLHSTTACF APRVPDRLEE LAVICANYDI PHVVNNAYGL QSSKCMHLIQ QGARVGRIDA FVQSLDKNFM VPVGGAIIAG FNEPFIQDIS KMYPGRASAS PSLDVLITLL SLGCSGYRKL

      LKERKEMFVY LSTQLKKLAE AHNERLLQTP HNPISLAMTL KTIDGHHDKA VTQLGSMLFT RQVSGARAVP LGNVQTVSGH TFRGFMSHAD NYPCAYLNAA AAIGMKMQDV DLFIKRLDKC LNIVRKEQTR ASVVSGADRN KAEDADIEEM ALKLDDVLGD VGQGPAL.

    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.

    Sepsecs Mouse
  • View Data Sheet

    Name :

    ProInsulin Human

    Description:

    ProInsulin C-Peptide Analogue Human Recombinant

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN. 

    Product # :

    CYT-1120

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    Description

    ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

    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.

    Proinsulin C Peptide
  • View Data Sheet

    Name :

    sRANKL Human, GST

    Description:

    Soluble RANK Ligand Human Recombinant, GST tag

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-631

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    Description

    RANKL Human Recombinant fused to GST tag produced in E.Coli is a single, non-glycosylated polypeptide having a molecular mass of 47 kDa. RANKL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The soluble RANKL protein solution contains 1mM EDTA and PBS pH-7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. By injecting soluble RANKL, novel osteopenia model mice were established in only 50 hours. Degree of bone loss can be controlled by changing doses of sRANKL. RANKL can be used in establishing osteopenia model for in vivo screening of drugs for osteoporosis, determination of effect and mechanism, evaluation of bone anabolic drugs.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered colorelss 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.

    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.

    Rankl Human Gst
  • View Data Sheet

    Name :

    NAIF1 Human

    Description:

    Nuclear Apoptosis Inducing Factor 1 Human Recombinant

    bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    Product # :

    PRO-1978

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    Description

    NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

    • Synonyms

      bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    • 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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

    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.

    Naif1 Human
  • View Data Sheet

    Name :

    EREG Human, HEK

    Description:

    Epiregulin Human Recombinant, HEK

    EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    Product # :

    CYT-1206

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    Description

    EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

    More Info

    • Introduction

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

    • Synonyms

      EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    • 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

      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 32.6kDa.

      What is the source or expression system of EREG Protein?
      HEK293 cells.

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

      What is the Biological Activity of EREG Protein?
      Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

      What is the amino acid sequence of EREG Protein?
      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

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

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

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

    Ereg Human
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