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Search results

1000 results found for “retinol binding protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    HLA-DOB Human

    Description:

    Major Histocompatibility Complex Class II DO Beta Human Recombinant

    HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

    Product # :

    PRO-1967

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    Description

    HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.

    • Synonyms

      HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

    • 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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.

    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.

    Hla Dob Human
  • View Data Sheet

    Name :

    VAMP1 Human

    Description:

    Synaptobrevin-1 Human Recombinant

    Vesicle-associated membrane protein 1, SYB1, VAMP-1, Synaptobrevin-1, VAMP1, DKFZp686H12131.

    Product # :

    PRO-577

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    Description

    VAMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (1-91) and having a molecular mass of 11.9 kDa. The VAMP-1 contains 20 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 1X PBS and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin 1(Vehicle-associated membrane, VAMP1) is one of the key proteins in the SNARE complex which is involved in regulated exocytosis. Synaptobrevin1 binds to t-SNAREs, syntaxin (STX) and SNAP25, after the fusion of synaptic vesicles to plasma membrane.

    • Synonyms

      Vesicle-associated membrane protein 1, SYB1, VAMP-1, Synaptobrevin-1, VAMP1, DKFZp686H12131.

    • 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 MSAPAQPPAE GTEGTAPGGG PPGPPPNMTS NRRLQQTQAQVEEVVDIIRV NVDKVLERDQ KLSELDDRAD ALQAGASQFE SSAAKLKRKY W.

    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.

    Vamp1 Human
  • View Data Sheet

    Name :

    MRM1 Human

    Description:

    Mitochondrial RRNA Methyltransferase 1 Human Recombinant

    Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.

    Product # :

    PRO-1416

    Price :

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    Description

    MRM1 Human Recombinant produced in E. coli is a single polypeptide chain containing 356 amino acids (21-353) and having a molecular mass of 38.8kDa. MRM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial rRNA methyltransferase 1 homolog (MRM1) is a part of the RNA methyltransferase TrmH family. MRM1 methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S).

    • Synonyms

      Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.

    • 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 MGSSHAARHG ERPGGEELSR LLLDDLVPTS RLELLFGMTP CLLALQAARR SVARLLLQAG KAGLQGKRAE LLRMAEARDI PVLRPRRQKL DTMCRYQVHQ GVCMEVSPLR PRPWREAGEA SPGDDPQQLW LVLDGIQDPR NFGAVLRSAH FLGVDKVITS RRNSCPLTPV VSKSSAGAME VMDVFSTDDL TGFLQTKAQQ GWLVAGTVGC PSTEDPQSSE IPIMSCLEFL WERPTLLVLG NEGSGLSQEV QASCQLLLTI LPRRQLPPGL ESLNVSVAAG ILLHSICSQR KGFPTEGERR QLLQDPQEPS ARSEGLSMAQ HPGLSSGPEK ERQNEG.

    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.

    Mrm1 Human
  • View Data Sheet

    Name :

    SAP18 Human

    Description:

    Sin3A-Associated Protein 18kDa Human Recombinant

    Histone deacetylase complex subunit SAP18, Sin3-associated polypeptide 18 kDa, Sin3-associated polypeptide p18, Cell growth-inhibiting protein 38, 2HOR0202, SAP18, GIG38.

    Product # :

    PRO-707

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    Description

    SAP18 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 173 amino acids (20- 172 a.a.) and having a molecular mass of 19.7 kDa.The SAP18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAP18 solution contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 30% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAP18 is a component of the histone deacetylase complex which has a significant role in the regulation of eukaryotic gene expression. SAP18 directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression once bound to the promoter. SAP18 plays an important part in gene-specific recruitment of the HDAC complex by a number of transcription factors including Gli, GAGA, and Bicoid. Histone acetylation is significant in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation is catalyzed by multisubunit complexes. SAP18 is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. SAP18 is a component of a splicing-dependent multiprotein EJC (exon junction complex) placed at splice junction on mRNAs.

    • Synonyms

      Histone deacetylase complex subunit SAP18, Sin3-associated polypeptide 18 kDa, Sin3-associated polypeptide p18, Cell growth-inhibiting protein 38, 2HOR0202, SAP18, GIG38.

    • 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 MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY.

    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.

    Sap18 Human
  • View Data Sheet

    Name :

    Prelamin-A

    Description:

    Prelamin-A Recombinant

    Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    Product # :

    PRO-689

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    Description

    Recombinant Prelamin-A is a 74kDa precursor of the nuclear lamin A protein. Prelamin-A is a structural component of the nuclear lamina and it is encoded by lamin A/C gene (LMNA). Due to the presence of a CAAX box sequence at carboxyl terminus, Prelamin-A in vivo goes through a serial of post-translational modifications, resulting in the farnesylation of the cysteine thiol, removal of the AAX tripeptide, carboxyl-methylation of the cysteinyl carboxy group and proteolysis of 18 C-terminal amino acids residues that lead to mature lamin A. Diverse mutations in the lamin A/C gene are associated with different deseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. Recombinant human prelamin A is fused to a 6 Histidine tag at the N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The Prelamin-A solution (0.1mg/ml) contains 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    • 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

      HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
      EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
      RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
      QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
      LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
      RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
      TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
      KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
      WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
      RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYL
      LGNSSPRTQSPQNCSIM

    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.

    Prelamin A
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

    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.

    Protein A G His
  • View Data Sheet

    Name :

    RQCD1 Human

    Description:

    RCD1 Required for Cell Differentiation1 Human Recombinant

    Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.

    Product # :

    PRO-008

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    Description

    RQCD1 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 319 amino acids (1-299 a.a.) and having a molecular mass of 35.7kDa. The RQCD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RQCD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RQCD1 is a novel transcriptional cofactor which mediates retinoic acid-induced cell differentiation. RQCD1 down-regulates MYB- and JUN-dependent transcription and may have a role in cell differentiation. RQCD1 also has a role in retinoic acid-controlled lung development.

    • Synonyms

      Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.

    • 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 MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ.

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    RQCD1 Human
  • View Data Sheet

    Name :

    VAMP2 Human

    Description:

    Synaptobrevin-2 Human Recombinant

    Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    Product # :

    PRO-578

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    Description

    VAMP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (1-89) and having a molecular mass of 13.8 kDa. The VAMP contains 37 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 1X PBS pH 7.4 and 1mM EDTA.

    Purity

    Greater than 95.0% as dtermined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

    • Synonyms

      Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA TAATAPPAAP AGEGGPPAPP PNLTSNRRLQ QTQAQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG ASQFETSAAK LKRKYW.

    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.

    Vamp2 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.

    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

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    Znrd1 Human
  • View Data Sheet

    Name :

    SIRT6 Human

    Description:

    Sirtuin-6 Human Recombinant

    Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-6.

    Product # :

    PRO-282

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    Description

    SIRT6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (1-355 a.a.) and having a molecular mass of 41 kDa. Recombinant SIRT6 is fused to 20 amino acids His-tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The SIRT6 protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SIRT6 is part of the sirtuin family of proteins (Class IV), homologs to the yeast Sir2 protein. SIRT6 is characterized by a sirtuin core domain. Yeast sirtuin proteins are recognized by their ability to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT6, a chromatin-associated protein is involved in DNA repair. Human Sirtuins function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.

    • Synonyms

      Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-6.

    • 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 MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH TGAGISTASG IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ LERVGLLRFL VSQNVDGLHV RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR DTVVGTMGLK ATGRLCTVAK ARGLRACRGE LRDTILDWED SLPDRDLALA DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN LQPTKHDRHA DLRIHGYVDE VMTRLMEHLG LEIPAWDGPR
      VLERALPPLP RPPTPKLEPK EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA KAVPS.

    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.

    Sirt6 Human
  • View Data Sheet

    Name :

    ARHGDIA Human

    Description:

    Rho GDP dissociation inhibitor (GDI) alpha Human Recombinant

    Rho GDP-dissociation inhibitor 1, Rho GDI 1, Rho-GDI alpha, ARHGDIA, GDIA1, RHOGDI, RHOGDI-1, MGC117248.

    Product # :

    PRO-002

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    Description

    ARHGDIA 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 202 amino acids (24-204 a.a.) and having a molecular mass of 22.9kDa. The ARHGDIA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARHGDIA solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rho GDP-dissociation inhibitor 1 (ARHGDIA) is a member of the RAS gene superfamily, which encodes small guanine nucleotide exchange (GTP/GDP) factors. ARHGDIA, which is localized to the cytoplasm, inhibits the dissociation of GDP from Rho proteins, thus preventing GTP from binding to and consequently activating Rho proteins. In humans, the ARHGDIA can be phosphorylated at Ser 101 by p21-activated kinase, an event that inhibits its activity and may result in positive feedback regulation of several ARHGDIA target proteins.

    • Synonyms

      Rho GDP-dissociation inhibitor 1, Rho GDI 1, Rho-GDI alpha, ARHGDIA, GDIA1, RHOGDI, RHOGDI-1, MGC117248.

    • 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 MSVNYKPPAQ KSIQEIQELD KDDESLRKYK EALLGRVAVS ADPNVPNVVV TGLTLVCSSA PGPLELDLTG DLESFKKQSF VLKEGVEYRI KISFRVNREI VSGMKYIQHT YRKGVKIDKT DYMVGSYGPR AEEYEFLTPV EEAPKGMLAR GSYSIKSRFT DDDKTDHLSW EWNLTIKKDW KD.

    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.

    Arhgdia Human
  • View Data Sheet

    Name :

    SRGN Human

    Description:

    Serglycin Human Recombinant

    Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    Product # :

    PRO-965

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    Description

    SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

    • Synonyms

      Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    • 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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.

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    Srgn Human
  • View Data Sheet

    Name :

    Activin-A, CHO Human

    Description:

    Activin-A Human Recombinant, CHO

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-1258

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    • More Info

    Description

    Activin-A Human Recombinant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 26.0kDa. The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Human Activin-A was lyophilized from a concentrated filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.

    More Info

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

      Human INHBA protein should be reconstituted in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26 kDa.
      What is the source or expression system of Activin A Protein?
      CHO Cells.

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

      What is the Biological Activity of Activin A Protein?
      Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.

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

      What is the amino acid sequence of ACTIVIN A Protein?
      GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS

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

       

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    Activin A Protein
  • View Data Sheet

    Name :

    DENR Human

    Description:

    Density-Regulated Protein Human Recombinant

    Density-regulated protein, DRP, Protein DRP1, Smooth muscle cell-associated protein 3, SMAP-3.

    Product # :

    PRO-926

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    Description

    DENR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198) and having a molecular mass of 24.3 kDa.The DENR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DENR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      DENR takes part in the translation of target mRNAs by scanning and recognizing the initiation codon. DENR protein is involved in the intonation of the translational profile of a subset of cancer-related mRNAs when engaged to the translational initiation complex by the oncogene MCTS1.

    • Synonyms

      Density-regulated protein, DRP, Protein DRP1, Smooth muscle cell-associated protein 3,
      SMAP-3.

    • 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 MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE KWPEVDDDSI EDLGEVKK

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    Denr Human
  • View Data Sheet

    Name :

    BATF Human

    Description:

    Basic Leucine Zipper Transcription Factor Human Recombinant

    Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.

    Product # :

    PRO-119

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    Description

    BATF 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 145 amino acids (1-125 a.a.) and having a molecular mass of 16.2kDa. The BATF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BATF solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl and 40% glycerol.

    Purity

    BATF purity was found to be greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.

    • Synonyms

      Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.

    • Physical Appearance

      BATF is supplied as a 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 MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS PRFQP.

    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.

    Batf Human
  • View Data Sheet

    Name :

    NHP2 Human

    Description:

    NHP2 Ribonucleoprotein Homolog Human Recombinant

    H/ACA ribonucleoprotein complex subunit 2, Nucleolar protein family A member 2, snoRNP protein NHP2, NHP2, NOLA2, NHP2P.

    Product # :

    PRO-067

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    Description

    NHP2 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 173 amino acids (1-153 a.a.) and having a molecular mass of 19.3kDa. The NHP2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NHP2 solution (0.25 mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NHP2 belongs to the H/ACA snoRNPs (small nucleolar ribonucleoproteins) gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been organized into 2 families: C/D and H/ACA. NHP2 (NOLA2) forms a small ribonucleoprotein particle with GAR1 (NOLA1), Nop10 for the isomerization of uridine to pseudouridine. NHP2 is involved in a variety of aspects of rRNA processing and modification. NHP2 localizes to the dense fibrillar component of the nucleolus and in nuclear Cajal bodies.

    • Synonyms

      H/ACA ribonucleoprotein complex subunit 2, Nucleolar protein family A member 2, snoRNP protein NHP2, NHP2, NOLA2, NHP2P.

    • 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 MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP LPL.

    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.

    Nhp2 Human
  • View Data Sheet

    Name :

    RLN2 Human, Sf9

    Description:

    Relaxin-2 Human Recombinant, Sf9

    Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    Product # :

    PRO-2406

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    Description

    RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

    • Synonyms

      Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    • 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

      ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.

    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.

    Rln2 Human Sf9
  • View Data Sheet

    Name :

    LBP Mouse

    Description:

    Lipopolysaccaride Mouse Recombinant

    Lipopolysaccharide-binding protein, LBP, Ly88.

    Product # :

    PRO-539

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    Description

    LBP is produced from mouse LBP transfected CHO-cells in serum free medium. For transfection we have cloned complete mouse LBP cDNA into expression vector pPOL-DHFR. Before transfection the complete mouse LBP cDNA was amplified by PCR and cloned into expression vector p-POL-DHFR. RmLBP was produced by his-tag by means of metal affinity purification with Talon and controlled by SDS page. Showing a 58kDa band on SDS-PAGE. Attention: His-tag at the c-terminal end of the LBP has no protease site and is not to split off.

    Source

    Chinese Hamster Ovarian Cells (CHO).

    Formulation

    Recombinant Mouse LBP was lyophilized from a protein solution (1 mg/ml) containing phosphate-buffered saline, pH 7.2.

    Biological Activity

    Up to 2µg/ml LBP mediates binding of FITC-LPS (0.5µg/ml) to CD14+CHO transfectants (2 x 106/ml).

    More Info

    • Introduction

      Lipopolysaccharides (LPS) are a type of glycolipids on the outer cell wall of Gram-negative bacteria. Lipopolysaccharide binding protein (aka LBP) is a plasma protein which facilitates the diffusion of bacterial LPS (endotoxin). LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. LBP belongs to a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). The LBP gene is found on chromosome 20, directly downstream of the BPI gene. LBP catalyzes the transfer of LPS monomers from LPS aggregates to HDL particles, to phospholipid bilayers, and to a binding site on soluble CD14 (sCD14). sCD14 is capable of speeding up the transfer by receiving an LPS monomer from an LPS aggregate, and then yielding it to an HDL particle, therefore acting as a soluble "shuttle" for an insoluble lipid.

    • Synonyms

      Lipopolysaccharide-binding protein, LBP, Ly88.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Lbp Mouse
  • View Data Sheet

    Name :

    GrpE E.Coli

    Description:

    HSP-70 Cofactor (HSP24) E.Coli Recombinant

    HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    Product # :

    HSP-014

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    Description

    GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

    • Synonyms

      HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    • 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

      MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

    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.

    Grpe Ecoli
  • View Data Sheet

    Name :

    ERLIN2 Human

    Description:

    ER Lipid Raft Associated 2 Protein Human Recombinant

    Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.

    Product # :

    PRO-1266

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    Description

    ERLIN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (25-339 a.a) and having a molecular mass of 37.8 kDa.ERLIN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ERLIN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ER Lipid Raft Associated 2 (ERLIN2) is a domain-containing protein which is a member of the band 7/mec-2 family. ERLIN2 is a ubiquitously expressed 339 amino acid protein.ERLIN2 which is localized to the lipid raft-like domains in the membrane of the endoplasmic reticulum (ER), plays a key role in the ER-associated degradation (ERAD) pathway that eliminates metabolically regulated and abnormal proteins from the ER.

    • Synonyms

      Erlin-2, Endoplasmic reticulum lipid raft-associated protein 2, Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2, SPFH domain-containing protein 2,ERLIN2, C8orf2, SPFH2, UNQ2441, PRO5003, PRO9924, NET32, SPG18.

    • 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 MGSKIEEGHI GVYYRGGALL TSTSGPGFHL MLPFITSYKS VQTTLQTDEV KNVPCGTSGG VMIYFDRIEV VNFLVPNAVY DIVKNYTADY DKALIFNKIH HELNQFCSVH TLQEVYIELF DQIDENLKLA LQQDLTSMAP GLVIQAVRVT KPNIPEAIRR NYELMESEKT KLLIAAQKQK VVEKEAETER KKALIEAEKV AQVAEITYGQ KVMEKETEKK ISEIEDAAFL AREKAKADAE CYTAMKIAEA NKLKLTPEYL QLMKYKAIAS NSKIYFGKDI PNMFMDSAGS VSKQFEGLAD KLSFGLEDEP LETATKEN.

    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.

    Erlin2 Human
  • View Data Sheet

    Name :

    REG1A Human

    Description:

    Regenerating Islet-Derived 1 Alpha Human Recombinant

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

    Product # :

    PRO-289

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Reg1A Human
  • View Data Sheet

    Name :

    FAM3D Human

    Description:

    Family with Sequence Similarity 3, Member D Human Recombinant

    Protein FAM3D, FAM3D, EF7, OIT1.

    Product # :

    PRO-1585

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    Description

    FAM3D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-224) containing 209 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 23.3kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    FAM3D filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Family with Sequence Similarity 3, Member D (FAM3D) is a member of the FAM3 family. The FAM3D gene is linked to narcolepsy and diabetes mellitus in pancreatic adenocarcinoma, however FAM3D function of remains vague. FAM3D is amply expressed in the placenta and weakly expressed in the small intestine.

    • Synonyms

      Protein FAM3D, FAM3D, EF7, OIT1.

    • 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; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. FAM3D is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASYMSFSMKTIR LPRWLAASPT KEIQVKKYKC GLIKPCPANY FAFKICSGAA NVVGPTMCFE DRMIMSPVKN NVGRGLNIAL VNGTTGAVLG QKAFDMYSGD VMHLVKFLKE IPGGALVLVA SYDDPGTKMN DESRKLFSDL GSSYAKQLGF RDSWVFIGAK DLRGKSPFEQ FLKNSPDTNK YEGWPELLEM EGCMPPKPF.

    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.

    Fam3D Human
  • View Data Sheet

    Name :

    CUTC Human

    Description:

    cutC Copper Transporter Homolog Human Recombinant

    Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.

    Product # :

    PRO-911

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    Description

    CUTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-273 a.a) and having a molecular mass of 31.5kDa.CUTC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CUTC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUTC belongs to the Cut family and may be involved in efflux trafficking of cuprous ion. The Cut family is linked with the copper homeostasis and involved in several vital metabolisms, such as uptake, storage, delivery, and efflux of copper. Copper which is an essential heavy metal trace element has an imperative role in cell physiology.

    • Synonyms

      Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.

    • 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 MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV.

    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.

    Cutc Human
  • View Data Sheet

    Name :

    s100bb Human

    Description:

    s100bb Human homodimer

    Product # :

    PRO-2797

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    • More Info

    Description

    s100bb Human produced in Human brain tissue is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.

    Source

    Human brain tissue.

    Formulation

    s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.

    Purity

    Greater than 95.0% .

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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 s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      S100BB is not only active in mature brains but also plays a significant role during brain development. It contributes to neural progenitor cell proliferation, neuronal migration, and differentiation. Studies have suggested that alterations in S100BB expression during development might influence the wiring of neural circuits, potentially impacting cognitive functions later in life. Investigating these developmental aspects of S100BB provides essential insights into neurogenesis and brain architecture.

      Implications in Neurological Disorders:

      Research has indicated potential links between abnormal S100BB levels and neurological disorders. Elevated S100BB levels have been observed in conditions such as traumatic brain injury, stroke, and neurodegenerative diseases. Its release into the bloodstream following CNS damage has positioned S100BB as a biomarker for CNS injury. Additionally, studies have explored its involvement in neuroinflammation and synaptic dysfunction, offering a glimpse into its role in diseases like Alzheimer’s and Parkinson’s.

      Conclusion:

      S100BB, once regarded as a brain-specific protein, has emerged as a pivotal player in neurological signaling and development. Its intricate involvement in cellular processes within the CNS underscores its significance in understanding brain function and disorders. As research delves deeper into the regulatory mechanisms and functional implications of S100BB, it holds promise for unveiling novel therapeutic targets for neurological diseases. This study aims to shed light on the multifaceted nature of S100BB, emphasizing its crucial roles in the intricate landscape of the central nervous system.

    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.

    S100Bb Human
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