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Search results

1000 results found for “Prefoldin”

Name

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  • View Data Sheet

    Name :

    FAM49B Human

    Description:

    Family with Sequence Similarity 49, Member B Human Recombinant

    BM-009, L1, Protein FAM49B, FAM49B.

    Product # :

    PRO-1411

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    Description

    FAM49B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347amino acids (1-324 a.a) and having a molecular mass of 39.1kDa. FAM49B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FAM49B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Family with Sequence Similarity 49, Member B (FAM49B) is a member of the FAM49 family. In the latest genome-wide transcriptional analysis, a gene signature was identified for multiple sclerosis (MS), which reverted back to normal during pregnancy. The reversion was mostly evident for seven genes: SOCS2, TNFAIP3, NR4A2, CXCR4, POLR2J, FAM49B, and STAG3L1, most of which are negative regulators of inflammation.

    • Synonyms

      BM-009, L1, Protein FAM49B, FAM49B.

    • 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 MGSMGNLLKV LTCTDLEQGP NFFLDFENAQ PTESEKEIYN QVNVVLKDAE GILEDLQSYR GAGHEIREAI QHPADEKLQE KAWGAVVPLV GKLKKFYEFS QRLEAALRGL LGALTSTPYS PTQHLEREQA LAKQFAEILH FTLRFDELKM TNPAIQNDFS YYRRTLSRMR INNVPAEGEN EVNNELANRM SLFYAEATPM LKTLSDATTK FVSENKNLPI ENTTDCLSTM ASVCRVMLET PEYRSRFTNE ETVSFCLRVM VGVIILYDHV HPVGAFAKTS KIDMKGCIKV LKDQPPNSVE GLLNALRYTT KHLNDETTSK QIKSMLQ.

    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.

    Fam49B Human
  • View Data Sheet

    Name :

    FGF 8 Mouse

    Description:

    Fibroblast Growth Factor-8 Mouse Recombinant

    Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

    Product # :

    CYT-070

    Price :

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    Description

    FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.The FGF-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-8 protein was 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.

    Biological Activity

    The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 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 FGF-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 28.1kDa.

      What is the source or expression system of FGF8 Protein?
      Escherichia Coli.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

      What is the amino acid sequence of FGF8 Protein?
      QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 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.

    Fgf 8 Mouse
  • View Data Sheet

    Name :

    CALR Human

    Description:

    Calreticulin Human Recombinant

    cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.

    Product # :

    PRO-813

    Price :

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    Description

    CALR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (18-417 a.a.) and having a molecular mass of 48.7 kDa. CALR protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CALR Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CALR is a multifunctional protein that acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin is localized in the nucleus, and participates in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is nearly identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. CALR binds to antibodies in specific sera of systemic lupus and Sjogren patients which have anti-Ro/SSA antibodies, it is well conserved among species, and it is positioned in the endoplasmic and sarcoplasmic reticulum where it binds calcium. The amino terminus of CALR interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. CALR reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, CALR acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.

    • Synonyms

      cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.

    • 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 MEPAVYFKEQ FLDGDGWTSR WIESKHKSDF GKFVLSSGKF YGDEEKDKGL QTSQDARFYA LSASFEPFSN KGQTLVVQFT VKHEQNIDCG GGYVKLFPNS LDQTDMHGDS EYNIMFGPDI CGPGTKKVHV IFNYKGKNVL INKDIRCKDD EFTHLYTLIV RPDNTYEVKI DNSQVESGSL EDDWDFLPPK KIKDPDASKP EDWDERAKID DPTDSKPEDW DKPEHIPDPD AKKPEDWDEE MDGEWEPPVI QNPEYKGEWK PRQIDNPDYK GTWIHPEIDN PEYSPDPSIY AYDNFGVLGL DLWQVKSGTI FDNFLITNDE AYAEEFGNET WGVTKAAEKQ MKDKQDEEQR LKEEEEDKKR KEEEEAEDKE DDEDKDEDEE DEEDKEEDEE EDVPGQAKDE L.

    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.

    Calr Human
  • View Data Sheet

    Name :

    PKACa2- RIa2

    Description:

    Inactive Protein Kinase A holoenzyme type I alpha Recombinant

    Protein Kinase A holoenzyme type I alpha, PKACa2- RIa2.

    Product # :

    PKA-203

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    Description

    Inactive holoenzyme consisting of one dimeric regulatory subunit type I alpha and two monomeric catalytic subunits (cAMP-free). Protein Kinase A Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PKA holoenzyme type-I alpha is supplied in 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Holoenzyme can be activated by adding the second messenger cAMP (Activation constant about 100nM) releasing two monomeric catalytic subunits.

    More Info

    • Introduction

      The protein kinase A holoenzyme is a heterotetramer composed of two types of subunits: Catalytic and Regulatory. The Catalyticsubunit contains the enzyme's active site. It also contains a domain that binds ATP and a domain that binds the regulatory subunit. The Regulatory subunit consists oftwo molecules which bind one another in an anti-parallel orientation to form a homodimer; for type I subunits- this binding is covalent via disulfide bonds. This subunit also has has two domains that bind cyclic AMP, a domain that interacts with a catalytic subunit, and an "auto-inhibitory" domain that serves as a substrate or pseudosubstrate for the catalytic subunit. Regulatory subunits may also have biologic activity distinct from their role in modulating catalytic subunit activity. Regulatory subunits exist in two major forms, RI and RII, with each form having two subtypes designated alpha and beta. Each of the four isotypes of the regulatory subunit is encoded by a different gene. In addition, three isotypes of the catalytic subunit have been identified (alpha, beta and gamma). The different isotypes tend to have different distributions within cells and among tissues. Type I enzymes inhabit cytoplasmic, soluble fractions of the cell, whereas type II enzymes tend to associate with cellular membranes.

    • Synonyms

      Protein Kinase A holoenzyme type I alpha, PKACa2- RIa2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      PKA should be stored at 4°C if entire vial will be used within 2-4 weeks. For long term storage it is recommended to store at -20°C. Avoid multiple freeze-thaw cycles.

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    Pkaca2 Ria2
  • View Data Sheet

    Name :

    TNAA E.Coli

    Description:

    Tryptophanase E.Coli Recombinant

    Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.

    Product # :

    ENZ-852

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    Description

    TNAA Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-471) and having a molecular mass of 55.2kDa.TNAA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TNAA solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tryptophanase, also known as tnaA, catalyzes chemical reaction using 2 substrates which are L-tryptophan and H2O. tnaA protein's three products are indole, pyruvate, and NH3.

    • Synonyms

      Tryptophanase/L-cysteine desulfhydrase, PLP-dependent, Tryptophanase, TNAA, L-tryptophan indole-lyase, TNase, tnaA, ind.

    • 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 MGSMENFKHL PEPFRIRVIE PVKRTTRAYR EEAIIKSGMN PFLLDSEDVF IDLLTDSGTG AVTQSMQAAM MRGDEAYSGS RSYYALAESV KNIFGYQYTI PTHQGRGAEQ IYIPVLIKKR EQEKGLDRSK MVAFSNYFFD TTQGHSQING CTVRNVYIKE AFDTGVRYDF KGNFDLEGLE RGIEEVGPNN VPYIVATITS NSAGGQPVSL ANLKAMYSIA KKYDIPVVMD SARFAENAYF IKQREAEYKD WTIEQITRET YKYADMLAMS AKKDAMVPMG GLLCMKDDSF FDVYTECRTL CVVQEGFPTY GGLEGGAMER LAVGLYDGMN LDWLAYRIAQ VQYLVDGLEE IGVVCQQAGG HAAFVDAGKL LPHIPADQFP AQALACELYK VAGIRAVEIG SFLLGRDPKT GKQLPCPAEL LRLTIPRATY TQTHMDFIIE AFKHVKENAA NIKGLTFTYE PKVLRHFTAK LKEV.

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    Tnaa Ecoli
  • 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

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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.

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    Krt16 Human
  • View Data Sheet

    Name :

    PRMT1 Human

    Description:

    Protein Arginine Methyltransferase 1 Human Recombinant

    ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    Product # :

    ENZ-364

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    Description

    PRMT1 Human Recombinant (a.a. 1-353) fused with His-MBP tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 750 amino acids and having a molecular mass of 84 kDa.The PRMT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRMT1 solution contains 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT & 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
      The PRMT1 protein functions as a histone methyltransferase specific for H4.
      PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
      PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
      CAF1 is a new regulator of PRMT1-dependent arginine methylation.
      PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
      PRMT1 plays a post-translationally part in regulating the transcriptional activity.
      PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

    • Synonyms

      ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    • 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

      MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEKPNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLYAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYV HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

    • Unit Definition

      One unit will transfer 1pmol of methyl group to synthetic peptide of histone H4 for 10 minutes at 37°C.

    • Specific Activity

      10,000 Units/ml.

    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.

    Prmt1 Human
  • View Data Sheet

    Name :

    PRPS2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant

    Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.

    Product # :

    PKA-009

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    Description

    PRPS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.4kDa. PRPS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PRPS2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.

    • Synonyms

      Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.

    • 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 MGSMPNIVLF SGSSHQDLSQ RVADRLGLEL GKVVTKKFSN QETSVEIGES VRGEDVYIIQ SGCGEINDNL MELLIMINAC KIASSSRVTA VIPCFPYARQ DKKDKVGESR APISAKLVAN MLSVAGADHI ITMDLHASQI QGFFDIPVDN LYAEPAVLQW IRENIAEWKN CIIVSPDAGG AKRVTSIADR LNVEFALIHK ERKKANEVDR MVLVGDVKDR VAILVDDMAD TCGTICHAAD KLLSAGATKV YAILTHGIFS GPAISRINNA AFEAVVVTNT IPQEDKMKHC TKIQVIDISM ILAEAIRRTH NGESVSYLFS HVPL.

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    Prps2 Human
  • View Data Sheet

    Name :

    PRPSAP2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 Human Recombinant

    PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    Product # :

    PRO-1801

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    Description

    PRPSAP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 43.3kDa. PRPSAP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRPSAP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 (PRPSAP2) is a protein which relates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine, pyrimidine, histidine, tryptophan and NAD. PRS is a complex with 2 catalytic subunits and 2 associated subunits. PRPSAP2 encodes a non-catalytic associated subunit of PRS.

    • Synonyms

      PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    • 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 MGSMFCVTPP ELETKMNITK GGLVLFSANS NSSCMELSKK IAERLGVEMG KVQVYQEPNR ETRVQIQESV RGKDVFIIQT VSKDVNTTIM ELLIMVYACK TSCAKSIIGV IPYFPYSKQC KMRKRGSIVS KLLASMMCKA GLTHLITMDL HQKEIQGFFN IPVDNLRASP FLLQYIQEEI PDYRNAVIVA KSPASAKRAQ SFAERLRLGI AVIHGEAQDA ESDLVDGRHS PPMVRSVAAI HPSLEIPMLI PKEKPPITVV GDVGGRIAII VDDIIDDVDS FLAAAETLKE RGAYKIFVMA THGLLSSDAP RRIEESAIDE VVVTNTIPHE VQKLQCPKIK TVDISMILSE AIRRIHNGES MSYLFRNIGL DD.

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    Prpsap2 Human
  • View Data Sheet

    Name :

    CKS1B Human

    Description:

    CDC28 Protein Kinase Regulatory Subunit 1B Human Recombinant

    CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    Product # :

    PRO-1834

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    Description

    CKS1B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79) and having a molecular mass of 12.0 kDa. CKS1B is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CKS1B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      CKS1B protein which binds to the catalytic subunit of cyclin dependent kinases is vital for their biological function. The CKS1B mRNA is expressed in HeLa cells during the course of cell cycle in several forms which suggests that the encoded protein has a particular function. Two transcript variants were identified for this gene however it seems that only one of them encodes a protein.

    • Synonyms

      CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    • 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 MGSMSHKQIY YSDKYDDEEF EYRHVMLPKD IAKLVPKTHL MSESEWRNLG VQQSQGWVHY MIHEPEPHIL LFRRPLPKKP KK

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    Cks1B Human
  • View Data Sheet

    Name :

    UROS Human

    Description:

    Uroporphyrinogen III Synthase Human Recombinant

    Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.

    Product # :

    ENZ-140

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    Description

    UROS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-265 a.a.) and having a molecular mass of 30.7kDa.UROS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UROS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Uroporphyrinogen III synthase (UROS) is an enzyme involved in the 4th step of porphyrin metabolism and in the conversion of hydroxymethyl bilane into uroporphyrinogen III. Defects in the UROS protein can cause molecular lesions which lead to the autosomal recessive Gunther disease, otherwise known as congenital erythropoietic porphyria (CEP).

    • Synonyms

      Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKVLLLKDAK EDDCGQDPYI RELGLYGLEA TLIPVLSFEF LSLPSFSEKL SHPEDYGGLI FTSPRAVEAA ELCLEQNNKT EVWERSLKEK WNAKSVYVVG NATASLVSKI GLDTEGETCG NAEKLAEYIC SRESSALPLL FPCGNLKREI LPKALKDKGI AMESITVYQT VAHPGIQGNL NSYYSQQGVP ASITFFSPSG LTYSLKHIQE LSGDNIDQIK FAAIGPTTAR ALAAQGLPVS CTAESPTPQA LATGIRKALQ PHGCC.

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    Uros Human
  • View Data Sheet

    Name :

    RPS10 Human

    Description:

    Ribosomal Protein S10 Human Recombinant

    DBA9, S10, 40S ribosomal protein S10, RPS10.

    Product # :

    PRO-1409

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    Description

    RPS10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 21kDa. RPS10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RPS10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomes (the organelles that catalyze protein synthesis) consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS10 which is is located in the cytoplasm and a part of the S10E family of ribosomal proteins, is a ribosomal protein that is a component of the 40S subunit. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.

    • Synonyms

      DBA9, S10, 40S ribosomal protein S10, RPS10.

    • 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 MGSMLMPKKN RIAIYELLFK EGVMVAKKDV HMPKHPELAD KNVPNLHVMK AMQSLKSRGY VKEQFAWRHF YWYLTNEGIQ YLRDYLHLPP EIVPATLRRS RPETGRPRPK GLEGERPARL TRGEADRDTY RRSAVPPGAD KKAEAGAGSA TEFQFRGGFG RGRGQPPQ.

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    Rps10 Human
  • View Data Sheet

    Name :

    Alarelin

    Description:

    Alarelin

    Alarelin, Alarelin Acetate.

    Product # :

    HOR-291

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    Description

    Alarelin acetate peptide is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1167.3 Dalton and a Molecular formula of C56H78N16O12 x C2H4O2. The CAS No. is 79561-22-1.

    Formulation

    The Alarelin was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by Analysis by RP-HPLC.

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    • Introduction

      Alarelin (Gonadotrophin-releasing hormone) is a synthetic LH-RH agonist that is found in higher amounts than that of LH-RH in rat hypophyseal stimulation of gonadotropin secretion in vivo and in vitro and in ovulation inductions. Alarelin is known for its induction of ovulation. Alarelin acetate is the acetate form of a hypothalamic peptide that stimulates the release of FSH and LH from the pituitary gland.

    • Synonyms

      Alarelin, Alarelin Acetate.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      5-oxo-pro-His-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Nhet x CH3COOH.

    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.

    Alarelin
  • View Data Sheet

    Name :

    PPIF Antibody

    Description:

    Cyclophilin-F, Mouse Anti Human

    Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    Product # :

    ANT-389

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

      Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    • Immunogen

      Anti-human Cyclophilin-F mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cyclophilin-F amino acids 30-207 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT1F5AT.

    • Applications

      Cyclophilin-F antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:500~1:1,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:500 and Immunohistochemistry is 1:50.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Cyclophilin-F antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Ppif Antibody
  • View Data Sheet

    Name :

    BSA

    Description:

    Bovine Serum Albumin

    Serum albumin, ALB, BSA.

    Product # :

    PRO-422

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    Description

    Contains 583 amino acid residues derived from the prototypical bovine serum albumin sequence. Suitable for use as a biochemical, excipient (an inert substance used as a diluent or vehicle for a protein), in culture media and chromatographic applications.

    Source

    Bovine Serum.

    Purity

    Greater than 97.0%.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume.

    • Synonyms

      Serum albumin, ALB, BSA.

    • Physical Appearance

      Lyophilized freeze dry yellowish powder.

    • Stability

      Lyophilized BSA although stable at room temperature for 3 weeks, should be stored 2-8°C. Upon reconstitution BSA 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 BSA in sterile 18MΩ-cm H2O for 20 minutes at room temperature and at a concentration no greater than 200mg/ml.

    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.

    Bovine Serum Albumin
  • View Data Sheet

    Name :

    pGH 22kDa Human

    Description:

    Growth Hormone Placental 22kDa Human Recombinant

    GHL, GHV, GH-V, hGH-V, PGH.

    Product # :

    CYT-235

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    Description

    Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GHL, GHV, GH-V, hGH-V, PGH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions 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 Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, not less than 100 µg/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-Phe-Pro-Thr-Ile.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 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 GH-22K-placental 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.

    Placental Gh 22K Human
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

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    Description

    Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Dog
  • View Data Sheet

    Name :

    Liraglutide

    Description:

    Liraglutide

    Product # :

    HOR-028

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    • HPLC, MS

    Description

    Liraglutide peptide is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3751 Dalton and a Molecular formula of C172H265N43O51.

    Formulation

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

    Purity

    Greater than 97% as determined by RP-HPLC.

    HPLC, MS

    liraglutide hplc - Product image 1
    liraglutide mass spec - Product image 2

    More Info

    • Introduction

      Liraglutide is a long-acting GLP1 analogue sharing 97% a.a. homology to human GLP1. Liraglutide differs from GLP1 by the substitution of arginine for lysine at position 34. While GLP1 is degraded swiftly by DPP4 resulting in short life of insulin, Liraglutide contains a fatty acid that binds to albumin and prolongs the half-life of the structure. liraglutide causes insulin to secret in the presence of increasing glucose levels. Due toits receptor site, liraglutide inhibits glucagon secretion and delays gastric emptying.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Liraglutide between 2-8°C, do not freeze. Upon reconstitution Lypressin 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 Liraglutide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
      Lypressin is also soluble in 1% Acetic Acid.

    • Amino Acid Sequence

      H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys(γ-Glu-palmitoyl)-Glu-Phe-Ile-Ala-Trp-Leu-Val-Arg-Gly-Arg-Gly-OH

    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.

    Liraglutide
  • View Data Sheet

    Name :

    NPEPPS Human

    Description:

    Aminopeptidase Puromycin Sensitive Human Recombinant

    PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.

    Product # :

    ENZ-1196

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    Description

    NPEPPS Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 925 amino acids (1-919 a.a.) and having a molecular mass of 104kDa. NPEPPS is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    NPEPPS protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800 pmol/min/ug and is defined as the amount of enzyme that cleaves 1 pmole of H-Leu[1]AMC per minute at pH7.0 at 37°C.

    More Info

    • Synonyms

      PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.

    • 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

      MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY PLPKIDLIAI ADFAAGAMEN GLVTYRETA LLIDPKNSCS SSRQWVALVV GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR DAESIHQYLL QRKASPPTVH HHHHH.

    • Background

      NPEPPS is involved in the proteolytic degradation of misfolded or damaged proteins, contributing to the maintenance of protein homeostasis within the cell. It specifically removes N-terminal amino acids from peptides, thereby regulating their activity and facilitating their further degradation by other proteases.

      This enzyme is particularly important in the nervous system, where it degrades neuropeptides and helps regulate synaptic signaling and neuronal communication.

    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.

    Npepps Human
  • View Data Sheet

    Name :

    Ostreolysin

    Description:

    Ostreolysin Pleurotus Ostreatus Recombinant

    Product # :

    PRO-2600

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    Description

    Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines. 

    More Info

    • Introduction

      Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.

    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.

    Ostreolysin
  • View Data Sheet

    Name :

    ETNK2 Human

    Description:

    EthanolamineKinase 2 Human Recombinant

    Ethanolaminekinase-2

    Product # :

    PKA-077

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    Description

    ETNK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 47.2kDa.ETNK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ETNK2 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ETNK2 belongs to theethanolaminekinase family which catalyzes the 1st step of PtdEtn biosynthesis via the cytidine diphosphate.

    • 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 MGSMAVPPSA PQPRASFHLR RHTPCPQCSW GMEEKAAASA SCREPPGPPR AAAVAYFGIS VDPDDILPGA LRLIQELRPH WKPEQVRTKR FTDGITNKLV ACYVEEDMQD CVLVRVYGER TELLVDRENE VRNFQLLRAH SCAPKLYCTF QNGLCYEYMQ GVALEPEHIR EPRLFRLIAL EMAKIHTIHA NGSLPKPILW HKMHNYFTLV KNEINPSLSA DVPKVEVLER ELAWLKEHLS QLESPVVFCH NDLLCKNIIY DSIKGHVRFI DYEYAGYNYQ AFDIGNHFNE FAGVNEVDYC LYPARETQLQ WLHYYLQAQK GMAVTPREVQ RLYVQVNKFA LASHFFWALW ALIQNQYSTI DFDFLRYAVI RFNQYFKVKP QASALEMPK.

    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.

    Etnk2 Human
  • View Data Sheet

    Name :

    IMPAD1 Mouse Bioactive

    Description:

    Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive

    Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    Product # :

    PRO-2380

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    Description

    IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

    • Synonyms

      Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    • 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

      ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

    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.

    Impad1 Mouse Bioactive
  • View Data Sheet

    Name :

    PRDX1 Mouse

    Description:

    Peroxiredoxin-1 Mouse Recombinant

    Peroxiredoxin-1, Macrophage 23 kDa stress protein, Osteoblast-specific factor 3, OSF-3, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2.

    Product # :

    ENZ-951

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    Description

    PRDX1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 207 amino acids (1-199a.a.) and having a molecular mass of 23.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). PRDX1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PRDX1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2,500 pmol/min/ug. Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for minute.

    More Info

    • Introduction

      PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
      PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
      Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

    • Synonyms

      Peroxiredoxin-1, Macrophage 23 kDa stress protein, Osteoblast-specific factor 3, OSF-3, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2.

    • 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

      MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQKL EHHHHHH.

    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.

    Prdx1 Mouse
  • View Data Sheet

    Name :

    Leptin Human, His

    Description:

    Leptin Human Recombinant, His Tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-287

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)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 known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.

    • Solubility

      The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

    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 Human His
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