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Search results

1000 results found for “Sirtuin”

Name

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  • View Data Sheet

    Name :

    GALM Human

    Description:

    Galactose Mutarotase Human Recombinant

    Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    Product # :

    ENZ-541

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    Description

    GALM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-342 a.a.) and having a molecular mass of 39.9 kDa. The GALM is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALM solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALM is a main enzyme of carbohydrate metabolism catalysing the translation of beta-D-galactose to alpha-D-galactose. GALM is needed for normal galactose metabolism by preserveing the equilibrium of alpha and beta anomers of galactose. GALM is required for the production of complex oligosaccharides.

    • Synonyms

      Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    • 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 MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA.

    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.

    Galm Human
  • View Data Sheet

    Name :

    GAS7 Human

    Description:

    Growth Arrest-Specific 7 Isoform b Human Recombinant

    GAS7, GAS-7, Growth arrest-specific protein 7, KIAA0394, MGC1348, MLL/GAS7.

    Product # :

    PRO-680

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    Description

    GAS7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-416a.a.) and having a molecular mass of 49.8 kDa.GAS7 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GAS7 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GAS7 is mainly expressed in terminally differentiated brain cells and predominantly in mature cerebellar Purkinje neurons. GAS7 is involved in neuronal development by promoting maturation and morphological differentiation of cerebellar neurons. Inhibition of GAS7 production in terminally differentiating cultures of embryonic murine cerebellum impedes neurite outgrowth. Over-expression of GAS7 initiats the development of human osteosarcoma.

    • Synonyms

      GAS7, GAS-7, Growth arrest-specific protein 7, KIAA0394, MGC1348, MLL/GAS7.

    • 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 MKPGMVPPPP GEESQTVILP PGWQSYLSPQ GRRYYVNTTT NETTWERPSS SPGIPASPGS HRSSLPPTVN GYHASGTPAH PPETAHMSVR KSTGDSQNLG SSSPSKKQSK ENTITINCVT FPHPDTMPEQ QLLKPTEWSY CDYFWADKKD PQGNGTVAGF ELLLQKQLKG KQMQKEMSEF IRERIKIEED YAKNLAKLSQ NSLASQEEGS LGEAWAQVKK SLADEAEVHL KFSAKLHSEV EKPLMNFREN FKKDMKKCDH HIADLRKQLA SRYASVEKAR KALTERQRDL EMKTQQLEIK LSNKTEEDIK KARRKSTQAG DDLMRCVDLY NQAQSKWFEE MVTTTLELER LEVERVEMIR QHLCQYTQLR HETDMFNQST VEPVDQLLRK VDPAKDRELW VREHKTGNIR PVDMEI.

    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.

    Gas7 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

    Price :

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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 :

    PRKACA Human

    Description:

    cAMP-Dependent Protein Kinase A catalytic subunit α Human Recombinant

    cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    Product # :

    PKA-200

    Price :

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    Description

    cAMP-dependent PKA is an ubiquitous serine/threonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catalytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant PKA catalytic subunit a is a 41kDa protein. The a-isoform is the predominant form with a broad tissue distribution and can be used for in vitro enzymological studies of neural and hormonal signal transduction or to phosphorylate target proteins in vivo including Ion channels, transcriptional activator proteins and regulatory enzymes of glycogen metabolism.

    Source

    Escherichia Coli.

    Formulation

    PKA catalytic subunit a is supplied in a buffer containing 20mM MOPS pH7, 150mM NaCl, 1mM DTT, 1mM EDTA and 50% Glycerin.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Synonyms

      cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    • 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

      MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE F.

    • Assay Conditions

      Roskoski-AssayProtein kinase activity can be measured using a modified radioactive assay according to Roskoski et al.The assay will be performed in a mixture containing 50mM MOPS (pH7.0), 10mM MgCI2, 0.25 mg/ml bovine serum albumin, 100 IJM Kemptide (peptide substrate), 100 IJM unlabeled ATP mixed with [y_32p] ATP (500-1000 cpm/pmol) and Ca subunit in a final volume of 50 IJI. Reaction is started by addition of the Ca subunit and can be stopped after 5 minutes incubation at 30°C by spotting the reaction mix onto Whatman P-81 filters and soaking the filters four times in 75mM phosphoric acid (10 ml per sample) for at least 5 minutes. After four washing steps rinse filters with ethanol, dry and count. Roskoski, R., Jr. (1983) Methods Enzymol. 99, 3-6For the detection of phosphorylation in substrate proteins the phosphotransferase reaction can alternatively be stopped by taking aliquots of the mixture and adding SDS sample buffer. The phosphorylation status of the substrate proteins can subsequently be analysed using SDS PAGE and autoradiography. Zimmermann, B. (1999) Journal of Biological Chemistry.274, 9, 5370-78.

    • Unit Definition

      One unit is defined as the amount of cAMP-Dependent Protein Kinase, recombinant C? catalytic subunit, required to incorporate 1 pmol of phosphate into the specific substrate peptide kemptide (LRRASLG) in one minute at 30°C.

    • Specific Activity

      The specific activity of the recombinant PKA catalytic subunit alpha, is >10,000,000 U/mg.

    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.

    Prkaca
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

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    CYT-509

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

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

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain 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.

    Leptin Receptor Chicken
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Granulysin protein was lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    CHMP2B Human

    Description:

    Chromatin Modifying Protein 2B Human Recombinant

    Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    Product # :

    PRO-877

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    Description

    CHMP2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-213) and having a molecular mass of 26.1 kDa.The CHMP2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHMP2B protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.

    • Synonyms

      Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    • 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 MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD EEIERQLKAL GVD

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    Chmp2B Human
  • View Data Sheet

    Name :

    CISD1 Human

    Description:

    CDGSH Iron Sulfur Domain 1 Human Recombinant

    CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.

    Product # :

    PRO-1221

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    Description

    CISD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 100 amino acids (32-108) and having a molecular mass of 11.4 kDa.CISD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CISD1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CISD1 protein holds a CDGSH iron-sulfur domain and is known to bind a redox-active [2Fe-2S] cluster. CISD1 is restricted to the outer membrane of mitochondria and takes part in oxidation regulation.

    • Synonyms

      CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.

    • 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 MGSKRFYVKD HRNKAMINLH IQKDNPKIVH AFDMEDLGDK AVYCRCWRSK KFPFCDGAHT KHNEETGDNV GPLIIKKKET

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    Cisd1 Human
  • View Data Sheet

    Name :

    UCHL5 Human

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L5 Human Recombinant

    Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.

    Product # :

    ENZ-097

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    Description

    UCHL5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing349 amino acids (1-329a.a.) and having a molecular mass of 39.7kDa.UCHL5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UCHL5 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 200mM NaCl, 0.1mM PMSF, 2mM EDTA and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 500 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at
     pH 8.0, at 37°C.

    More Info

    • Introduction

      UCHL5 is a member of the peptidase C12 family. UCHL5 protein is a protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains, and deubiquitinating enzyme related to the 19S regulatory subunit of the 26S proteasome.

    • Synonyms

      Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.

    • 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

      MGSSHHHHHHSSGLVPRGSH MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL KTLAEHQQLI PLVEKAKEKQ NAKKAQETK

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    Uchl5 Human
  • View Data Sheet

    Name :

    CLTA Human

    Description:

    Clathrin, Light Chain A Human Recombinant

    Clathrin light chain A, Lca, CLTA.

    Product # :

    PRO-1144

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    Description

    CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.

    • Synonyms

      Clathrin light chain A, Lca, CLTA.

    • 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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
      TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.

    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.

    Clta Human
  • View Data Sheet

    Name :

    Visfatin Human

    Description:

    Visfatin Human Recombinant

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    CYT-318

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    Description

    Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.

    Source

    Escherichia Coli.

    Formulation

    Visfatin was lyophilized with no additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.

    More Info

    • Introduction

      Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
      Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

      Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.

    • Amino Acid Sequence

      MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.

    • Background

      About Visfatin Human


      Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
      element that synergized with stem cell factors and IL-7. One of its main functions is to
      enhance the development of B cell precursors.

      The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
      identified in vertebrates, including mice and humans, and it’s being studied due to its link
      to inflammatory conditions, beta cell function, and cardiovascular disease.


      What’s the Function of Visfatin Human Recombinant?

      Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
      polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
      chromatography, and it contains a total molecular mass of 52.6 kDa.


      What Are the Main Applications of Visfatin Human Recombinant?

      The cytokine is being researched because of its involvement in glucose homeostasis,
      dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
      Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
      experts can get further answers regarding the cytokine’s involvement in different
      processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
      atherosclerosis.

      Findings can also help during the identification of high-risk people for cardiovascular
      disease and diabetes.

    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.

    Visfatin Human
  • View Data Sheet

    Name :

    VPS24 Human

    Description:

    Vacuolar Protein Sorting 24 Human Recombinant

    Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    Product # :

    PRO-872

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    Description

    VPS24 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-222 a.a) and having a molecular mass of 27.2kDa (Molecular weight on SDS-PAGE will appear higher).VPS24 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VPS24 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Charged multivesicular body protein 3 (VPS24/CHMP3) is a member of the vacuolar sorting protein family and function as chromatin modifying proteins. VPS24 links directly with CHMP2 and CHMP4 for the disassembly of ESCRT-III complex in an ATP-dependent manner. During HIV-1 infection, the virus uses the ESCRT-III complex to mediate budding and exocytosis of viral proteins. VPS24 overexpression strongly hinders HIV-1 release.

    • Synonyms

      Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    • 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 MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS.

    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.

    Vps24 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.

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    Znhit1 Human
  • View Data Sheet

    Name :

    Leptin Human, Mutant

    Description:

    Leptin Mutant D23L Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1243

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    Description

    Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Mutant D23L 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 Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    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.

    Mutant Leptin
  • View Data Sheet

    Name :

    ORM1

    Description:

    Orosomucoid 1 Human Recombinant

    Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.

    Product # :

    PRO-889

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    Description

    ORM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (19-201) and having a molecular mass of 21.7 kDa.The ORM1 is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ORM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

    • Synonyms

      Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 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

      MQIPLCANLV PVPITNATLD QITGKWFYIA SAFRNEEYNK SVQEIQATFF YFTPNKTEDT IFLREYQTRQ DQCIYNTTYL NVQRENGTIS RYVGGQEHFA HLLILRDTKT YMLAFDVNDE KNWGLSVYAD KPETTKEQLG EFYEALDCLR IPKSDVVYTD WKKDKCEPLE KQHEKERKQE EGES.

    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.

    Orm1 Human
  • View Data Sheet

    Name :

    SORD Human, His

    Description:

    Sorbitol Dehydrogenase Human Recombinant, His Tag

    EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    Product # :

    ENZ-520

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    Description

    SORD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 377 amino acids (1-357 a.a.) and having a molecular mass of 40.4 kDa. SORD protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SORD protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

    • Synonyms

      EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    • 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 MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP.

    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.

    Sord Human
  • View Data Sheet

    Name :

    Bartonella 17kDa

    Description:

    Bartonella Henselae 17kDa Recombinant

    Product # :

    PRO-2568

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    Description

    Recombinant Bartonella Henselae 17kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 18kDa. Bartonella 17kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bartonella 17kDa is supplied at a 20mM HEPES buffer pH-8.0 and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.

      P17 is the 1st antigen which was discovered to be strongly reactive with sera from Cat Scratch Disease patients. Bartonella henselae participates in host recognition by the type IV secretion system as a homolog of the virB5 family.

      Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.

    • Physical Appearance

      Sterile Filtered 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.

    Bartonella Henselae 17Kda
  • View Data Sheet

    Name :

    p38a/SAPK2 Human

    Description:

    p38a/SAPK2 Human Recombinant

    Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    Product # :

    PKA-217

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    Description

    p38/SAPK2 is a non-glycosilated polypeptide produced by phosphorylation of the purified p38 alpha with MKK6 having a molecular mass of 42.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    p38/SAPK2 is supplied in 25mM Tris-HCl, 150mM NaCl, 1mM DTT, 50% glycerol, pH 8.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      p38a/SAPK2 is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

    • Synonyms

      Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    • 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.

    • Unit Definition

      No protease activity detectable, specific activity is 2.357.900 U*/mg (*1 U = 1 pmol/min transferred to myelin basic protein at 30°C).

    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.

    P38Alpha Human
  • View Data Sheet

    Name :

    CRTAM Human

    Description:

    Cytotoxic and Regulatory T Cell Molecule Human Recombinant

    Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    Product # :

    PRO-2247

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    Description

    CRTAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 278 amino acids (18-287 a.a.) and having a molecular mass of 31.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CRTAM is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CRTAM protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.

    • Synonyms

      Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    • 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

      SLTNHTETIT VEEGQTLTLK CVTSLRKNSS LQWLTPSGFT IFLNEYPALK NSKYQLLHHS ANQLSITVPN VTLQDEGVYK CLHYSDSVST KEVKVIVLAT PFKPILEASV IRKQNGEEHV VLMCSTMRSK PPPQITWLLG NSMEVSGGTL HEFETDGKKC NTTSTLIIHT YGKNSTVDCI IRHRGLQGRK LVAPFRFEDL VTDEETASDA LERNSLSSQD PQQPTSTVSV TEDSSTSEID KEEKEQTTQD PDLTTEANPQ YLGLARKKSG LEHHHHHH.

    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.

    Crtam Human
  • View Data Sheet

    Name :

    Adiponectin Human, HEK

    Description:

    Adiponectin Human Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-434

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    • sds-page

    Description

    Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

    Purity

    Greater than 98% as determined by HPLC and SDS PAGE.

    Biological Activity

    In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

    sds-page

    adiponectin human HEK sds-page - Product image 1

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.

    • Solubility

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

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

    • Background

      What is the molecular weight/Mw of adiponectin Protein?
      Adiponectin Protein has a total Mw of 25.5kDa.

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

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

      What is the Biological Activity of adiponectin Protein?
      In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

      What is the amino acid sequence of adiponectin Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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

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

    Adiponectin Human Hek
  • View Data Sheet

    Name :

    DIRAS1 Human

    Description:

    DIRAS family, GTP-binding RAS-like 1 Human Recombinant

    GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    Product # :

    PRO-256

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    Description

    DIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 24.1 kDa. DIRAS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    DIRAS1 Human solution (1mg/ml) containing 20mM Tris-HCl buffer(pH 8.0) containing 20% glycerol, 1mM DTT, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.

    • Synonyms

      GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    • 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 MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG KCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR KGKC.

    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.

    Diras1 Human
  • View Data Sheet

    Name :

    ARL9 Human

    Description:

    ADP-Ribosylation Factor-Like 9 Human Recombinant

    ADP-ribosylation factor-like protein 9, ARL9.

    Product # :

    PRO-1009

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    Description

    ARL9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (1-123 a.a.) and having a molecular mass of 15.9kDa. ARL9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

    • Synonyms

      ADP-ribosylation factor-like protein 9, ARL9.

    • 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 MEFLEIGGSK PFRSYWEMYL SKGLLLIFVV DSADHSRLPE AKKYLHQLIA ANPVLPLVVF ANKQDLEAAY HITDIHEALA LSEVGNDRKM FLFGTYLTKN GSEIPSTMQD AKDLIAQLAA DVQ.

    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.

    Arl9 Human
  • View Data Sheet

    Name :

    ATG5 Human

    Description:

    Autophagy Related 5 Human Recombinant

    Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.

    Product # :

    PRO-454

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    Description

    ATG5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-275a.a.) and having a molecular mass of 34.6kDa.ATG5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATG5 at a concentration of 0.25mg/ml containing 20mM Tris-HCl, pH 8.0, 1mM DTT , 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

    • Synonyms

      Autophagy protein 5, APG5-like, Apoptosis-specific protein, ATG5, ASP, APG5, APG5L, hAPG5.

    • 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 MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLPRVSYLTLVTD KVKKHFQKVM RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNITVHFKSFPEK DLLHCPSKDA IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLKEVCPSAIDPE DGEKKNQVMI HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD

    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.

    Atg5 Human
  • View Data Sheet

    Name :

    SNRPB Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptides B & B1 Human Recombinant

    Small nuclear ribonucleoprotein-associated proteins B and B', snRNP-B, Sm protein B/B', Sm-B/B', SmB/B', SNRPB, COD, SNRPB1, SmB/SmB'.

    Product # :

    PRO-1511

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    Description

    SNRPB Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 25.4 kDa which migrates at 30kDa on SDS-PAGE. SNRPB is expressed with a -6x His tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    SNRPB is supplied in 20mM HEPES buffer pH-7.5, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPB is one of several nuclear proteins which are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the SNRPB protein may also have a role in pre-mRNA splicing or snRNP structure. SNRPB binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. SNRPB functions in the U7 snRNP complex which is involved in histone 3'-end processing.

    • Synonyms

      Small nuclear ribonucleoprotein-associated proteins B and B', snRNP-B, Sm protein B/B', Sm-B/B', SmB/B', SNRPB, COD, SNRPB1, SmB/SmB'.

    • 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.

    Snrpb Human
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