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Search results

1000 results found for “Receptor Activity-Modifying Protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CD3D Human

    Description:

    CD3D Human Recombinant

    CD3d Molecule, CD3d Antigen, Delta Polypeptide (TiT3 Complex), CD3d Molecule, Delta (CD3-TCR Complex), T-Cell Receptor T3 Delta Chain, T3D, T-Cell Surface Glycoprotein CD3 Delta Chain, CD3 Antigen, Delta Subunit, OKT3, Delta Chain, CD3d Antigen, CD3 Delta, CD3-DELTA, IMD19, CD3D.

    Product # :

    PRO-2539

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    Description

    CD3D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (22-105 a.a.) and fused to a 239 aa hIgG-His-tag at C-terminus containing a total of 323 amino acids and having a molecular mass of 36.5kDa.CD3D shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD3D protein solution (0.5mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD3D, also known as Delta Polypeptide (TiT3 Complex), is a single-pass type 1 membrane protein. CD3D jointly with CD3-zeta, CD3-gamma, CD3-epsilon and the T-cell receptor alpha/beta and gamma/delta heterodimers, creates the T-cell receptor-CD3 complex. Once antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transferred through the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. Likewise, CD3D takes an important part in adaptive immune response and participates in thymocyte differentiation.

    • Synonyms

      CD3d Molecule, CD3d Antigen, Delta Polypeptide (TiT3 Complex), CD3d Molecule, Delta (CD3-TCR Complex), T-Cell Receptor T3 Delta Chain, T3D, T-Cell Surface Glycoprotein CD3 Delta Chain, CD3 Antigen, Delta Subunit, OKT3, Delta Chain, CD3d Antigen, CD3 Delta, CD3-DELTA, IMD19, CD3D.

    • 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

      FKIPIEELED RVFVNCNTSI TWVEGTVGTL LSDITRLDLG KRILDPRGIY RCNGTDIYKD KESTVQVHYR MCQSCVELDP ATVALEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.

    Cd3D Human
  • View Data Sheet

    Name :

    EEF1A1 Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant

    Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    Product # :

    PRO-1910

    Price :

    Quantity :

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    • description
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    Description

    EEF1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (1-462 a.a) and having a molecular mass of 50kDa.

    Source

    Escherichia Coli.

    Formulation

    EEF1A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.

    • Synonyms

      Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    • 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

      MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK

    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.

    Eef1A1 Human
  • View Data Sheet

    Name :

    LIN28 Human

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

    Price :

    Quantity :

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    • description
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    • purity
    • More Info

    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

    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.

    Lin28 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

    Price :

    Quantity :

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    • description
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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 :

    I TAC Human, His

    Description:

    I-TAC Human Recombinant (CXCL11), His Tag

    Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

    Product # :

    CHM-232

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    Description

    I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.

    • Synonyms

      Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

    • 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 MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.

    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.

    I Tac Human His
  • View Data Sheet

    Name :

    NFKBIB Human

    Description:

    NF-kappa-B Inhibitor Beta Human Recombinant

    NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    Product # :

    PRO-1046

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    Description

    NFKBIB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-356 a.a) and having a molecular mass of 40.3kDa (Molecular weight on SDS-PAGE will appear higher).NFKBIB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NF-kappa-B inhibitor beta (NFKBIB) is a member of the NF-kappa-B inhibitor family, which inhibit NF-kappa-B by complexing with, and trapping it in the cytoplasm. Phosphorylation of serine residues on these proteins by kinases marks them for destruction via the ubiquitination pathway, thus allowing activation of the NF-kappa-B, which translocates to the nucleus to act as a transcription factor.

    • Synonyms

      NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    • 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 MGSHMAGVAC LGKAADADEW CDSGLGSLGP DAAAPGGPGL GAELGPGLSW APLVFGYVTE DGDTALHLAV IHQHEPFLDF LLGFSAGTEY MDLQNDLGQT ALHLAAILGE TSTVEKLYAA GAGLCVAERR GHTALHLACR VGAHACARAL LQPRPRRPRE
      APDTYLAQGP DRTPDTNHTP VALYPDSDLE KEEEESEEDW KLQLEAENYE GHTPLHVAVI HKDVEMVRLL RDAGADLDKP EPTCGRSPLH LAVEAQAADV LELLLRAGAN PAARMYGGRT PLGSAMLRPN PILARLLRAH GAPEPEGEDE KSGPCSSSSD SDSGDEGDEY DDIVVHSSRS QTRLPPTPAS KPLPDDPRPV.

    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.

    Nfkbib Human
  • View Data Sheet

    Name :

    EREG Human, His

    Description:

    Epiregulin Human Recombinant, His Tag

    Epiregulin, Proepiregulin, ER, ERP.

    Product # :

    CYT-859

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    • sds-page

    Description

    EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE

    sds-page

    EREG-sds-page - Product image 1

    More Info

    • Introduction

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

    • Synonyms

      Epiregulin, Proepiregulin, ER, ERP.

    • 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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 7.7kDa.

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

      What is the Purity of EREG Protein?
      EREG Protein is >80% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EREG Protein?
      MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

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

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

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

    Ereg Human His
  • View Data Sheet

    Name :

    Inhibin alpha A Chain Human

    Description:

    Inhibin-Alpha A Chain Human Recombinant

    Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    Product # :

    HOR-293

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    Description

    Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    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.

    Inhibin A Alpha Chain Human
  • View Data Sheet

    Name :

    SPINK7 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

    Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    Product # :

    PRO-1507

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    Description

    SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma

    • Synonyms

      Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    • 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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

    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.

    Spink7 Human
  • View Data Sheet

    Name :

    CXCL1 Human

    Description:

    GRO-Alpha Human Recombinant (CXCL1)

    Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    Product # :

    CHM-329

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    Description

    GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

    Purity

    Greater than 97.0% 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 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 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 Ala-Ser-Val-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

      What is the source or expression system of CXCL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 HUMAN Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL1 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

      What applications can CXCL1 HUMAN Protein be used in?
      CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 HUMAN Protein?
      The endotoxin level is minimal, CXCL1 HUMAN 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.

    Gro A Human
  • View Data Sheet

    Name :

    REN Human

    Description:

    Renin Human Recombinant

    Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.

    Product # :

    PRO-1529

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    Description

    REN Human Recombinant produced in E. coli is a single polypeptide chain containing 365 amino acids (67-406) and having a molecular mass of 39.9kDa. REN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

    • Synonyms

      Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.

    • 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 MGSHMLTLGN TTSSVILTNY MDTQYYGEIG IGTPPQTFKV VFDTGSSNVW VPSSKCSRLY TACVYHKLFD ASDSSSYKHN GTELTLRYST GTVSGFLSQD IITVGGITVT QMFGEVTEMP ALPFMLAEFD GVVGMGFIEQ AIGRVTPIFD NIISQGVLKE DVFSFYYNRD SENSQSLGGQ IVLGGSDPQH YEGNFHYINL IKTGVWQIQM KGVSVGSSTL LCEDGCLALV DTGASYISGS TSSIEKLMEA LGAKKRLFDY VVKCNEGPTL PDISFHLGGK EYTLTSADYV FQESYSSKKL CTLAIHAMDI PPPTGPTWAL GATFIRKFYT EFDRRNNRIG FALAR.

    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.

    Ren Human
  • View Data Sheet

    Name :

    CBFB HUman

    Description:

    Core Binding Factor Beta Human Recombinant

    PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    Product # :

    PRO-534

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    Description

    CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.

    • Synonyms

      PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
      ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
      REEMEVRVSQ LLAVTGKKTT RP.

    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.

    Cbfb Human
  • View Data Sheet

    Name :

    Recombinant EGFR Antibody

    Description:

    Recombinant Anti Human Epidermal Growth Factor Receptor

    Product # :

    ANT-600

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    Description

    Recombinant Anti Human Epidermal Growth Factor Receptor monoclonal antibody produced in CHO is a glycosylated dimer containing 1326 amino acids and having a molecular mass of 187.2 kDa.

    Source

    CHO.

    Formulation

    The protein 15.6mg/ml solution contains 20mmol/L Na2HPO4- NaH2PO4, 0.005% Tween 80, pH7.0.

    Purity

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

    Biological Activity

    Compared with reference standard, the range of biological activity was found to be 86%.

    More Info

    • Introduction

      The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

    • Physical Appearance

      Sterile filtered colorless liquid formulation.

    • Stability

      Recombinant EGFR Antibody should be stored between 2-8°C. Please do not freeze.

    • Amino Acid Sequence

      Heavy chain
      QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTP
      FTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKG
      PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
      VVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK
      PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTV
      LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
      GFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL
      HNHYTQKSLSLSPGK.
      Light chain
      DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRF
      SGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQ
      LKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
      EKHKVYACEVTHQGLSSPVTKSFNRGEC.

    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.

    Recombinant Egfr Antibody
  • View Data Sheet

    Name :

    SERPING1 Human HEK

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1639

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    Description

    SERPING1 Human Recombinant produced by transfected human cells is a single polypeptide chain containing 486 amino acids (23-500). SERPING1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SERPING1 was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 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 SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
      EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
      VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
      RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
      FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
      ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
      HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH

    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.

    Serping1 Human Hek
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

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

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

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

    Epiregulin Human
  • View Data Sheet

    Name :

    FABP6 Human, His

    Description:

    Fatty Acid Binding Protein 6 Human Recombinant, His Tag

    I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.

    Product # :

    PRO-667

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    Description

    FABP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids and having a molecular mass of 18 kDa. FABP6 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP6 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP6 also called ileal fatty acid binding protein, is part of the small family of highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 cytosolic protein binds bile acid. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. Alternate transcription promoters generate 2 transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is acetylated on Ala2. FABP6 binds together fatty acids and bile acids and is directly involved in fatty acid transport and metabolism.

    • Synonyms

      I-BABP, ILBP, I-15P, I-BAP, ILBP3, ILLBP, I-BABP, I-BALB, FABP-6, Gastrotropin, Ileal lipid-binding protein, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, Fatty acid-binding protein 6, FABP6.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

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    Fabp6 Human His
  • View Data Sheet

    Name :

    IL1RL1 Human, Sf9

    Description:

    Interleukin-1 Receptor Like-1 Human Recombinant, Sf9

    IL33R, Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    Product # :

    CYT-984

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    Description

    IL 1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-328 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 318 amino acids and having a molecular mass of 36.0kDa.IL 1RL1 shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL1RL1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

    • Synonyms

      IL33R, Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    • 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

      KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

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    Il1Rl1 Human Sf9
  • View Data Sheet

    Name :

    Leptin tA Human, PEG

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

    Product # :

    CYT-702

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    Description

    Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. 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. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 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).

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    Leptin Ta Human Pegylated
  • View Data Sheet

    Name :

    Protein-A/G/L

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.

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    Protein A G L
  • View Data Sheet

    Name :

    RFXANK Human

    Description:

    Regulatory Factor X-Associated Ankyrin-Containing Protein Human Recombinant

    ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.

    Product # :

    PRO-1537

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    Description

    RFXANK Human Recombinant produced in E. coli is a single polypeptide chain containing 260 amino acids (1-237) and having a molecular mass of 28kDa. RFXANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Regulatory Factor X-Associated Ankyrin-Containing Protein (RFXANK) contains ankyrin repeats involved in protein-protein interactions. RFXANK, along with regulatory factor X-associated protein and regulatory factor-5, figures a complex which binds to the X box motif of certain MHC class II gene promoters and activates their transcription. After bound to the promoter, this complex associates with the non-DNA-binding factor MHC class II transactivator, which controls the cell type specificity and inducibility of MHC class II gene expression. Mutations in RFXANK have been linked to bare lymphocyte syndrome type II, complementation group B.

    • Synonyms

      ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.

    • 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 MGSMELTQPA EDLIQTQQTP ASELGDPEDP GEEAADGSDT VVLSLFPCTP EPVNPEPDAS VSSPQGSSLK HSTTLTNRQR GNEVSALPAT LDCDNLVNKP DERGFTPLIW ASAFGEIETV RFLLEWGADP HILAKERESA LSLASTGGYT DIVGLLLERD VDINIYDWNG GTPLLYAVRG NHVKCVEALL ARGADLTTEA DSGYTPMDLA VALGYRKVQQ VIENHILKLF QSNLVPADPE.

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    Rfxank Human
  • View Data Sheet

    Name :

    SORBS3 Human

    Description:

    Sorbin And SH3 Domain Containing 3 Human Recombinant

    Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

    Product # :

    PRO-1829

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    Description

    SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

    • Synonyms

      Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV

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    Sorbs3 Human
  • View Data Sheet

    Name :

    SNAPIN Human

    Description:

    SNAP Associated Protein Human Recombinant

    SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    Product # :

    PRO-663

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    Description

    SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

    • Synonyms

      SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    • 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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.

    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.

    Snapin Human
  • View Data Sheet

    Name :

    LECT1 Human

    Description:

    Leukocyte Cell Derived Chemotaxin 1 Human Recombinant

    BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    Product # :

    PRO-1846

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

    • Synonyms

      BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    • 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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.

    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.

    Lect1 Human
  • View Data Sheet

    Name :

    NABP1 Human

    Description:

    Nucleic Acid Binding Protein 1 Human Recombinant

    Nucleic Acid Binding Protein 1, OBFC2A, Sensor Of Single-Strand DNA Complex Subunit B2, Single-Stranded DNA-Binding Protein 2, SSB2, Oligonucleotide/Oligosaccharide-Binding Fold Containing 2A, Nucleic Acid-Binding Protein 1, Oligonucleotide/Oligosaccharide-Binding Fold-Containing Protein 2A, Sensor Of SsDNA Subunit B2, SOSS-B2, SOSS Complex Subunit B2, hSSB2.

    Product # :

    PRO-1718

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    • description
    • source
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    Description

    NABP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a) and having a molecular mass of 24.8kDa.NABP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NABP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.2M, NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleic acid binding protein 1 is a part of the SOSS complex, amultiprotein complex which functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint.In the SOSS complex, NABP1 acts as a sensor of single-stranded DNA which binds to single-stranded DNA, inparticular to polypyrimidines. The SOSS complex links with DNA lesions and affects diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair andmaintenance of genomic stability. NABP1 is essential for efficient homologous recombination-dependent repairof double-strand breaks (DSBs) and ATM-dependent signaling pathways.

    • Synonyms

      Nucleic Acid Binding Protein 1, OBFC2A, Sensor Of Single-Strand DNA Complex Subunit B2, Single-Stranded DNA-Binding Protein 2, SSB2, Oligonucleotide/Oligosaccharide-Binding Fold Containing 2A, Nucleic Acid-Binding Protein 1, Oligonucleotide/Oligosaccharide-Binding Fold-Containing Protein 2A, Sensor Of SsDNA Subunit B2, SOSS-B2, SOSS Complex Subunit B2, hSSB2.

    • 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 MGSMNRVNDP LIFIRDIKPG LKNLNVVFIV LEIGRVTKTK DGHEVRSCKV ADKTGSITIS VWDEIGGLIQ PGDIIRLTRG YASMWKGCLT LYTGRGGELQ KIGEFCMVYS EVPNFSEPNP DYRGQQNKGA QSEQKNNSMN SNMGTGTFGP VGNGVHTGPE SREHQFSHAG RSNGRGLINP QLQGTASNQT VMTTISNGRD PRRAFKR.

    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.

    Nabp1 Human
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