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Search results

1000 results found for “activating transcription factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    IL 22 Human

    Description:

    Interleukin-22 Human Recombinant

    IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    Product # :

    CYT-328

    Price :

    Quantity :

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    Shipped at Room temp

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    • source
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    Description

    Interleukin-22 Human Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 2 x 146 amino acids and having a total molecular mass of 33,607 Dalton. The IL-22 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg contains 50mM Phosphate buffer pH=7.1.

    Purity

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

    Biological Activity

    The Biological Activity was determined by the ability to activiate STAT following receptor ligand interaction.

    Citations

    More Info

    • Introduction

      IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.

    • Synonyms

      IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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

    Il 22 Human
  • View Data Sheet

    Name :

    ADAT1 Human

    Description:

    Adenosine Deaminase tRNA-Specific 1 Human Recombinant

    tRNA-specific adenosine deaminase 1, hADAT1, tRNA-specific adenosine- 37 deaminase, ADAT1, ADAT-1.

    Product # :

    ENZ-307

    Price :

    Quantity :

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    Description

    Adenosine Deaminase tRNA-Specific 1 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing amino acids 1-502 and having a total molecular mass of 57.7 kda. ADAT-1 contains T7 tag at N-terminus. ADAT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Adenosine Deaminase tRNA-Specific-1 at 0.1mg/ml, 10mM Tris, pH 8.0, 0.1% Triton X-100, 0.002% NaN3.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      This gene is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, proteins encoded by these genes participate in the pre-mRNA editing of nuclear transcripts. The protein encoded by this gene, tRNA-specific adenosine deaminase 1, is responsible for the deamination of adenosine 37 to inosine in eukaryotic tRNA.

    • Synonyms

      tRNA-specific adenosine deaminase 1, hADAT1, tRNA-specific adenosine- 37 deaminase, ADAT1, ADAT-1.

    • 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.

    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.

    Adat1 Human
  • View Data Sheet

    Name :

    CTSZ Human, Sf9

    Description:

    Cathepsin-Z Human Recombinant, Sf9

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1097

    Price :

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
      HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
      AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
      AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
      GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV 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.

    Cathepsin Z Protein
  • View Data Sheet

    Name :

    PNPT1 Human

    Description:

    Polyribonucleotide Nucleotidyltransferase 1 Human Recombinant

    Polyribonucleotide Nucleotidyltransferase 1, Polynucleotide Phosphorylase-Like Protein, Polynucleotide Phosphorylase 1, 3-5 RNA Exonuclease OLD35, PNPase Old-35, EC 2.7.7.8, PNPase 1, COXPD13, DFNB70, PNPASE, OLD35, Polyribonucleotide Nucleotidyltransferase 1, Mitochondrial, Deafness, Autosomal Recessive 70, Polynucleotide Phosphorylase, 3-5 RNA Exonuclease, EC 2.7.7, Old-35, Polyribonucleotide nucleotidyltransferase 1, mitochondrial, 3'-5' RNA exonuclease OLD35, PNPase old-35.

    Product # :

    ENZ-888

    Price :

    Quantity :

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    • description
    • source
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    Description

    PNPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 761 amino acids (46-783 a.a) and having a molecular mass of 83.3kDa. PNPT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PNPT1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

    • Synonyms

      Polyribonucleotide Nucleotidyltransferase 1, Polynucleotide Phosphorylase-Like Protein, Polynucleotide Phosphorylase 1, 3-5 RNA Exonuclease OLD35, PNPase Old-35, EC 2.7.7.8, PNPase 1, COXPD13, DFNB70, PNPASE, OLD35, Polyribonucleotide Nucleotidyltransferase 1, Mitochondrial, Deafness, Autosomal Recessive 70, Polynucleotide Phosphorylase, 3-5 RNA Exonuclease, EC 2.7.7, Old-35, Polyribonucleotide nucleotidyltransferase 1, mitochondrial, 3'-5' RNA exonuclease OLD35, PNPase old-35.

    • 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 MGSAVAVDLG NRKLEISSGK LARFADGSAV VQSGDTAVMV TAVSKTKPSP SQFMPLVVDY RQKAAAAGRI PTNYLRREIG TSDKEILTSR IIDRSIRPLF PAGYFYDTQV LCNLLAVDGV NEPDVLAING ASVALSLSDI PWNGPVGAVR IGIIDGEYVV NPTRKEMSSS TLNLVVAGAP KSQIVMLEAS AENILQQDFC HAIKVGVKYT QQIIQGIQQL VKETGVTKRT PQKLFTPSPE IVKYTHKLAM ERLYAVFTDY EHDKVSRDEA VNKIRLDTEE QLKEKFPEAD PYEIIESFNV VAKEVFRSIV LNEYKRCDGR DLTSLRNVSC EVDMFKTLHG SALFQRGQTQ VLCTVTFDSL ESGIKSDQVI TAINGIKDKN FMLHYEFPPY ATNEIGKVTG LNRRELGHGA LAEKALYPVI PRDFPFTIRV TSEVLESNGS SSMASACGGS LALMDSGVPI SSAVAGVAIG LVTKTDPEKG EIEDYRLLTD ILGIEDYNGD MDFKIAGTNK GITALQADIK LPGIPIKIVM EAIQQASVAK KEILQIMNKT ISKPRASRKE NGPVVETVQV PLSKRAKFVG PGGYNLKKLQ AETGVTISQV DEETFSVFAP TPSAMHEARD FITEICKDDQ EQQLEFGAVY TATITEIRDT GVMVKLYPNM TAVLLHNTQL DQRKIKHPTA LGLEVGQEIQ VKYFGRDPAD GRMRLSRKVL QSPATTVVRT LNDRSSIVMG EPISQSSSNS Q.

    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.

    Pnpt1 Human
  • View Data Sheet

    Name :

    Leptin Ovine, MTS

    Description:

    Leptin Ovine Recombinant, MTS tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-531

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    Description

    Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

    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) Gel filtration analysis.
    (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.

    Citations

    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 Ovine MTS tagged 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 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 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 Ovine Mts
  • View Data Sheet

    Name :

    METRN Mouse

    Description:

    Meteorin Mouse Recombinant

    Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    Product # :

    PRO-2241

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    Description

    METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.

    • Synonyms

      Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    • 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

      GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.

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

    Metrn Mouse
  • View Data Sheet

    Name :

    MREG Human

    Description:

    Melanoregulin Human Recombinant

    Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

    Product # :

    PRO-1885

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    Description

    MREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 27.3kDa.MREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Melanoregulin (MREG) takes part in membrane fusion and in regulating the biogenesis of disk membranes of photoreceptor rods. MREG is expressed in photoreceptor cells as two isoforms as a result of alternative splicing. MREG interacts with Peripherin-2, a photoreceptor specific tetraspanin protein which is required to preserve normal cell structure during the renewal process of membrane fusion. Moreover, MREG plays a part in the incorporation of pigments into hair.

    • Synonyms

      Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGLRDWL RTVCCCCGCE CLEERALPEK EPLVSDNNPY SSFGATLVRD DEKNLWSMPH DVSHTEADDD RTLYNLIVIR NQQAKDSEEW QKLNYDIHTL RQVRREVRNR WKCILEDLGF QKEADSLLSV TKLSTISDSK NTRKAREMLL KLAEETNIFP TSWELSERYL FVVDRLIALD AAEEFFKLAR RTYPKKPGVP CLADGQKELH YLPFPSP

    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.

    Mreg Human
  • View Data Sheet

    Name :

    TSSK2 Human

    Description:

    Testis Specific Serine Kinase 2 Human Recombinant

    800x600 Testis-specific serine/threonine-protein kinase 2, DGS-G, SPOGA2, STK22B, TSK2, TSK-2, TSSK-2, TSSK2, DiGeorge syndrome protein G, Serine/threonine-protein kinase 22B, DGSG, Testis Specific Serine Kinase 2.

    Product # :

    PKA-057

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    Description

    TSSK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43kDa.TSSK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TSSK2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TSSK2 is a testis-specific serine/threonine-protein kinase required during spermatid development which phosphorylates TSKS at 'Ser-288' and SPAG16. TSSK2 takes part in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, TSSK2 is necessary for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.

    • Synonyms

      Testis-specific serine/threonine-protein kinase 2, DGS-G, SPOGA2, STK22B, TSK2, TSK-2, TSSK-2, TSSK2, DiGeorge syndrome protein G, Serine/threonine-protein kinase 22B, DGSG, Testis Specific Serine Kinase 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 MGSMDDATVL RKKGYIVGIN LGKGSYAKVK SAYSERLKFN VAVKIIDRKK TPTDFVERFL PREMDILATV NHGSIIKTYE IFETSDGRIY IIMELGVQGD LLEFIKCQGA LHEDVARKMF RQLSSAVKYC HDLDIVHRDL KCENLLLDKD FNIKLSDFGF SKRCLRDSNG RIILSKTFCG SAAYAAPEVL QSIPYQPKVY DIWSLGVILY IMVCGSMPYD DSDIRKMLRI QKEHRVDFPR SKNLTCECKD LIYRMLQPDV SQRLHIDEIL SHSWLQPPKP KATSSASFKR EGEGKYRAEC KLDTKTGLRP DHRPDHKLGA KTQHRLLVVP ENENRMEDRL AETSRAKDHH ISGAEVGKAS T.

    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.

    Tssk2 Human
  • View Data Sheet

    Name :

    AHA1 Antibody

    Description:

    Activator of HSP90 ATPase-1, Mouse Anti Human

    AHSA1, ACA1, p38, C14orf3, Activator of HSP90 ATPase-1.

    Product # :

    ANT-611

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    More Info

    • Introduction

      AHA1 is a cochaperone that stimulates hsp90 ATPase activity. AHSA1 binds the middle domain of Hsp90 (amino acid 272-627) and functions as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding.
      AHA1 affects a step in the endoplasmic reticulum to golgi trafficking.

    • Synonyms

      AHSA1, ACA1, p38, C14orf3, Activator of HSP90 ATPase-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AHA1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AHA1 protein 19-337 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT3E9AT.

    • Applications

      AHA1 antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution for Western blot analysis is 1:1000.

    • 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

      AHA1 antibody was purified from mouse ascitic fluids by protein-A 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.

    Aha1 Antibody
  • View Data Sheet

    Name :

    CCL2 Mouse, His

    Description:

    Monocyte Chemotactic Protein-1 Mouse Recombinant (CCL2), His Tag

    Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    Product # :

    CHM-014

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    Description

    MCP-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (24-148 a.a) and having a molecular mass of 16kDa.MCP-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MCP-1 protein solution (0.25mg/ml) containing PBS (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CCL2 Mouse, His-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

    • Synonyms

      Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQPDAVNAPL TCCYSFTSKM IPMSRLESYK RITSSRCPKE AVVFVTKLKR EVCADPKKEW VQTYIKNLDR NQMRSEPTTL FKTASALRSS APLNVKLTRK SEANASTTFS TTTSSTSVGV TSVTVN.

    • Background

      What is the molecular weight/Mw of CCL2 MOUSE, HIS Protein?
      CCL2 MOUSE, HIS Protein has a total Mw of 16kDa.

      What is the source or expression system of CCL2 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL2 MOUSE, HIS Protein?
      CCL2 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL2 MOUSE, HIS Protein?
      The biological functionality of CCL2 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL2 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQPDAVNAPL TCCYSFTSKM IPMSRLESYK RITSSRCPKE AVVFVTKLKR EVCADPKKEW VQTYIKNLDR NQMRSEPTTL FKTASALRSS APLNVKLTRK SEANASTTFS TTTSSTSVGV TSVTVN.

      What applications can CCL2 MOUSE, HIS Protein be used in?
      CCL2 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL2 MOUSE, HIS Protein?
      The endotoxin level is minimal, CCL2 MOUSE, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL2 MOUSE, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL2 MOUSE, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Mcp 1 Mouse His
  • View Data Sheet

    Name :

    CXCL8 Human (1-77)

    Description:

    Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-327

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    Description

    Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) 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

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

    sds-page

    IL8 Human sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.

      What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

      What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

      What applications can CXCL8 HUMAN (1-77) Protein be used in?
      CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
      The endotoxin level is minimal, CXCL8 HUMAN (1-77) Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 HUMAN (1-77) that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL8 HUMAN (1-77)?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 8 77 Human
  • View Data Sheet

    Name :

    IL5 Rhesus Macaque

    Description:

    Interleukin-5 Rhesus Macaque Recombinant

    Interleukin-5, IL-5, Eosinophil differentiation factor, T-cell replacing factor, TRF, IL5.

    Product # :

    CYT-772

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    Description

    IL5 Rhesus Macaque Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide protein containing 2x115 amino acids chains and having a total molecular mass of 26.1kDa.The IL-5 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4 and 5% Trehalose.

    Purity

    Greater than 98.0% as determined by HPLC and SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

    Citations

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      Interleukin-5, IL-5, Eosinophil differentiation factor, T-cell replacing factor, TRF, IL5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-5 Rhesus Macaque although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 Rhesus Macaque 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 Interleikin-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPTEIPASAL VKETLALLST HRTLLIANET LRIPVPVHKN HQLCTEEIFQ GIGTLESQTV QGGTVERLFK NLSLIKKYIG GQKKKCGEER RRVNQFLDYL QEFLGVMNTE WIIES.

    • Background

      What is the molecular weight/Mw of IL 5 RHESUS MACAQUE Protein?
      IL 5 RHESUS MACAQUE Protein has a total Mw of 26.1kDa.

      What is the source or expression system of IL 5 RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of IL 5 RHESUS MACAQUE Protein?
      IL 5 RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 5 RHESUS MACAQUE Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

      What is the amino acid sequence of IL 5 RHESUS MACAQUE Protein?
      IPTEIPASAL VKETLALLST HRTLLIANET LRIPVPVHKN HQLCTEEIFQ GIGTLESQTV QGGTVERLFK NLSLIKKYIG GQKKKCGEER RRVNQFLDYL QEFLGVMNTE WIIES.

      What applications can IL 5 RHESUS MACAQUE Protein be used in?
      IL 5 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 5 RHESUS MACAQUE Protein?
      The endotoxin level is minimal, IL 5 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 5 RHESUS MACAQUE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 5 RHESUS MACAQUE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 5 Rhesus Macaque
  • View Data Sheet

    Name :

    SH2D1A Human

    Description:

    SH2 domain containing 1A Human Recombinant

    SH2 domain-containing protein 1A, Duncan disease SH2-protein, Signaling lymphocytic activation molecule-associated protein, SLAM-associated protein, T-cell signal transduction molecule SAP, SH2D1A, DSHP, SAP, LYP, XLP, EBVS, IMD5, XLPD, MTCP1, FLJ18687, FLJ92177, SAP/SH2D1A.

    Product # :

    PRO-006

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    Description

    SH2D1A Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 148 amino acids (1-128 a.a.) and having a molecular mass of 16.3kDa. The SH2D1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SH2D1A solution (1 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH2D1A acts as an inhibitor of the signaling lymphocyte activation molecule (SLAM) self-association. The SH2D1A protein is expressed at a high level in the thymus and the lung, with a lower level of expression in the spleen and the liver. The SH2D1A protein contains an SH2 domain and a short tail. SH2D1A has a key role in the bidirectional stimulation of T and B cells. Defects in the SH2D1A gene cause the X-linked lymphoproliferative disease (XLPD), aka Duncan disease. The XLPD is distinguished by a rare congenital immunodeficiency following an EBV infection (Epstein-Barr virus).

    • Synonyms

      SH2 domain-containing protein 1A, Duncan disease SH2-protein, Signaling lymphocytic activation molecule-associated protein, SLAM-associated protein, T-cell signal transduction molecule SAP, SH2D1A, DSHP, SAP, LYP, XLP, EBVS, IMD5, XLPD, MTCP1, FLJ18687, FLJ92177, SAP/SH2D1A.

    • 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 MDAVAVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYHGY IYTYRVSQTE TGSWSAETAP GVHKRYFRKI KNLISAFQKP DQGIVIPLQY PVEKKSSARS TQGTTGIRED PDVCLKAP.

    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.

    Sh2D1A Human
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

    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.

    Human Nars
  • View Data Sheet

    Name :

    MET Human

    Description:

    Met Proto-Oncogene Human Recombinant

    Hepatocyte growth factor receptor, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met, MET,HGFR, AUTS9, RCCP2.

    Product # :

    PRO-207

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    Description

    Met Proto-Oncogene Human Recombinant produced in Insect cells amino acids 1039-1345, having a molecular weight of 34.6kDa.MET is purified by proprietary chromatographic techniques.

    Source

    Insect cells.

    Formulation

    MET protein (1mg/ml) is supplied in 50mM Tris, 300mM NaCl, 10% Glycerol, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mesenchymal epithelial transition factor (c-MET) is a proto-oncogenic receptor tyrosine kinase. The endogenous ligand for c-MET is HGF (hepatocyte growth factor), which is a disulfide-linked heterodimeric molecule produced predominantly by mesenchymal cells. In the adult, c-MET protein expression is limited to stem and progenitor cells and is required for wound healing and hepatocyte regeneration. In the embryo, c-MET receptors are expressed on cells of epithelial origin, which are vital for invasive growth and mediate epithelial-mesenchymal transition (EMT). Abnormal activation of the HGF/MET pathway leads to a variety of cancers. c-MET mutation is linked with a poor prognosis since it can trigger tumor growth, angiogenesis and metastasis.

    • Synonyms

      Hepatocyte growth factor receptor, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met, MET,HGFR, AUTS9, RCCP2.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      DSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTL
      LDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVL
      PYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDE
      KFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFG
      VLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEM
      RPSFSELVSRISAIFSTFI.

    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.

    Met Human
  • View Data Sheet

    Name :

    ZNRD1 Human

    Description:

    Zinc Ribbon Domain Containing 1 Human Recombinant

    Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.

    Product # :

    PRO-1747

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    Description

    ZNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-126a.a) and having a molecular mass of 16.3kDa.ZNRD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZNRD1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Zinc Ribbon Domain Containing 1 (ZNRD1) is a protein which shows similarity to the Saccharomyces cerevisiae Rpa12p subunit of RNA polymerase I. ZNRD1 contains two potential zinc-binding motifs and takes part in regulation of cell proliferation. ZNRD1 is involved in cancer and human immunodeficiency virus progression. Alternate splicing of this gene results in two transcript variants encoding the same protein. Additional splice variants have been found, but their full-length sequences have not been determined.

    • Synonyms

      Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSVMDLA NTCSSFQSDL DFCSDCGSVL PLPGAQDTVT CIRCGFNINV RDFEGKVVKT SVVFHQLGTA MPMSVEEGPE CQGPVVDRRC PRCGHEGMAY HTRQMRSADE GQTVFYTCTN CKFQEKEDS

    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.

    Znrd1 Human
  • View Data Sheet

    Name :

    Adiponectin Human, HMW

    Description:

    Adiponectin glycosylated Human Recombinant, HMW Rich

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

    Product # :

    CYT-764

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    Description

    Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

    Source

    HEK293.

    Formulation

    Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    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

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 24.6 kDa.

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


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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

      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 Hmw
  • View Data Sheet

    Name :

    PDIA6 Human, Active

    Description:

    Protein Disulfide Isomerase A6 Human Recombinant, Active

    Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    Product # :

    ENZ-994

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    Description

    PDIA6 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 442 amino acids (20-440 a.a.) and having a molecular mass of 48.5kDa. The PDIA6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDIA6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 10 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of INS in the presence of DTT.

    Citations

    More Info

    • Introduction

      PDIA6 belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6, also has a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

    • Synonyms

      Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    • 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 MLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL.

    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.

    Pdia6 Human Active
  • View Data Sheet

    Name :

    Leptin N82K Human, PEG

    Description:

    Leptin N82K Human Recombinant, Pegylated

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1107

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    Description

    Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

    Purity

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

    Biological Activity

    Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

    Citations

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Mutant Protein
  • View Data Sheet

    Name :

    IL12 Human, Sf9

    Description:

    Interleukin-12 Human Recombinant, Sf9

    23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-1111

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    Description

    Interleukin 12 Human Recombinant is a glycosylated heterodimer containing 503 amino acids (306 amino acid rHuIL-12 p40 and the 197 amino acid rHuIL-12 p35 subunits) and having a molecular mass of 60kDa. IL12 is purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

    Greater than 97.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

    Citations

    More Info

    • Introduction

      interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is an essential part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.

    • Synonyms

      23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Interleukin 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:

      >IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.

      >IL-12B

      IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.

    • Background

      What is the molecular weight/Mw of IL12 HUMAN, SF9 Protein?
      IL12 HUMAN, SF9 Protein has a total Mw of 60kDa.

      What is the source or expression system of IL12 HUMAN, SF9 Protein?
      Baculovirus.

      What is the Purity of IL12 HUMAN, SF9 Protein?
      IL12 HUMAN, SF9 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 HUMAN, SF9 Protein?
      Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

      What is the amino acid sequence of IL12 HUMAN, SF9 Protein?
      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
      >IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
      >IL-12B
      IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.

      What applications can IL12 HUMAN, SF9 Protein be used in?
      IL12 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL12 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12 HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il12 Protein
  • View Data Sheet

    Name :

    KLRK1 Human

    Description:

    Killer Cell lectin-Like Receptor Subfamily K, Member 1 Human Recombinant

    CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    Product # :

    PRO-1290

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    Description

    KLRK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (73-216 a.a.) and having a molecular mass of 19.2kDa. KLRK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLRK1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.

    • Synonyms

      CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    • 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 MGSMIWSAVF LNSLFNQEVQ IPLTESYCGP CPKNWICYKN NCYQFFDESK NWYESQASCM SQNASLLKVY SKEDQDLLKL VKSYHWMGLV HIPTNGSWQW EDGSILSPNL LTIIEMQKGD CALYASSFKG YIENCSTPNT YICMQRTV.

    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.

    Klrk1 Human
  • View Data Sheet

    Name :

    IL7 Human, Yeast

    Description:

    Interleukin-7 Human Recombinant, Yeast

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-298

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    Description

    Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

    Citations

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, YEAST Protein?
      IL7 HUMAN, YEAST Protein has a total Mw of 17.4kDa.

      What is the source or expression system of IL7 HUMAN, YEAST Protein?
      Saccharomyces cerevisiae.

      What is the Purity of IL7 HUMAN, YEAST Protein?
      IL7 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 HUMAN, YEAST Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

      What is the amino acid sequence of IL7 HUMAN, YEAST Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

      What applications can IL7 HUMAN, YEAST Protein be used in?
      IL7 HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 HUMAN, YEAST Protein?
      The endotoxin level is minimal, IL7 HUMAN, YEAST Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 HUMAN, YEAST that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 HUMAN, YEAST?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-7 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.

    Il 7 Human Yeast
  • View Data Sheet

    Name :

    IL7 Mouse

    Description:

    Interleukin-7 Mouse Recombinant

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-372

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    Description

    Interleukin-7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4 and 2% trehalose.

    Purity

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

    Biological Activity

    The ED50was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.

    Citations

    More Info

    • Introduction

      Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells. IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.

    • Background

      What is the molecular weight/Mw of IL7 MOUSE Protein?
      IL7 MOUSE Protein has a total Mw of 14.9kDa.

      What is the source or expression system of IL7 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL7 MOUSE Protein?
      IL7 MOUSE Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 MOUSE Protein?
      The ED50was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.

      What is the amino acid sequence of IL7 MOUSE Protein?
      ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.

      What applications can IL7 MOUSE Protein be used in?
      IL7 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 MOUSE Protein?
      The endotoxin level is minimal, IL7 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets

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

    Il 7 Mouse
  • View Data Sheet

    Name :

    GLK E.Coli, Active

    Description:

    Glucokinase E.coli Recombinant, BioActive

    Glucokinase, ECK2384, JW2385.

    Product # :

    PKA-121

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    Description

    GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 70unit/mg obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. One unit will oxidize 1.0 umole of Glucose to D-glucose 6-phosphate per minute in the presence of Beta-NADP at pH 9.0 at 37C.

     

    Citations

    More Info

    • Introduction

      Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.

    • Synonyms

      Glucokinase, ECK2384, JW2385.

    • 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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL

    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.

    Glucokinase
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