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Search results

1000 results found for “gluteradoxin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    OTOR Human

    Description:

    Otoraplin Human Recombinant

    Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    Product # :

    CYT-582

    Price :

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    Shipped at Room temp

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    • source
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    Description

    Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
      Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

    • Synonyms

      Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
      KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
      DIDFFCE.

    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.

    Otoraplin Human
  • View Data Sheet

    Name :

    CXCL14 Rat

    Description:

    BRAK (CXCL14) Rat Recombinant

    C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    Product # :

    CHM-021

    Price :

    Quantity :

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    Description

    CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

    Citations

    More Info

    • Introduction

      CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

    • Synonyms

      C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

    • Background

      What is the molecular weight/Mw of CXCL14 RAT Protein?
      CXCL14 RAT Protein has a total Mw of 9.4kDa.

      What is the source or expression system of CXCL14 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL14 RAT Protein?
      CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL14 RAT Protein?
      Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CXCL14 RAT Protein?
      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

      What applications can CXCL14 RAT Protein be used in?
      CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL14 RAT Protein?
      The endotoxin level is minimal, CXCL14 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL14 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL14 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Cxcl14 Rat
  • View Data Sheet

    Name :

    ING1 Human

    Description:

    Inhibitor of Growth Family, Member 1 Human Recombinant

    Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    Product # :

    PRO-2130

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.

    • Synonyms

      Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    • 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 MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.

    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.

    Ing1 Human
  • View Data Sheet

    Name :

    TSTA3 Human

    Description:

    Tissue Specific Transplantation Antigen P35B Human Recombinant

    FX, P35B, SDR4E1, GDP-L-fucose synthase, Protein FX .

    Product # :

    ENZ-259

    Price :

    Quantity :

    Shipping Method :

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    Description

    TSTA3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-321 a.a.) and having a molecular mass of 38 kDa. The TSTA3 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 Tris pH-8, 2mM DTT, 50mM NaCl & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TSTA3 is a NADP(H)-binding protein. TSTA3 catalyzes the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-deoxymannose to GDP-L-fucose. GDP-L-fucose is the substrate of numerous fucosyltransferases that take part in the expression of several glycoconjugates, including blood group ABH antigens and developmental adhesion antigens.
      Mutations in TSTA3 result in leukocyte adhesion deficiency, type II.

    • Synonyms

      FX, P35B, SDR4E1, GDP-L-fucose synthase, Protein FX .

    • 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 MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD TAQTRALFEK VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS AFEVGARKVV SCLSTCIFPD KTTYPIDETM IHNGPPHNSN FGYSYAKRMI DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF NIEDGHVLPG LIHKVHLAKS SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI ILSVGEEDEV SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP FKQAVKETCA WFTDNYEQAR K.

    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.

    Tsta3 Human
  • View Data Sheet

    Name :

    PSMD10 Human

    Description:

    Gankyrin Human Recombinant

    26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

    Product # :

    ENZ-404

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    Description

    PSMD10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids and having a molecular mass of 24.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    The PSMD10 protein solution (1mg/ml) contains 1x PBS pH-7.4 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.

    • Synonyms

      26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN AVNQNGCTPL HYAASKNRHE IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG NLKMIHILLY YKASTNIQDT EGNTPLHLAC DEERVEEAKL LVSQGASIYI ENKEEKTPLQ VAKGGLGLIL KRMVEG.

    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.

    Psmd10 Human
  • View Data Sheet

    Name :

    CXCL15 Mouse

    Description:

    Lungkine (CXCL15) Mouse Recombinant

    C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    Product # :

    CHM-286

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    Description

    Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

    Citations

    More Info

    • Introduction

      Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

    • Synonyms

      C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

    • Background

      What is the molecular weight/Mw of CXCL15 MOUSE Protein?
      CXCL15 MOUSE Protein has a total Mw of 16.4kDa.

      What is the source or expression system of CXCL15 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL15 MOUSE Protein?
      CXCL15 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL15 MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

      What is the amino acid sequence of CXCL15 MOUSE Protein?
      QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

      What applications can CXCL15 MOUSE Protein be used in?
      CXCL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL15 MOUSE Protein?
      The endotoxin level is minimal, CXCL15 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL15 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL15 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Lungkine Mouse
  • View Data Sheet

    Name :

    GSTA1 Mouse

    Description:

    Glutathione S-Transferase Alpha 1 Mouse Recombinant

    Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.

    Product # :

    ENZ-873

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    Description

    GSTA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 28kDa.GSTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is defined as the amount of enzyme that conjugate 1.0 pmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C and is > 4,000 pmol/min/ug.

    Citations

    More Info

    • Introduction

      Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.

    • Synonyms

      Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.

    • 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 MGSMAGKPVL HYFNARGRME CIRWLLAAAG VEFEEKFIQS PEDLEKLKKD GNLMFDQVPM VEIDGMKLAQ TRAILNYIAT KYDLYGKDMK ERALIDMYSE GILDLTEMIG QLVLCPPDQR EAKTALAKDR TKNRYLPAFE KVLKSHGQDY LVGNRLTRVD IHLLEVLLYV EEFDASLLTP FPLLKAFKSR ISSLPNVKKF LQPGSQRKPP MDAKQIQEAR KAFKIQ.

    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.

    Gsta1 Mouse
  • View Data Sheet

    Name :

    GUK1 Human

    Description:

    Guanylate Kinase 1 Human Recombinant

    GMK, GMP kinase.

    Product # :

    PKA-266

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    Description

    GUK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (1-197 a.a.)and having a total molecular mass of 23.9 kDa. GUK1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GUK1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.

    • Synonyms

      GMK, GMP kinase.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA.

    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.

    Guk1 Human
  • View Data Sheet

    Name :

    RRAGC Human

    Description:

    Ras-Related GTP Binding C Human Recombinant

    Ras-related GTP-binding protein C, Rag C, RagC, GTPase-interacting protein 2, TIB929, RRAGC, GTR2.

    Product # :

    PRO-1050

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    Description

    RRAGC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-399 a.a) and having a molecular mass of 46.7kDa.RRAGC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RRAGC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ras-related GTP binding C (RRAGC) is a monomeric guanine nucleotide-binding protein, or G protein. As a result of binding GTP or GDP, small G proteins act as molecular regulators in various cell processes and signaling pathways. RRAGC regulates the organization of the actin cytoskeleton and has an intrinsic GTPase activity. RRAGC is possibly necessary for the amino acid-induced relocalization of mTORC1 to the lysosomes and its succeeding activation by the GTPase RHEB, which is key step in the activation of the TOR signaling cascade by amino acids.

    • Synonyms

      Ras-related GTP-binding protein C, Rag C, RagC, GTPase-interacting protein 2, TIB929, RRAGC, GTR2.

    • 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 MGSHMSLQYG AEETPLAGSY GAADSFPKDF GYGVEEEEEE AAAAGGGVGA GAGGGCGPGG ADSSKPRILL MGLRRSGKSS IQKVVFHKMS PNETLFLEST NKIYKDDISN SSFVNFQIWD FPGQMDFFDP TFDYEMIFRG TGALIYVIDA QDDYMEALTR
      LHITVSKAYK VNPDMNFEVF IHKVDGLSDD HKIETQRDIH QRANDDLADA GLEKLHLSFY LTSIYDHSIF EAFSKVVQKL IPQLPTLENL LNIFISNSGI EKAFLFDVVS KIYIATDSSP VDMQSYELCC DMIDVVIDVS CIYGLKEDGS GSAYDKESMA IIKLNNTTVL YLKEVTKFLA
      LVCILREESF ERKGLIDYNF HCFRKAIHEV FEVGVTSHRS CGHQTSASSL KALTHNGTPR NAI.

    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.

    RRAGC Human
  • View Data Sheet

    Name :

    ACAD8 Human

    Description:

    Acyl-Coenzyme A Dehydrogenase 8 Human Recombinant

    Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.

    Product # :

    ENZ-294

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    Description

    ACAD8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 416 amino acids (23-415) and having a molecular mass of 45.1kDa.ACAD8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACAD8 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of ?-oxidationin Fatty acid metabolism.
      Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer formation.

    • Synonyms

      Acyl-CoA dehydrogenase family member 8 mitochondrial, ACAD-8, Isobutyryl-CoA dehydrogenase, Activator-recruited cofactor 42 kDa component, ARC42, FLJ22590.

    • 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 MGSLVQTGHR SLTSCIDPSM GLNEEQKEFQ KVAFDFAARE MAPNMAEWDQ KELFPVDVMR KAAQLGFGGV YIQTDVGGSG LSRLDTSVIF EALATGCTST TAYISIHNMC AWMIDSFGNE EQRHKFCPPL CTMEKFASYC LTEPGSGSDA ASLLTSAKKQ GDHYILNGSK AFISGAGESD IYVVMCRTGG PGPKGISCIV VEKGTPGLSF GKKEKKVGWN SQPTRAVIFE DCAVPVANRI GSEGQGFLIA VRGLNGGRIN IASCSLGAAH ASVILTRDHL NVRKQFGEPL ASNQYLQFTL ADMATRLVAA RLMVRNAAVA LQEERKDAVA LCSMAKLFAT DECFAICNQA LQMHGGYGYL KDYAVQQYVR DSRVHQILEG SNEVMRILIS RSLLQE.

    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.

    Acad8 Human
  • View Data Sheet

    Name :

    MGP Human

    Description:

    Matrix Gla Protein Human Recombinant

    Matrix Gla protein, Cell growth-inhibiting gene 36 protein, MGLAP, NTI.

    Product # :

    PRO-922

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    Description

    MGP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (20-96) and having a molecular mass of 11.8 kDa.The MGP is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MGP is vital for the regulation of calcification in the extracellular matrix, particularly in cartilage and arteries. The K-dependent vitamin MGP has five to six residues of Gla, a Ca2+ binding amino acid crucial for vitamin K-dependent gamma carboxylase for its formation. MGP is formed by COOH-terminal processing by carboxypeptidase B-like enzymatic activity and localized in the human bone.

    • Synonyms

      Matrix Gla protein, Cell growth-inhibiting gene 36 protein, MGLAP, NTI.

    • 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 MYESHESMES YELNPFINRR NANTFISPQQ RWRAKVQERI RERSKPVHEL NREACDDYRL CERYAMVYGY NAAYNRYF

    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.

    Mgp Human
  • View Data Sheet

    Name :

    CTACK Mouse

    Description:

    CTACK Mouse Recombinant (CCL27)

    C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    Product # :

    CHM-013

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    Description

    CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

    Citations

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

    • Background

      What is the molecular weight/Mw of CTACK MOUSE Protein?
      CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

      What is the Biological Activity of CTACK MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

      What is the amino acid sequence of CTACK MOUSE Protein?
      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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

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

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

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

    Ctack Mouse
  • View Data Sheet

    Name :

    ADH1A Human

    Description:

    Alcohol Dehydrogenase 1A Human Recombinant

    Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.

    Product # :

    ENZ-580

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    Description

    ADH1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-375) and having a molecular mass of 42kDa.ADH1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.

    • Synonyms

      Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.

    • 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 MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK
      IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK
      FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF.

    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.

    Adh1A Human
  • View Data Sheet

    Name :

    DDAH1 Human

    Description:

    Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant

    DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 1.

    Product # :

    ENZ-014

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    Description

    DDAH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285a.a.) and having a molecular mass of 33.5kDa.DDAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DDAH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dimethylarginine dimethylaminohydrolase 1, is a part of the Dimethylarginine Dimethylaminohydrolase gene family. DDAH1 participates in nitric oxide generation by regulating cellular concentrations of methylarginines, that in turn inhibit nitric oxide synthase activity. Deficiency of DDAH1 results in ADMA (asymmetric dimethylarginine) increase and a decrease in cGMP generation.

    • Synonyms

      DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 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 MGSMAGLGHP AAFGRATHAV VRALPESLGQ HALRSAKGEE VDVARAERQH QLYVGVLGSK LGLQVVELPA DESLPDCVFV EDVAVVCEET ALITRPGAPS RRKEVDMMKE ALEKLQLNIV EMKDENATLD GGDVLFTGRE FFVGLSKRTN QRGAEILADT FKDYAVSTVP VADGLHLKSF CSMAGPNLIA IGSSESAQKA LKIMQQMSDH RYDKLTVPDD IAANCIYLNI PNKGHVLLHR TPEEYPESAK VYEKLKDHML IPVSMSELEK VDGLLTCCSV LINKKVDS

    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.

    Ddah1 Human
  • View Data Sheet

    Name :

    ALDOB Human

    Description:

    Aldolase B Fructose-Bisphosphate Human Recombinant

    Fructose-bisphosphate aldolase B, Liver-type aldolase, ALDOB, ALDB, Aldolase B fructose-bisphosphate, ALDO2, aldolase 2, Aldolase B fructose-bisphosphatase.

    Product # :

    ENZ-245

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    Description

    ALDOB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 388 amino acids (1-364) and having a molecular mass of 42kDa.ALDOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALDOB solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ALDOB is a tetrameric glycolytic enzyme which catalyzes the reversible cleavage of fructose 1-phosphate into dihydroxyacetone phosphate and glyceraldehyde. Fructose-bisphosphate aldolase B (ALDOB) is one of 3 known aldolase isoenzymes, and is located in the kidney and the small adult intestine where it is linked with aldolases A or C. ALDOB is regulated by Insulin and glucagon and is implicated in hereditary fructose intolerance disease.

    • Synonyms

      Fructose-bisphosphate aldolase B, Liver-type aldolase, ALDOB, ALDB, Aldolase B fructose-bisphosphate, ALDO2, aldolase 2, Aldolase B fructose-bisphosphatase.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MGSHMAHRFP ALTQEQKKEL SEIAQSIVAN GKGILAADES VGTMGNRLQR IKVENTEENR RQFREILFSV DSSINQSIGG VILFHETLYQ KDSQGKLFRN ILKEKGIVVG IKLDQGGAPL AGTNKETTIQ GLDGLSERCA QYKKDGVDFG KWRAVLRIAD
      QCPSSLAIQE NANALARYAS ICQQNGLVPI VEPEVIPDGD HDLEHCQYVT EKVLAAVYKA LNDHHVYLEG TLLKPNMVTA GHACTKKYTP EQVAMATVTA LHRTVPAAVP GICFLSGGMS EEDATLNLNA INLCPLPKPW KLSFSYGRAL QASALAAWGG KAANKEATQE AFMKRAMANC
      QAAKGQYVHT GSSGAASTQS LFTACYTY.

    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.

    Aldob Human
  • View Data Sheet

    Name :

    DEFB118 Human

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

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    • sds-page
    • Citations

    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    DEFB118-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 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.

    Defb118 Human
  • View Data Sheet

    Name :

    SERPINA3

    Description:

    Alpha-1 AntiChymotrypsin Human Recombinant

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-750

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    Description

    SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • 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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.

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    Serpina3 Human Recombinant
  • View Data Sheet

    Name :

    SH3GL3 Human

    Description:

    SH3-Domain GRB2-Like 3 Human Recombinant

    SH3-Domain GRB2-Like 3, SH3 Domain-Containing GRB2-Like Protein 3, SH3 Domain Protein 2C, Endophilin-3, EEN-B2, SH3D2C, CNSA3, Endophilin-A3, HsT19371, SH3P13, EEN-2B-L3.

    Product # :

    PRO-2159

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    Description

    SH3GL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (1-347 a.a) and having a molecular mass of 41.7kDa. SH3GL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SH3GL3 protein solution (1mg/ml) containing PBS (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH3-Domain GRB2-Like 3, also known as SH3GL3, is a part of the endophilin family. SH3GL3 contains 1 BAR domain and 1 SH3 domain and takes part in endocytosis. SH3GL3 is a protein coding gene which drafts proteins with high curvature to membranes.

    • Synonyms

      SH3-Domain GRB2-Like 3, SH3 Domain-Containing GRB2-Like Protein 3, SH3 Domain Protein 2C, Endophilin-3, EEN-B2, SH3D2C, CNSA3, Endophilin-A3, HsT19371, SH3P13, EEN-2B-L3.

    • 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 MGSMSVAGLK KQFHKASQLF SEKISGAEGT KLDDEFLDME RKIDVTNKVV AEILSKTTEY LQPNPAYRAK LGMLNTVSKI RGQVKTTGYP QTEGLLGDCM LKYGKELGED STFGNALIEV GESMKLMAEV KDSLDINVKQ TFIDPLQLLQ DKDLKEIGHH LKKLEGRRLD YDYKKKRVGK IPDEEVRQAV EKFEESKELA ERSMFNFLEN DVEQVSQLAV FIEAALDYHR QSTEILQELQ SKLQMRISAA SSVPRREYKP RPVKRSSSEL NGVSTTSVVK TTGSNIPMDQ PCCRGLYDFE PENQGELGFK EGDIITLTNQ IDENWYEGMI HGESGFFPIN YVEVIVPLPQ.

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    Sh3Gl3 Human
  • View Data Sheet

    Name :

    DsbE E.Coli

    Description:

    Thiol Disulfide Interchange Protein E.Coli Recombinant DsbE

    Thiol:disulfide interchange protein dsbE, Cytochrome c biogenesis protein ccmG, dsbE, ccmG, yejQ, b2195, JW2183.

    Product # :

    HSP-025

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    Description

    Recombinant DsbE produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.1 kDa. DsbE is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The DsbE protein solution contains 20mM Tris-HCl, pH-7.5, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DsbE is a reducing Dsb protein involved in electron transfer for cytochrome c maturation in the periplasm of Escherichia coli. DsbE is one of 12 proteins required for their assembly in the periplasm. DsbE functions is to decrease disulphide bonds formed among correctly paired cysteine residues in the cytochrome c apoproteins prior to haem attachment by CcmF and CcmH.

    • Synonyms

      Thiol:disulfide interchange protein dsbE, Cytochrome c biogenesis protein ccmG, dsbE, ccmG, yejQ, b2195, JW2183.

    • 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

      MRNAEGDDPT NLESALIGKP VPKFRLESLD NPGQFYQADV LTQGKPVLLN VWATWCPTCR AEHQYLNQLS AQGIRVVGMN YKDDRQKAIS WLKELGNPYA LSLFDGDGML GLDLGVYGAP ETFLIDGNGI IRYRHAGDLN PRVWEEEIKP LWEKYSKEAA Q.

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    Dsbe Ecoli
  • View Data Sheet

    Name :

    NQO2 Human

    Description:

    NAD(P)H Dehydrogenase Quinone 2 Human Recombinant

    DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].

    Product # :

    ENZ-515

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    Description

    NQO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251amino acids (1-231 a.a.) and having a molecular mass of 28.1 kDa. NQO2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    NQO2 Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NQO2 is a flavoprotein that catalyzes the 2-electron reduction of diverse quinones, redox dyes, and the vitamin K menadione. NQO2 mainly uses dihydronicotinamide riboside (NRH) as the electron donor. NQO2 catalyzes the metabolic detoxification of quinones and their derivatives to hydroquinones. This detoxification process protects cells against quinone-induced oxidative stress, cytotoxicity and mutagenicity.

    • Synonyms

      DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].

    • 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 MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q.

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    Nqo2 Human
  • View Data Sheet

    Name :

    BCL2L1 Mouse

    Description:

    BCL2-Like 1 Recombinant Mouse

    Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.

    Product # :

    PRO-2239

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    Description

    BCL2L1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a) and having a molecular mass of 25.8kDa. BCL2L1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCL2L1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BCL2-Like 1 (BCL2L1) belongs to the BCL-2 protein family. BCL2L1 is found at the outer mitochondrial membrane controls outer mitochondrial membrane channel (VDAC) opening. In addition, BCL2L1 regulate s a switch between cell death modes during mitotic arrest.

    • Synonyms

      Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.

    • 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 MGSMSQSNRE LVVDFLSYKL SQKGYSWSQF SDVEENRTEA PEETEAERET PSAINGNPSW HLADSPAVNG ATGHSSSLDA REVIPMAAVK QALREAGDEF ELRYRRAFSD LTSQLHITPG TAYQSFEQVV NELFRDGVNW GRIVAFFSFG GALCVESVDK EMQVLVSRIA SWMATYLNDH LEPWIQENGG WDTFVDLYGN NAAAESRKGQ ER.

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    Bcl2L1 Mouse
  • 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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    • Citations

    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.

    Citations

    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.

    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.

    Srgn Human
  • View Data Sheet

    Name :

    BLMH Human

    Description:

    BLM Hydrolase Human Recombinant

    BMH, BH, BLM hydrolase.

    Product # :

    ENZ-018

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    BLMH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 475 amino acids (1-455a.a.) and having a molecular mass of 54.7kDa.BLMH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BLMH protein solution (1mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 1,000 pmole/min/ug. Measured by the hydrolysis of Met-AMC at pH 7.5, at 37C.

    Citations

    More Info

    • Introduction

      BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. The standard physiological role of BLMH has not been determined, but it shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

    • Synonyms

      BMH, BH, BLM hydrolase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM GALAE

    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.

    Blmh Human
  • View Data Sheet

    Name :

    ETHE1 Human

    Description:

    Ethylmalonic Encephalopathy 1 Human Recombinant

    Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.

    Product # :

    PRO-1027

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
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    • More Info
    • Citations

    Description

    ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.

    • Synonyms

      Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.

    • 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 MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA

    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.

    Ethe1 Human
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