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Search results

1000 results found for “LIN Protein”

Name

Description

Product #

Price

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  • View Data Sheet

    Name :

    LIMD2 Human

    Description:

    LIM Domain Containing 2 Human Recombinant

    LIM Domain-Containing Protein 2

    Product # :

    PRO-1620

    Price :

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    Description

    LIMD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-127) and having a molecular mass of 16.5kDa.LIMD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIMD2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      LIMD2 is a protein-coding gene which holds one LIM zinc-binding domain. LIMD2 is related to illnesses such as intrahepatic cholangiocarcinoma and estrogen-receptor negative breast cancer.

    • Synonyms

      LIM Domain-Containing Protein 2

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMFQAAGA AQATPSHDAK GGGSSTVQRS KSFSLRAQVK ETCAACQKTV YPMERLVADK LIFHNSCFCC KHCHTKLSLG SYAALHGEFY CKPHFQQLFK SKGNYDEGFG RKQHKELWAH KEVDPGTKTA

    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.

    Limd2 Human
  • View Data Sheet

    Name :

    CETN3 Human

    Description:

    Centrin-3 Human Recombinant

    CEN3, CEN-3, CETN-3.

    Product # :

    PRO-533

    Price :

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    Description

    CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

    • Synonyms

      CEN3, CEN-3, CETN-3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
      KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
      AIMTGDI.

    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.

    Cetn3 Human
  • View Data Sheet

    Name :

    FURIN Human

    Description:

    Furin Human Recombinant

    Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    Product # :

    PRO-2199

    Price :

    Quantity :

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    Description

    FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

    • Synonyms

      Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

    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.

    Furin Human
  • View Data Sheet

    Name :

    CAPZA2 Human

    Description:

    Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant

    Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.

    Product # :

    PRO-1721

    Price :

    Quantity :

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    • description
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    • Citations

    Description

    CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.

    • Synonyms

      Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.

    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.

    Capza2 Human
  • View Data Sheet

    Name :

    MBP Protein

    Description:

    Myelin Basic Protein Human

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

    Product # :

    PRO-2798

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • More Info
    • Citations

    Description

    MBP Human produced in Human brain is checked using poly and monoclonal antibodies against MBP.

    Source

    Human brain.

    Formulation

    MBP was lyophilized containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Myelin Basic Protein (MBP) stands as a cornerstone in the intricate architecture of the nervous system. As a vital component of the myelin sheath, MBP plays a pivotal role in ensuring the integrity and rapid transmission of nerve impulses. Over the years, scientific inquiry into MBP has revealed its multifaceted functions, not only as a structural element but also as a regulatory molecule involved in various cellular processes. This research seeks to unravel the complexities of MBP, exploring its structural characteristics, physiological significance, and its involvement in neurological disorders.

      Structural Marvel of MBP:

      MBP, an intrinsically disordered protein, boasts a unique structure allowing it to interact with lipid membranes, especially those found in the myelin sheath. Its high arginine and lysine content gives it a positive charge, enabling strong electrostatic interactions with the negatively charged lipids in myelin. This structural adaptation is crucial for the compact wrapping of myelin around axons, facilitating efficient electrical signal conduction.

      Physiological Significance in Myelination:

      In the central nervous system (CNS), oligodendrocytes produce myelin, a lipid-rich substance that insulates axons. MBP, as a major constituent of myelin, plays an indispensable role in this process. It stabilizes the myelin sheath’s structure, ensuring its tight adherence to the axon and promoting the fast, saltatory conduction of nerve impulses. Without functional MBP, myelin integrity is compromised, leading to reduced nerve conduction velocity and impaired neural communication.

      Beyond Structural Functions:

      Recent studies have revealed that MBP is not merely a structural protein but also possesses regulatory functions. It participates in signaling pathways crucial for oligodendrocyte development and myelination. Moreover, MBP’s interaction with cytoskeletal elements suggests its involvement in cellular processes such as axon guidance and neuronal plasticity. Understanding these regulatory roles provides insights into the broader impact of MBP on neural development and function.

      Implications in Neurological Disorders:

      Alterations in MBP have been linked to various neurological disorders, including multiple sclerosis (MS). In MS, the immune system erroneously targets MBP, leading to demyelination and subsequent neurological impairments. Research into MBP-related pathologies not only aids in understanding disease mechanisms but also offers potential therapeutic avenues. Targeting MBP-specific immune responses is a focus of research for developing MS treatments.

      Conclusion:

      MBP, as the guardian of neural transmission, stands as a testament to the marvels of biological architecture. Its intricate structure and multifaceted functions make it indispensable for the proper functioning of the nervous system. Beyond its role as a structural protein, MBP’s involvement in cellular signalling adds layers to its significance. In the realm of neurological disorders, MBP’s complexities provide both challenges and opportunities, guiding scientists toward innovative therapies. This research delves into the world of MBP, appreciating its contributions to neuroscience while aiming to decipher the mysteries that lie within its molecular intricacies.

    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 Human
  • View Data Sheet

    Name :

    FABP4 Protein

    Description:

    Fatty Acid Binding Protein 4 Human Recombinant

    Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    Product # :

    PRO-416

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    Description

    14.7kDa protein containing 132 amino acid residues.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
      In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.

    • Synonyms

      Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA.

    • Specificity

      The amino acid sequence of the recombinant human FABP4 is 100% homologous to the amino acid sequence of the human FABP4.

    • Purification Method

      Two-step procedure using size exclusion chromatography before and after refolding.

    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.

    Fabp4 Human
  • View Data Sheet

    Name :

    Gliadin Alpha Wheat

    Description:

    Gliadin Alpha Wheat Recombinant

    Product # :

    PRO-2147

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    Description

    Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.

    Purity

    Protein is >90% pure.

    Citations

    More Info

    • Introduction

      Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
      LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
      QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
      WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
      QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.

    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.

    Gliadin Alpha Wheat
  • View Data Sheet

    Name :

    LXN Mouse

    Description:

    Latexin Mouse Recombinant

    Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    Product # :

    PRO-2218

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    Description

    LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

    • Synonyms

      Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    • 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 MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.

    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.

    Lxn Mouse
  • View Data Sheet

    Name :

    TAGLN3 Human

    Description:

    Transgelin-3 Human Recombinant

    Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    Product # :

    PRO-946

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    Description

    TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.

    • Synonyms

      Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    • 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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM

    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.

    Tagln3 Human
  • View Data Sheet

    Name :

    CEA Protein

    Description:

    Carcinoembryonic Antigen Human

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-2801

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    Description

    CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

    Source

    Liver tissue.

    Formulation

    CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • 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.

    • Applications

      Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.

    • Background

      Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.

      Structural Complexity of CEA:

      CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.

      CEA in Cancer Biology:

      CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.

      Beyond Cancer: CEA in Development and Inflammation:

      While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.

      CEA as a Diagnostic and Therapeutic Target:

      The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

    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.

    Cea 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.

    Citations

    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 :

    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 :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    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.

    Cystatin C Human Recombinant
  • View Data Sheet

    Name :

    LMNA Human

    Description:

    Lamin A/C Human Recombinant

    Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    Product # :

    PRO-2666

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    Description

    LMNA Human Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.5M NaCl, 1.5mM EDTA and 20%(v/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
      Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
      Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

    • Synonyms

      Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    • 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

      MAHHHHHHVG TGSNDDDDKS PDMETPSQRR ATRSGAQASS TPLSPTRITR LQEKEDLQEL NDRLAVYIDR VRSLETENAG LRLRITESEE VVSREVSGI KAAYEAELGD ARKTLDSVAK ERARLQLELS KVREEFKELK ARNTKKEGDL IAAQARLKDL EALLNSKEAA LSTALSEKRT LEGELHDLRG QVAKLEAALG EAKKQLQDEM LRRVDAENRL QTMKEELDFQ KNIYSEELRE TKRRHETRLV EIDNGKQREF ESRLADALQE LRAQHEDQVE QYKKELEKTY SAKLDNARQS AERNSNLVGA AHEELQQSRI RIDSLSAQLS QLQKQLAAKE AKLRDLEDSL ARERDTSRRL LAEKEREMAE MRARMQQQLD EYQELLDIKL ALDMEIHAYR KLLEGEEERL RLSPSPTSQR SRGRASSHSS QTQGGGSVTK KRKLESTESR SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV TVVEDDEDED GDDLLHHHHG SHCSSSGDPA EYNLRSRTVL CGTCGQPADK ASASGSGAQS PQNCSIM

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    Lmna Human
  • 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

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    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 :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    Citations

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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

    Protein A G His
  • View Data Sheet

    Name :

    Protein G

    Description:

    Protein G Recombinant

    Product # :

    PRO-402

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    Description

    The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized white powder containing no additives.

    Purity

    >96% as determined by SDS-PAGE and RP-HPLC.

    sds-page

    Protein-G sds-page - Product image 1

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Recombinant Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      Reconstitution with deionized water or PBS.

    • Amino Acid Sequence

      LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.

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

    Protein G
  • View Data Sheet

    Name :

    SEPT5 Human

    Description:

    Septin-5 Human Recombinant

    Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta chain.

    Product # :

    PRO-879

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    Description

    SEPT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 45.2 kDa.The SEPT5 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SEPT5 protein (0.25mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.3M NaCl, 1mM DTT and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SEPT5 is a member of the septin gene family of nucleotide binding proteins which were initially defined in yeast as cell division cycle regulatory proteins. Septins are extremely conserved in yeast, Drosophila, and mouse and seem to regulate cytoskeletal organization. Interference of septin function disrupts cytokinesis and results in high multinucleate or polyploid cells.

    • Synonyms

      Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta 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 MGSMSTGLRY KSKLATPEDK QDIDKQYVGF ATLPNQVHRK SVKKGFDFTL MVAGESGLGK STLVHSLFLT DLYKDRKLLS AEERISQTVE ILKHTVDIEE KGVKLKLTIV DTPGFGDAVN NTECWKPITD YVDQQFEQYF RDESGLNRKN IQDNRVHCCL YFISPFGHGL RPVDVGFMKA LHEKVNIVPL IAKADCLVPS EIRKLKERIR EEIDKFGIHV YQFPECDSDE DEDFKQQDRE LKESAPFAVI GSNTVVEAKG QRVRGRLYPW GIVEVENQAH CDFVKLRNML IRTHMHDLKD VTCDVHYENY RAHCIQQMTS KLTQDSRMES PIPILPLPTP DAETEKLIRM KDEELRRMQE MLQRMKQQMQ DQ

    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.

    Sept5 Human
  • View Data Sheet

    Name :

    MINA Human

    Description:

    MYC Induced Nuclear Antigen Human Recombinant

    MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    Product # :

    PRO-2078

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    Description

    MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MINA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.

    • Synonyms

      MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    • 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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.

    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.

    Mina Human
  • View Data Sheet

    Name :

    Protein-A/G/L

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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

    Protein A G L
  • View Data Sheet

    Name :

    REN Human

    Description:

    Renin Human Recombinant

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

    Product # :

    PRO-1529

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Ren Human
  • View Data Sheet

    Name :

    GAL Human

    Description:

    Galanin Prepropeptide Human Recombinant

    GALN, GLNN, GMAP, GAL, GAL1.

    Product # :

    PRO-1433

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    Description

    GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.

    • Synonyms

      GALN, GLNN, GMAP, GAL, GAL1.

    • 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 MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.

    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.

    Gal Human
  • View Data Sheet

    Name :

    Prelamin-A

    Description:

    Prelamin-A Recombinant

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

    Product # :

    PRO-689

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    Quantity :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Prelamin A
  • View Data Sheet

    Name :

    Noggin Human, Sf9

    Description:

    Noggin Human Recombinant, Sf9

    SYM1, SYNS1, NOG.

    Product # :

    CYT-1119

    Price :

    Quantity :

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    Shipped at Room temp

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    More Info

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

    Description

    Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

    Purity

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

    Biological Activity

    Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

    Citations

    More Info

    • Introduction

      Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.

    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.

    Noggin Protein
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