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Search results

1000 results found for “Myoglobin”

Name

Description

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  • View Data Sheet

    Name :

    MBP (27-396) E.Coli

    Description:

    Maltose Binding Protein (27-396) E.coli Recombinant

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2321

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    Description

    Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (27-396 a.a) and having a molecular mass of 40.8kDa. MBP protein was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MBP protein solution (1mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • 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

      MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTRIT 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.

    Mbp 27 396 Ecoli
  • View Data Sheet

    Name :

    CCL22 Human

    Description:

    Macrophage-Derived Chemokine Human Recombinant (CCL22)

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    Product # :

    CHM-250

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    Description

    MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 8.1 kDa. The MDC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL22 filtered (0.4µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 500mM NaCl pH-7.4.

    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 T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
      MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
      CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
      Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

    • Background

      What is the molecular weight/Mw of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein has a total Mw of 8.1kDa.

      What is the source or expression system of CCL22 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 HUMAN Protein?
      Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL22 HUMAN Protein?
      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

      What applications can CCL22 HUMAN Protein be used in?
      CCL22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 HUMAN Protein?
      The endotoxin level is minimal, CCL22 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.

    Mdc Human
  • View Data Sheet

    Name :

    RHOG Human

    Description:

    Ras Homolog Gene Family Member G Human Recombinant

    Ras homolog family member G(rho G), rho-related GTP-binding protein RhoG, MGC125836, RhoG, ARHG, MGC125835.

    Product # :

    PRO-1136

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    • description
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    • More Info

    Description

    RHOG Human Recombinant produced in E. coli is a single polypeptide chain containing 225 amino acids (1-188) and having a molecular mass of 25.2 kDa. RHOG is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RHOG solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.5M NaCl, 50mM Imidazole and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RHOG belongs to the Rac subfamily of the Rho family of small G proteins. RHOG is a small monomeric GTP-binding protein (G protein), and is a key element of several intracellular signalling pathways. RHOG is needed for the formation of membrane ruffles during macropinocytosis. RHOG takes part in cell migration and is essential for the formation of cup-like structures during trans-endothelial migration of leukocytes. Similar to various small G proteins RHOG has a role in several cellular signalling mechanisms such as cell motility, gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.

    • Synonyms

      Ras homolog family member G(rho G), rho-related GTP-binding protein RhoG, MGC125836, RhoG, ARHG, MGC125835.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMQS IKCVVVGDGA VGKTCLLICY TTNAFPKEYI PTVFDNYSAQ SAVDGRTVNL NLWDTAGQEE YDRLRTLSYP QTNVFVICFS IASPPSYENV RHKWHPEVCH HCPDVPILLV GTKKDLRAQP DTLRRLKEQG QAPITPQQGQ ALAKQIHAVR YLECSALQQD GVKEVFAEAV RAVLNPTPIK RGRSC

    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.

    Rhog Human
  • View Data Sheet

    Name :

    Tissue Factor Human, Active

    Description:

    Coagulation Factor III Active Human Recombinant

    Tissue factor, TF, Coagulation factor III, CD142.

    Product # :

    PRO-2845

    Price :

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    • description
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    • More Info

    Description

    Recombinant Human Tissue Factor Active is a glycosylated, polypeptide chain containing 225 amino acids and having a total molecular mass of 45.0kDa. Coagulation Factor III is fused at C-terminus & is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 20mM Tris and 150mM NaCl, pH 8.0.

    Purity

    Greater than 98.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

    More Info

    • Synonyms

      Tissue factor, TF, Coagulation factor III, CD142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH.

    • Background

      Tissue Factor is the main initiator of the extrinsic blood coagulation pathway. after vascular injury, Tissue Factor binds circulating Factor VII/VIIa, forming the TF–FVIIa complex, which activates Factors IX and X, leading to thrombin generation and fibrin clot formation. Tissue Factor also participates in cell signalling influencing inflammation, angiogenesis, wound healing, and tumor progression.

      What is the molecular weight / Mw of Tissue Factor Protein?
      Tissue Factor Protein has a total Mw of 45kDa.

      What is the source or expression system of Tissue Factor Protein?
      CHO Cells

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

      What is the Biological Activity of Tissue Factor Protein?
      The enzymatic activity was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

      What is the amino acid sequence of Tissue Factor Protein?
      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH

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

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

    Tissue Factor Human, Active
  • View Data Sheet

    Name :

    SPA Long

    Description:

    Staphylococcal Protein-A Long Form Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-1926

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    Description

    SPA Recombinant Long Form produced in E.Coli is a single non-glycosylated polypeptide chain. SPA Long Form is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 422 amino acids and having a molecular mass of 46.6kDa.

    Source

    Escherichia Coli.

    Formulation

    SPA protein was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AQHDEAQQNA FYQVLNMPNL NADQRNGFIQ SLKDDPSQSA NVLGEAQKLN DSQAPKADAQ QNNFNKDQQS AFYEILNMPN LNEAQRNGFI QSLKDDPSQS TNVLGEAKKL NESQAPKADN NFNKEQQNAF YEILNMPNLN EEQRNGFIQS LKDDPSQSAN LLSEAKKLNE SQAPKADNKF NKEQQNAFYE ILHLPNLNEE QRNGFIQSLK DDPSQSANLL AEAKKLNDAQ APKADNKFNK EQQNAFYEIL HLPNLTEEQR NGFIQSLKDD PSVSKEILAE AKKLNDAQAP KEEDNKKPGK EDGNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNNKPGK EDGNKPGKED NNKPGKEDGN KPGKEDGNKP GKEDGNGVHV VKPGDTVNDI AKANGTTADK IAADNKLADK NMIKPGQELV VD.

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    Spa Long
  • View Data Sheet

    Name :

    C.Albicans PLB1

    Description:

    Candida Albicans Phospholipase B1 Recombinant

    Product # :

    PRO-2809

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    Description

    Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffer and 25mM K2CO3.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • 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.

    • Background

      Potential as a Therapeutic Target:

      Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.

      Challenges and Future Directions:

      While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.

      Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.

    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.

    Candida Albicans Plb1
  • View Data Sheet

    Name :

    HHEX Human

    Description:

    Hematopoietically Expressed Homeobox Human Recombinant

    Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    Product # :

    PRO-1624

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    Description

    HHEX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.4kDa. HHEX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HHEX solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.

    • Synonyms

      Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    • 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 MGSMQYPHPG PAAGAVGVPL YAPTPLLQPA HPTPFYIEDI LGRGPAAPTP APTLPSPNSS FTSLVSPYRT PVYEPTPIHP AFSHHSAAAL AAAYGPGGFG GPLYPFPRTV NDYTHALLRH DPLGKPLLWS PFLQRPLHKR KGGQVRFSND QTIELEKKFE TQKYLSPPER KRLAKMLQLS ERQVKTWFQN RRAKWRRLKQ ENPQSNKKEE LESLDSSCDQ RQDLPSEQNK GASLDSSQCS PSPASQEDLE SEISEDSDQE VDIEGDKSYF NAG

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    Hhex Human
  • View Data Sheet

    Name :

    APP Human, HEK

    Description:

    Amyloid beta (A4) Precursor Protein Human Recombinant, HEK

    ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, A4, AD1, beta-amyloid peptide, beta-amyloid precursor protein, testicular tissue protein Li 2, AAA, ABETA, alpha-sApp, CTF gamma, PN2.

    Product # :

    PRO-2777

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    Description

    APP Human Recombinant is a single, glycosylated, polypeptide chain (18-701 a.a) containing a total of 690 amino acids, having a molecular mass of 78.2 kDa. APP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The APP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    > 90% by SDS-PAGE.

    Biological Activity

    The inhibitory function of APP on activity of trypsin was measured by a fluorometric

    assay using Mca-RPKPVE-Nval-WRK(Dnp)-NH2 at pH 7.5 at 37C.  The IC50 ≤ 1 nM.

    More Info

    • Synonyms

      ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, A4, AD1, beta-amyloid peptide, beta-amyloid precursor protein, testicular tissue protein Li 2, AAA, ABETA, alpha-sApp, CTF gamma, PN2.

    • 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

      LEVPTDGNAG LLAEPQIAMF CGRLNMHMNV QNGKWDSDPS GTKTCIDTKE GILQYCQEVY PELQITNVVE ANQPVTIQNW CKRGRKQCKT HPHFVIPYRC LVGEFVSDAL LVPDKCKFLH QERMDVCETH LHWHTVAKET CSEKSTNLHD YGMLLPCGID KFRGVEFVCC PLAEESDNVD SADAEEDDSD VWWGGADTDY ADGSEDKVVE VAEEEEVAEV EEEEADDDED DEDGDEVEEE AEEPYEEATE RTTSIATTTT TTTESVEEVV REVCSEQAET GPCRAMISRW YFDVTEGKCA PFFYGGCGGN RNNFDTEEYC MAVCGSAMSQ SLLKTTQEPL ARDPVKLPTT AASTPDAVDK YLETPGDENE HAHFQKAKER LEAKHRERMS QVMREWEEAE RQAKNLPKAD KKAVIQHFQE KVESLEQEAA NERQQLVETH MARVEAMLND RRRLALENYI TALQAVPPRP RHVFNMLKKY VRAEQKDRQH TLKHFEHVRM VDPKKAAQIR SQVMTHLRVI YERMNQSLSL LYNVPAVAEE IQDEVDELLQ KEQNYSDDVL ANMISEPRIS YGNDALMPSL TETKTTVELL PVNGEFSLDD LQPWHSFGAD SVPANTENEV EPVDARPAAD RGLTTRPGSG LTNIKTEEIS EVKMDAEFRH DSGYEVHHQK LVFFAEDVGS NKGA HHHHHH.

    • Background

      Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid plaques and neurofibrillary tangles in the brain, leading to cognitive decline and memory loss. The amyloid beta (Aβ) peptide, derived from the amyloid beta (A4) precursor protein, has been identified as a key player in the pathogenesis of AD. This research aims to explore the significance of the amyloid beta precursor protein, its processing, and the implications it holds for understanding and treating Alzheimer's disease.
      The amyloid beta precursor protein (APP) is a transmembrane protein widely expressed in various tissues, with higher concentrations found in the brain. APP undergoes sequential proteolytic processing by enzymes known as secretases, leading to the generation of Aβ peptides of different lengths. Of particular importance is the production of the Aβ42 peptide, which has a propensity to aggregate and form the characteristic amyloid plaques in AD.
      Understanding the processing and metabolism of APP is crucial for unraveling the mechanisms underlying AD pathology. Mutations in the APP gene and dysregulation of its processing have been associated with familial forms of AD, highlighting the pivotal role of APP in disease development. Investigating the function of APP and its proteolytic fragments can provide valuable insights into the molecular events leading to AD and potentially lead to the identification of therapeutic targets.
      This research will delve into the processing of the amyloid beta precursor protein, shedding light on the different cleavage pathways mediated by α-, β-, and γ-secretases. The paper will discuss the impact of these proteolytic events on the generation of Aβ peptides and how alterations in these pathways contribute to AD pathogenesis. Furthermore, it will explore the aggregation properties of Aβ peptides and their role in the formation of amyloid plaques, as well as their impact on neuronal function and viability.
      The study will also examine the potential of APP and Aβ as biomarkers for AD diagnosis and progression monitoring. Investigating the levels of APP and Aβ peptides in biological fluids and utilizing imaging techniques to detect amyloid plaques could enhance early diagnosis and facilitate the development of novel therapeutic interventions.
      By elucidating the molecular mechanisms involving APP and Aβ in AD, this research aims to contribute to the understanding of the disease pathogenesis and identify potential therapeutic targets. Additionally, it underscores the importance of ongoing research in this field to develop effective strategies for early diagnosis, disease modification, and improved patient outcomes.

    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.

    App Protein
  • View Data Sheet

    Name :

    SNRPC Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

    U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    Product # :

    PRO-1004

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    Description

    SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNRPC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.3M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

    • Synonyms

      U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    • 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 MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.

    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.

    Snrpc Human
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

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    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • 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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

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    Pcsk1N Human
  • View Data Sheet

    Name :

    INHBC Human

    Description:

    Inhibin-Beta C Chain Human Recombinant

    Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    Product # :

    HOR-010

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    Description

    INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.

    • Synonyms

      Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    • 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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS

    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.

    Inhbc Human
  • View Data Sheet

    Name :

    TINAGL1 Human, Sf9

    Description:

    Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant, Sf9

    Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.

    Product # :

    PRO-2422

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    Description

    TINAGL1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 455 amino acids (22-467a.a.) and having a molecular mass of 51.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TINAGL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TINAGL1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.

    • Synonyms

      Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.

    • 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

      ADLAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHHH HHHHH.

    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.

    Tinagl1 Human Sf9
  • View Data Sheet

    Name :

    TPGS2 Human

    Description:

    Tubulin Polyglutamylase Complex Subunit 2 Human Recombinant

    Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

    Product # :

    PRO-1668

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    Description

    TPGS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 35.7kDa.TPGS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPGS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubulin Polyglutamylase Complex Subunit 2 (TPGS2) is a component of the neuronal polyglutamylase complex, which takes part in post-translational addition of glutamate residues to C-terminal tubulin tails. Alternatively spliced transcript variants encoding multiple isoforms have been monitored for TPGS2.

    • Synonyms

      Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

    • 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 MGSMEEEASS PGLGCSKPHL EKLTLGITRI LESSPGVTEV TIIEKPPAER HMISSWEQKN NCVMPEDVKN FYLMTNGFHM TWSVKLDEHI IPLGSMAINS ISKLTQLTQS SMYSLPNAPT LADLEDDTHE ASDDQPEKPH FDSRSVIFEL DSCNGSGKVC LVYKSGKPAL AEDTEIWFLD RALYWHFLTD TFTAYYRLLI THLGLPQWQY AFTSYGISPQ AKQWFSMYKP ITYNTNLLTE ETDSFVNKLD PSKVFKSKNK IVIPKKKGPV QPAGGQKGPS GPSGPSTSST SKSSSGSGNP TRK.

    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.

    Tpgs2 Human
  • View Data Sheet

    Name :

    TPM2 Human

    Description:

    Tropomyosin-2 Human Recombinant

    Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.

    Product # :

    PRO-069

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    Description

    TPM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-284a.a.) and having a molecular mass of 35.1kDa(molecular weight on SDS-PAGE will appear higher).TPM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPM2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin beta chain isoform 2 is affiliate to the actin filament binding protein family which primarily expressed in slow, type 1 muscle fibers. Mutations in TPM2 can change the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes.

    • Synonyms

      Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.

    • 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 MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESRA RQLEEELRTM DQALKSLMAS EEEYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE KTIDDLEETL ASAKEENVEI HQTLDQTLLE LNNL.

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    Tpm2 Human
  • View Data Sheet

    Name :

    CFP Human, Native

    Description:

    Complement Factor Properdin Human

    Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.

    Product # :

    PRO-2702

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    Description

    CFP Human produced in Human plasma having a molecular weight of 53kDa.

    Source

    Human Plasma.

    Formulation

    CFP solution contains PBS, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.

    • Synonyms

      Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFP Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, STS and HBSAG.

    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.

    Complement Factor Properdin
  • View Data Sheet

    Name :

    MECP2 Human

    Description:

    Methyl CpG Binding Protein 2 Human Recombinant

    Methyl CpG binding protein 2 (Rett syndrome), MeCp-2 protein, AUTSX3, MRX16, MRX79, MRXS13, MRXSL, PPMX, RTT, Mental retardation, X-linked 16, DKFZp686A24160.

    Product # :

    PRO-212

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    Description

    MECP2 Human Recombinant is expressed in 293 cells. The protein contains 486 amino acids (1-486a.a.) and fused to an N-terminal Flag tag, having an Mw of 53.56kDa.

    Source

    Mammalian system, 293 cells.

    Formulation

    The MECP2 solution (0.45mg/ml) contains 50mM Tris, 135mM NaCl, 20% Glycerol, pH 7.5 and 200µg/ml FLAG peptide.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      MECP2 is the key modificator of eukaryotic genomes and has a crucial part in mammalian development.
      Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 form a family of nuclear proteins linked by the existence in each of a methyl-CpG binding domain (MBD). Each one of these proteins, with the exception of MBD3, can bind specifically to methylated DNA. In addition, MECP2, MBD1 and MBD2 can inhibit transcription from methylated gene promoters. Unlike other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is expendable in stem cells, but is vital for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common reasons of mental retardation in females.

    • Synonyms

      Methyl CpG binding protein 2 (Rett syndrome), MeCp-2 protein, AUTSX3, MRX16, MRX79, MRXS13, MRXSL, PPMX, RTT, Mental retardation, X-linked 16, DKFZp686A24160.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      MECP2 although stable 4°C for 4 weeks, should be stored 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.

    • Amino Acid Sequence

      MDYKDDDDKMVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSA
      EPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAG
      KYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGT
      GRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMV
      IKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIE
      VKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVP
      LLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAA
      EKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS.

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    Mecp2 Human
  • View Data Sheet

    Name :

    Ag85B

    Description:

    Mycobacterium Tuberculosis major secretory protein Antigen 85B Recombinant

    Antigen 85-B, 85B, Extracellular alpha-antigen, Antigen 85 complex B, Ag85B, Mycolyl transferase 85B, EC 2.3.1.-, Fibronectin-binding protein B, 30 kDa extracellular protein, fbpB, A85B, Major Secretory Protein Antigen 85B.

    Product # :

    PRO-589

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    Description

    Ag85B Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 30kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized with no additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Antigen 85B Mycobacterium Tuberculosis-is the most abundant protein exposed by M. Tuberculosis, as well as a potent immunoprotective antigen and a leading drug target. Ag85 induces strong T-cell proliferation and IFN-g secretion in most healthy individuals exposed to M. tuberculosis, in BCG-vaccinated mice and humans, whereas the antibody against Ag85 are more prevalent in active tuberculosis patients with decreased cellular immune response.

    • Synonyms

      Antigen 85-B, 85B, Extracellular alpha-antigen, Antigen 85 complex B, Ag85B, Mycolyl transferase 85B, EC 2.3.1.-, Fibronectin-binding protein B, 30 kDa extracellular protein, fbpB, A85B, Major Secretory Protein Antigen 85B.

    • Physical Appearance

      Sterile Filtered and lyophilized, though might appear as a solution as a result of the glycerol content.

    • Stability

      Ag85B although stable room temperature for 4 weeks, should be stored desiccated 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 Antigen-85B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MRGSHHHHHHFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQ
      DDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETF
      LTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDP
      SQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVY
      CGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWE
      YWGAQLNAMKGDLQSSLGAG.

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    Ag85B
  • View Data Sheet

    Name :

    AMBP Human

    Description:

    Microglobulin Alpha-1 Protein Human

    Alpha-1 Microglobulin, A1M.

    Product # :

    PRO-407

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    Description

    Alpha 1-microglobulin (A1M) is an immunomodulatory protein with a broad spectrum of possible clinical applications and seems a promising marker for evaluation of tubular function.

    Source

    Purified from the urine of patients with chronic renal tubular proteinuria.

    Formulation

    Lyophilized from 0.02M NH4HCO3. May contain traces of buffer salts.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species. A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore. Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin. Alpha-1-microglobulin was first discovered in pathological human urine. It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include: inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.
      Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

    • Synonyms

      Alpha-1 Microglobulin, A1M.

    • Physical Appearance

      Sterile Filtered Off-White lyophilized (freeze-dried) powder.

    • Stability

      Human A1M although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      Use phosphate buffer, pH>7.0 containing 0.15M NaCl, is recommended.

    • Human Virus Test

      Starting material tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

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    Microglobulin Alpha 1 Human
  • View Data Sheet

    Name :

    CRP Mouse

    Description:

    C-Reactive Protein Mouse Recombinant

    C-reactive protein, pentraxin-related, Crp.

    Product # :

    PRO-2630

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    Description

    CRP Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 214 amino acids (20-225 a.a) and having a molecular mass of 24.1 kDa. CRP is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CRP solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M PMSF and 40% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-Reactive Protein or CRP, is a protein, part of the pentraxin superfamily. Among the protein’s activities, CRP can promote agglutination, swelling of the bacteria capsule, phagocytosis etc. this protein can also cause complement fixation via a calcium-dependent binding to the molecule phosphorylcholine.

    • Synonyms

      C-reactive protein, pentraxin-related, Crp.

    • 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

      HEDMFKKAFV FPKESDTSYV SLEAESKKPL NTFTVCLHFY TALSTVRSFS VFSYATKKNS NDILIFWNKD KQYTFGVGGA EVRFMVSEIP EAPTHICASW ESATGIVEFW IDGKPKVRKS LHKGYTVGPD ASIILGQEQD SYGGDFDAKQ SLVGDIGDVN MWDFVLSPEQ ISTVYVGGTL SPNVLNWRAL NYKAQGDVFI KPQLWSLEHH HHHH.

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    Crp Mouse
  • View Data Sheet

    Name :

    CYP2D6

    Description:

    Cytochrome P450 2D6 Human Recombinant

    Cytochrome P450 2D6, CYPIID6, P450-DB1, Debrisoquine 4-hydroxylase, CYP2D6, CPD6, CYP2D, CYP2D@, CYP2DL1, P450C2D, MGC120389, MGC120390, LKM1, liver/kidney microsomal antigen 1.

    Product # :

    ENZ-316

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    Description

    Cytochrome P450 2D6 Human Recombinant (also called liver/kidney microsomal antigen 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 60 kDa. The LKM1 is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    LKM-1 is supplied in 17mM HEPES pH-7.5, 425mM NaCl, 1mM DTT, 1% Triton X-100 and 15% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytochrome P450 2D6 is a member of a complex family of microsomal enzymes (mono-oxygenases) present in the endoplasmic reticulum membrane, which perform detoxification reaction on xenobiotic compounds. Cytochrome P450 2D6 is the molecular target of autoantibodies against the "liver kidney microsomal antigen 1" (LKM 1) which has been classically defined by immunofluorescence microscopy. The presence of these autoantibodies is considered indicative of Autoimmune Hepatitis Type 2; LKM 1 antibodies have also been detected in patients with hepatitis C viral infection. The International Autoimmune Hepatitis Group therefore has subdivided the AIH type 2 into two subgroups: 2a with HCV and 2b without HCV. AIH 2a patients are often over 40 and predominantly male.
      The use of a purified recombinant Cytochrome P450 2D6 antigen allows the differentiation of autoimmune hepatitis from drug-induced hepatitis where transient autoantibodies to other P450 family members occur which cannot be differentiated by immunofluorescence techniques.

    • Synonyms

      Cytochrome P450 2D6, CYPIID6, P450-DB1, Debrisoquine 4-hydroxylase, CYP2D6, CPD6, CYP2D, CYP2D@, CYP2DL1, P450C2D, MGC120389, MGC120390, LKM1, liver/kidney microsomal antigen 1.

    • Physical Appearance

      Sterile filtered 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative samples). 3. Immunodot analysis with positive/negative samples.

    • coating concentration

      0.35-0.6 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western-Blot with monoclonal anti-LKM-1 antibody and anti-LKM-1 autoantibody- positive sample.

    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.

    Cyp2D6 Human
  • View Data Sheet

    Name :

    HSA, Sf9

    Description:

    Serum Albumin Human, Sf9

    Albumin, Cell Growth Inhibiting Protein 42, Growth-Inhibiting Protein 20, Albumin (32 AA), Albumin (AA 34), Serum Albumin, PRO0883, PRO0903, PRO1341, ANALBA, FDAH, HAS, ALB.

    Product # :

    PRO-2195

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    Description

    HSA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-609 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 597 amino acids and having a molecular mass of 68kDa.HSA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.

    • Synonyms

      Albumin, Cell Growth Inhibiting Protein 42, Growth-Inhibiting Protein 20, Albumin (32 AA), Albumin (AA 34), Serum Albumin, PRO0883, PRO0903, PRO1341, ANALBA, FDAH, HAS, ALB.

    • 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

      RGVFRRDAHK SEVAHRFKDL GEENFKALVL IAFAQYLQQC PFEDHVKLVN EVTEFAKTCV ADESAENCDK SLHTLFGDKL CTVATLRETY GEMADCCAKQ EPERNECFLQ HKDDNPNLPR LVRPEVDVMC TAFHDNEETF LKKYLYEIAR RHPYFYAPEL LFFAKRYKAA FTECCQAADK AACLLPKLDE LRDEGKASSA KQRLKCASLQ KFGERAFKAW AVARLSQRFP KAEFAEVSKL VTDLTKVHTE CCHGDLLECA DDRADLAKYI CENQDSISSK LKECCEKPLL EKSHCIAEVE NDEMPADLPS LAADFVESKD VCKNYAEAKD VFLGMFLYEY ARRHPDYSVV LLLRLAKTYE TTLEKCCAAA DPHECYAKVF DEFKPLVEEP QNLIKQNCEL FEQLGEYKFQ NALLVRYTKK VPQVSTPTLV EVSRNLGKVG SKCCKHPEAK RMPCAEDYLS VVLNQLCVLH EKTPVSDRVT KCCTESLVNR RPCFSALEVD ETYVPKEFNA ETFTFHADIC TLSEKERQIK KQTALVELVK HKPKATKEQL KAVMDDFAAF VEKCCKADDK ETCFAEEGKK LVAASQAALG LHHHHHH

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    Hsa Sf9
  • View Data Sheet

    Name :

    NOV Human, HEK

    Description:

    Nephroblastoma Overexpressed Human Recombinant, HEK

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-1032

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    Description

    NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

    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.

    Nov Protein
  • View Data Sheet

    Name :

    EYA2 Human

    Description:

    Eyes Absent Homolog 2 Human Recombinant

    Eyes absent homolog 2 (Drosophila), EAB1, EC 3.1.3.48.

    Product # :

    PRO-1071

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EYA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 295 amino acids (244-514) and having a molecular mass of 33.2kDa.EYA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EYA2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EYA2 belongs to tyrosine phosphatase family which specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). EYA2 promotes effective DNA mending by dephosphorylating H2AX, promoting the enlistment of DNA repair complexes having MDC1. EYA2 role as histone phosphatase can explain its part in transcription regulation during organogenesis.

    • Synonyms

      Eyes absent homolog 2 (Drosophila), EAB1, EC 3.1.3.48.

    • 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 MGSMERVFVW DLDETIIIFH SLLTGTFASR YGKDTTTSVR IGLMMEEMIF NLADTHLFFN DLEDCDQIHV DDVSSDDNGQ DLSTYNFSAD GFHSSAPAAN LCLGSGVHGG VDWMRKLAFR YRRVKEMYNT YKNNVGGLIG TPKRETWLQL RAELEALTDL WLTHSLKALN LINSRPNCVN VLVTTTQLIP ALAKVLLYGL GSVFPIENIY SATKTGKESC FERIMQRFGR KAVYVVIGDG VEEEQGAKKH NMPFWRISCH ADLEALRHAL ELEYL.

    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.

    Eya2 Human
  • View Data Sheet

    Name :

    CAB39 Human

    Description:

    Calcium Binding Protein 39 Human Recombinant

    MO25, CAB-39, CGI-66, FLJ22682, Calcium Binding Protein 39.

    Product # :

    PRO-857

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CAB39 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 361 amino acids (1-341 a.a.) and having a molecular mass of 42 kDa. The CAB39 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAB39 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAB39 protein and STE20-related adaptor-alpha pseudo kinase, form a regulatory complex that is able of stimulating the activity of the LKB1 tumor suppressor protein kinase. CAB39 takes part as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.

    • Synonyms

      MO25, CAB-39, CGI-66, FLJ22682, Calcium Binding Protein 39.

    • 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 MPFPFGKSHK SPADIVKNLK ESMAVLEKQD ISDKKAEKAT EEVSKNLVAM KEILYGTNEK EPQTEAVAQL AQELYNSGLL STLVADLQLI DFEGKKDVAQ IFNNILRRQI GTRTPTVEYI CTQQNILFML LKGYESPEIA LNCGIMLREC IRHEPLAKII LWSEQFYDFF RYVEMSTFDI ASDAFATFKD LLTRHKLLSA EFLEQHYDRF FSEYEKLLHS ENYVTKRQSL KLLGELLLDR HNFTIMTKYISKPENLKLMM NLLRDKSRNI QFEAFHVFKV FVANPNKTQP ILDILLKNQA KLIEFLSKFQ NDRTEDEQFN DEKTYLVKQI RDLKRPAQQE A.

    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.

    Cab39 Human
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