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Search results

1000 results found for “KCTD”

Name

Description

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  • View Data Sheet

    Name :

    RRAGC Human

    Description:

    Ras-Related GTP Binding C Human Recombinant

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

    Product # :

    PRO-1050

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    RRAGC Human
  • View Data Sheet

    Name :

    HCV Core 1-120

    Description:

    Hepatitis C Virus Nucleocapsid (core) 1-120 a.a. Recombinant

    Product # :

    HCV-006

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    Description

    Recombinant HCV Core 1-120 produced in E. coli is a single polypeptide chain containing 140 amino acids (aa 1-120) and having a molecular mass of 15.7kDa.Recombinant HCV Core 1-120 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCV Core protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNA virus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes (1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG.

    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.

    Hcv Core 1 120
  • View Data Sheet

    Name :

    ACAT1 Human

    Description:

    Acetyl-Coenzyme A acetyltransferase 1 Human Recombinant

    Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    Product # :

    ENZ-665

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    Description

    ACAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 417 amino acids (34-427) and having a molecular mass of 43.8 kDa.ACAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ACAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acetoacetyl-CoA thiolase (ACAT1) is an enzyme member of the membrane-bound acyltransferase family and Sterol o-acyltransferase subfamily. The ACAT1 enzyme catalyzes the reversible formation of acetoacetyl-CoA from 2 molecules of acetyl-CoA. ACAT1 plays a part in lipoprotein compilation and dietary cholesterol absorption. Added to its acyltransferase activity, ACAT1 acts as a ligase.

    • Synonyms

      Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    • 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 MGSVSKPTLK EVVIVSATRT PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK
      IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV LANIKMLEID
      PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL.

    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.

    Acat1 Human
  • View Data Sheet

    Name :

    CD116 Human

    Description:

    GM-CSF Receptor Alpha Human Recombinant

    CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

    Product # :

    CYT-796

    Price :

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    • sds-page

    Description

    CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    CD116 Human-sds-page - Product image 1

    More Info

    • Introduction

      GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

    • Synonyms

      CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

    • 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.

    • Background

      Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications

      Abstract:

      The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.

      Introduction:

      CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.

      Role in CNTF Signaling:

      CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.

      Production Methods:

      Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.

      Therapeutic Applications:

      Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.

      Challenges and Future Directions:

      While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.

      Conclusion:

      Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.

      What is the molecular weight/Mw of CD116 Protein?
      CD116 Protein has a total Mw of 37.2kDa.

      What is the source or expression system of CD116 Protein?
      Escherichia Coli.

      What is the Purity of CD116 Protein?
      CD116 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD116 Protein?
      The biological functionality of CD116 Protein will be determined in the future.

      What is the amino acid sequence of CD116 Protein?
      CD116 Protein is composed from 324 amino acids.

      What applications can CD116 Protein be used in?
      CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD116 Protein?
      The endotoxin level is minimal, CD116 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.

    Csf2Ra Human
  • View Data Sheet

    Name :

    CST11 Human

    Description:

    Cystatin 11 Human Recombinant

    CST8L, CTES2, dJ322G13.6, SC13.

    Product # :

    PRO-1475

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    Description

    CST11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (26-103 a.a.) and having a molecular mass of 11.8kDa.CST11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CST11 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatin 11 (CST11) is a member of the Cystatin family. The Cystatin superfamily is comprised of proteins with multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, other family members have lost or perhaps never developed this inhibitory activity. The Cystatin superfamily consists of three inhibitory families, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The majority of the type 2 cystatin genes and pseudogenes are contained in the cystatin locus on chromosome 20. CST11 is located in the cystatin locus and encodes an epididymal-specific protein whose specific function has not been verified yet.

    • Synonyms

      CST8L, CTES2, dJ322G13.6, SC13.

    • 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 MGSARKKTFL SVHEVMAVEN YAKDSLQWIT DQYNKESDDK YHFRIFRVLK VQRQQVNCFF SVFAVPWFEQ YKILNKSCSS D.

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    Cst11 Human
  • View Data Sheet

    Name :

    ADH1C Human

    Description:

    Alcohol Dehydrogenase 1C Human Recombinant

    Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.

    Product # :

    ENZ-622

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    Description

    ADH1C Human Recombinant produced in E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4 kDa.ADH1C is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH1C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

    • Synonyms

      Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.

    • 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 MGSHMSTAGK VIKCKAAVLW ELKKPFSIEE VEVAPPKAHE VRIKMVAAGI CRSDEHVVSG NLVTPLPVIL GHEAAGIVES VGEGVTTVKP GDKVIPLFTP QCGKCRICKN PESNYCLKND LGNPRGTLQD GTRRFTCSGK PIHHFVGVST FSQYTVVDEN AVAKIDAASP LEKVCLIGCG FSTGYGSAVK VAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN KDKFAKAKEL GATECINPQD YKKPIQEVLK EMTDGGVDFS FEVIGRLDTM MASLLCCHEA CGTSVIVGVP PDSQNLSINP MLLLTGRTWK GAIFGGFKSK ESVPKLVADF MAKKFSLDAL ITNILPFEKI NEGFDLLRSG KSIRTVLTF.

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    Adh1C Human
  • View Data Sheet

    Name :

    CTSZ Human

    Description:

    Cathepsin-Z Human Recombinant

    Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    Product # :

    ENZ-748

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    Description

    CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    • 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 MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.

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    Ctsz Human
  • View Data Sheet

    Name :

    Cyclophilin D Human, His

    Description:

    Cyclophilin-D Human Recombinant, His Tag

    Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.

    Product # :

    ENZ-367

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    Description

    Cyclophilin-D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (amino acids 1-370) containing 390 amino acids and having a molecular mass of 42.9kDa. Cyclophilin-D is fused to a 20 aa His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 1x PBS pH-7.4 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.

    • Synonyms

      Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.

    • 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 MSHPSPQAKP SNPSNPRVFFDVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSMANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGEKPAKLCVIAE CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE MAIKKYAEVL RYVDSSKAVI ETADRAKLQPIALSCVLNIG ACKLKMSNWQ GAIDSCLEAL ELDPSNTKAL YRRAQGWQGLKEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK EKAVYAKMFA.

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    Cyclophilin D Human
  • View Data Sheet

    Name :

    AICDA Human

    Description:

    Activation-Induced Cytidine Deaminase Human Recombinant

    Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    Product # :

    ENZ-651

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    Description

    AICDA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198) and having a molecular mass of 26.1kDa.AICDA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AICDA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Activation-Induced Cytidine Deaminase (AICDA) belongs to the the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. AICDA is necessary for a number of crucial steps of B-cell terminal differentiation needed for efficient antibody responses. AICDA has a role in the epigenetic regulation of gene expression by participating in DNA demethylation. AICDA is strongly expressed in the lymph nodes and tonsils.

    • Synonyms

      Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    • 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 MDSLLMNRRK FLYQFKNVRW AKGRRETYLC YVVKRRDSAT SFSLDFGYLR NKNGCHVELL FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVADFLRG NPNLSLRIFT ARLYFCEDRK AEPEGLRRLH RAGVQIAIMT FKDYFYCWNT FVENHERTFK
      AWEGLHENSV RLSRQLRRIL LPLYEVDDLR DAFRTLGL.

    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.

    Aicda Human
  • View Data Sheet

    Name :

    AK3L1 Human

    Description:

    Adenylate Kinase-3 Like 1 Human Recombinant

    AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.

    Product # :

    PKA-346

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    Description

    AK3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids (1-223) and having a molecular mass of 29.3 kDa. The AK3L1 is fused with 35 amino acid His-tag at N-terminus.AK3L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK3L1 solution containing 20mM Tris-HCl pH-8, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AK3L1 is an affiliate of the adenylate kinase family of enzymes. AK3L1 enzyme is restricted to the mitochondrial matrix. Adenylate kinases-3 regulates the adenine and guanine nucleotide compositions within a cell by means of catalyzing the reversible transfer of phosphate group among these nucleotides. 5 different isozymes of adenylate kinase have been identified in vertebrates. The enzyme expression of various adenylate kinase isozymes is growth regulated and tissue-specific.

    • Synonyms

      AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.

    • 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 KDRWGSMASK LLRAVILGPP GSGKGTVSQR IAQNFGLQHL SSGHFLRENIKASTEVGEMA KQYIEKSLLV PDHVITRLMM SELENRRGQH WLLDGFPRTL GQAEALDKIC EVDLVISLNI PFETLKDRLS RRWIHPPSGR VYNLDFNPPH VHGIDDVTGE PLVQQEDDKP EAVAARLRQY KDVAKPVIEL YKSRGVLHQF SGTETNKIWP YVYTLFSNKI TPIQSKEAY.

    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.

    Ak3L1 Human
  • View Data Sheet

    Name :

    MTCP1 Human

    Description:

    Mature T-Cell Proliferation 1 Human Recombinant

    Mature T-Cell Proliferation 1, Mature T-Cell Proliferation-1 Type B1, MTCP-1 Type B1, P13MTCP1, Mature T-Cell Proliferation 1 Isoform P13, p8MTCP1, Protein P13 MTCP-1, C6.1B, p13MTCP1.

    Product # :

    PRO-1748

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    Description

    MTCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107a.a) and having a molecular mass of 15.0kDa.MTCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MTCP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl ,10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mature T-Cell Proliferation 1, also known as MTCP1 was recognized by involvement in some t(X;14) translocations linked with mature T-cellproliferations. This region has a complex gene structure, with a common promoter and 5' exon spliced to two dissimilar sets of 3' exons which encode two different proteins. It represents the upstream 13 kDa protein which belongs to the TCL1 family. In addition, MTCP1 enhances the phosphorylation and activation of AKT1 and AKT2. MTCP1 is involved in leukemogenesis.Among the diseases associated with MTCP1 are queensland tick typhus, and african tick-bite fever.

    • Synonyms

      Mature T-Cell Proliferation 1, Mature T-Cell Proliferation-1 Type B1, MTCP-1 Type B1, P13MTCP1, Mature T-Cell Proliferation 1 Isoform P13, p8MTCP1, Protein P13 MTCP-1, C6.1B, p13MTCP1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGEDVG APPDHLWVHQ EGIYRDEYQR TWVAVVEEET SFLRARVQQI QVPLGDAARP SHLLTSQLPL MWQLYPEERY MDNNSRLWQI QHHLMVRGVQ ELLLKLLPDD

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    Mtcp1 Human
  • View Data Sheet

    Name :

    ALDOC Human

    Description:

    Aldolase C Fructose-Bisphosphate Human Recombinant

    Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 3.

    Product # :

    ENZ-969

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    Description

    ALDOC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-364 a.a) and having a molecular mass of 39.4kDa. ALDOC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDOC protein solution (1mg/ml) containing 20mM Tris-Hcl Buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

    • Synonyms

      Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 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

      MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY.

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    Human Aldoc
  • View Data Sheet

    Name :

    DKK1 Human

    Description:

    Dickkopf-Related Protein 1 Human Recombinant

    Dickkopf-related protein 1, Dickkopf-1, Dkk-1, hDkk-1, SK, DKK1, dickkopf WNT signaling pathway inhibitor 1, Dickkopf 1 Homolog, Dickkopf Related Protein-1, Dickkopf-1 Like, Dickkopf-Like Protein 1, Dickkopf (Xenopus Laevis) Homolog 1, DKK-1.

    Product # :

    PRO-1566

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    Description

    DKK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (32-266 a.a) and having a molecular mass of 28.2kDa.DKK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DKK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 1 (DKK1) antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by creating a ternary complex with the transmembrane protein KREMEN which promotes internalization of LRP5/6. DKKs have a significant role in vertebrate development, where they locally inhibit Wnt controlled processes for instance antero-posterior axial patterning, limb development, somitogenesis and eye formation. Furthermore, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease in Adults.

    • Synonyms

      Dickkopf-related protein 1, Dickkopf-1, Dkk-1, hDkk-1, SK, DKK1, dickkopf WNT signaling pathway inhibitor 1, Dickkopf 1 Homolog, Dickkopf Related Protein-1, Dickkopf-1 Like, Dickkopf-Like Protein 1, Dickkopf (Xenopus Laevis) Homolog 1, DKK-1.

    • 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 MGSTLNSVLN SNAIKNLPPP LGGAAGHPGS AVSAAPGILY PGGNKYQTID NYQPYPCAED EECGTDEYCA SPTRGGDAGV QICLACRKRR KRCMRHAMCC PGNYCKNGIC VSSDQNHFRG EIEETITESF GNDHSTLDGY SRRTTLSSKM YHTKGQEGSV CLRSSDCASG LCCARHFWSK ICKPVLKEGQ VCTKHRRKGS HGLEIFQRCY CGEGLSCRIQ KDHHQASNSS RLHTCQRH.

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    Human Dkk1
  • View Data Sheet

    Name :

    DLD Human

    Description:

    Dihydrolipoamide Dehydrogenase Human Recombinant

    EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.

    Product # :

    ENZ-502

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    Description

    DLD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids (36-509 a.a.) and having a molecular mass of 54.4 kDa. The DLD is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DLD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.

    • Synonyms

      EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMADQ PIDADVTVIG SGPGGYVAAI KAAQLGFKTV CIEKNETLGG TCLNVGCIPS KALLNNSHYY HMAHGKDFAS RGIEMSEVRL NLDKMMEQKS TAVKALTGGI AHLFKQNKVV HVNGYGKITG KNQVTATKAD GGTQVIDTKN ILIATGSEVT PFPGITIDED TIVSSTGALS LKKVPEKMVV IGAGVIGVEL GSVWQRLGAD VTAVEFLGHV GGVGIDMEIS KNFQRILQKQ GFKFKLNTKV TGATKKSDGK IDVSIEAASG GKAEVITCDV LLVCIGRRPF TKNLGLEELG IELDPRGRIP VNTRFQTKIP NIYAIGDVVA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ LKEEGIEYKV GKFPFAANSR AKTNADTDGM VKILGQKSTD RVLGAHILGP GAGEMVNEAA LALEYGASCE DIARVCHAHP TLSEAFREAN LAASFGKSIN F.

    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.

    Dld Human
  • View Data Sheet

    Name :

    DPP4 Human

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant

    CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    Product # :

    ENZ-375

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    Description

    DPPIV Human Recombinant produced in Insect cells is a single, glycosylated polypeptide chain containing 737 amino acids (39-766) and having a molecular mass of 85.4kDa.DPPIV is fused to a 6 His Tag at C-terminus and purified using conventional chromatography techniques.

    Source

    Insect cells.

    Formulation

    DPP4 is formulated in 20mM Tris-HCl buffer pH-8, 100mM NaCl, 1mM EDTA and 10% glycerol.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    >200 Units/mg.

    More Info

    • Introduction

      DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

    • Synonyms

      CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 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.

    • Amino Acid Sequence

      ADPSRKTYTL TDYLKNTYRL KLYSLRWISD HEYLYKQENN ILVFNAEYGN SSVFLENSTF DEFGHSINDY SISPDGQFIL LEYNYVKQWR HSYTASYDIY DLNKRQLITE ERIPNNTQWV TWSPVGHKLA YVWNNDIYVK IEPNLPSYRI TWTGKEDIIY NGITDWVYEE EVFSAYSALW WSPNGTFLAY AQFNDTEVPL IEYSFYSDES LQYPKTVRVP YPKAGAVNPT VKFFVVNTDS LSSVTNATSI QITAPASMLI GDHYLCDVTW ATQERISLQW LRRIQNYSVM DICDYDESSG RWNCLVARQH IEMSTTGWVG RFRPSEPHFT LDGNSFYKII SNEEGYRHIC YFQIDKKDCT FITKGTWEVI GIEALTSDYL YYISNEYKGM PGGRNLYKIQ LSDYTKVTCL SCELNPERCQ YYSVSFSKEA KYYQLRCSGP GLPLYTLHSS VNDKGLRVLE DNSALDKMLQ NVQMPSKKLD FIILNETKFW YQMILPPHFD KSKKYPLLLD VYAGPCSQKA DTVFRLNWAT YLASTENIIV ASFDGRGSGY QGDKIMHAIN RRLGTFEVED QIEAARQFSK MGFVDNKRIA IWGWSYGGYV TSMVLGSGSG VFKCGIAVAP VSRWEYYDSV YTERYMGLPT PEDNLDHYRN STVMSRAENF KQVEYLLIHG TADDNVHFQQ SAQISKALVD VGVDFQAMWY TDEDHGIASS TAHQHIYTHM SHFIKQCFSL PHHHHHH.

    • Unit Definition

      One unit will hydrolyze 1 umole of p-nitroaniline per minute at pH8.0 at 37°C using 1mM of Gly-Pro p-nitroanilde as a substrate.

    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.

    Dpp4 Human
  • View Data Sheet

    Name :

    ASMT Human

    Description:

    Acetylserotonin O-Methyltransferase Human Recombinant

    HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    Product # :

    ENZ-664

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    Description

    ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

    • Synonyms

      HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    • 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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

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    Asmt Human
  • View Data Sheet

    Name :

    ECH1 Human

    Description:

    Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant

    peroxisomal, enoyl Coenzyme A hydratase 1.

    Product # :

    ENZ-562

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    Description

    ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

    • Synonyms

      peroxisomal, enoyl Coenzyme A hydratase 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTGSSAQEAA SGVALGEAPD HSYESLRVTS AQKHVLHVQL NRPNKRNAMN KVFWREMVEC FNKISRDADC RAVVISGAGK MFTAGIDLMD MASDILQPKG DDVARISWYL RDIITRYQET FNVIERCPKP VIAAVHGGCI GGGVDLVTAC DIRYCAQDAF FQVKEVDVGL AADVGTLQRL PKVIGNQSLV NELAFTARKM MADEALGSGL VSRVFPDKEV MLDAALALAA EISSKSPVAV QSTKVNLLYS RDHSVAESLN YVASWNMSML QTQDLVKSVQ ATTENKELKT VTFSKL.

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    Ech1 Human
  • View Data Sheet

    Name :

    NMT2 Human

    Description:

    N-Myristoyltransferase 2 Human Recombinant

    Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.

    Product # :

    ENZ-068

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    Description

    NMT2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 518 amino acids (1-498 a.a.) and having a molecular mass of 59.1kDa. The NMT2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NMT2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycylpeptide N-tetradecan-oyltransferases 2 (NMT2) is a cytoplasmic protein which is a member of the NMT family of proteins. The proteins in the NMT family catalyze the addition of a myristoyl group to the N-terminal glycine residue of eukaryotic, fungal and viral proteins. These proteins are mostly detected in the heart, gut, kidney, liver and placenta. NMT catalyzes the reaction of N-terminal myristoylation of various signaling proteins. NMT transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. There are several distinct NMTs which vary in the molecular weight and /or subcellular distribution.

    • Synonyms

      Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH RSLNPKKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL YNWRCPGTDS EKVGLVLQ.

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    Nmt2 Human
  • View Data Sheet

    Name :

    BD 3 Mouse

    Description:

    Beta Defensin-3 Mouse Recombinant

    Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    Product # :

    CYT-036

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    Description

    Beta Defensin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.6kDa. The BD-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse BD-3 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

    More Info

    • Introduction

      Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

    • Synonyms

      Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

    • Background

      What is the molecular weight/Mw of BD3 Protein?
      BD3 Protein has a total Mw of 4.6kDa.

      What is the source or expression system of BD3 Protein?
      Escherichia Coli.

      What is the Purity of BD3 Protein?
      BD3 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD3 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

      What is the amino acid sequence of BD3 Protein?
      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

      What applications can BD3 Protein be used in?
      BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD3 Protein?
      The endotoxin level is minimal, BD3 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.

    Bd 3 Mouse
  • View Data Sheet

    Name :

    NXT2 Human

    Description:

    NTF2-like Export Factor 2 Human Recombinant

    NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    Product # :

    PRO-1051

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    Description

    NXT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-197 a.a) and having a molecular mass of 25.3kDa.NXT2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NXT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear transport factor 2-like export factor 2 (NXT2) belongs to the NXT family proteins which are commonly involved in exporting nuclear RNA in eukaryotic cells. The NXT2 protein is a regulator of protein export for NES-containing proteins. In addition, NXT2 associates with NXF1, NXF2, NXF3 and NXF5 and has a role in mRNA nuclear export. NXT2 has a critical role in upholding morphogenetic integrity of embryonic heart in vertebrate species. The NXT2 protein contains a nuclear transport factor 2 (NTF2) domain, which has a vital role in the trafficking of macromolecules, ions, and small molecules between the cytoplasm and nucleus, it may also have a role in mRNA nuclear export.

    • Synonyms

      NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    • 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 MGSHMRKYRS HWSQGDREGY QRRSNYYEGP HTSHSSPADR TREEVVTPTL PEHTATRSQM ATSLDFKTYV DQACRAAEEF VNIYYETMDK RRRALTRLYL DKATLIWNGN AVSGLDALNN FFDTLPSSEF QVNMLDCQPV HEQATQSQTT VLVVTSGTVK
      FDGNKQHFFN QNFLLTAQST PNNTVWKIAS DCFRFQDWSS S.

    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.

    Nxt2 Human
  • View Data Sheet

    Name :

    STC 2 Human, His

    Description:

    Stanniocalcin-2 Human Recombinant, His Tag

    Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    Product # :

    HOR-008

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    Description

    STC 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (25-302 a.a.) and having a molecular mass of 33kDa. STC 2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STC 2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.25M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.

    • Synonyms

      Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    • 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 MGSTDATNPP EGPQDRSSQQ KGRLSLQNTA EIQHCLVNAG DVGCGVFECF ENNSCEIRGL HGICMTFLHN AGKFDAQGKS FIKDALKCKA HALRHRFGCI SRKCPAIREM VSQLQRECYL KHDLCAAAQE NTRVIVEMIH FKDLLLHEPY VDLVNLLLTC GEEVKEAITH SVQVQCEQNW GSLCSILSFC TSAIQKPPTA PPERQPQVDR TKLSRAHHGE AGHHLPEPSS RETGRGAKGE RGSKSHPNAH ARGRVGGLGA QGPSGSSEWE DEQSEYSDIR R.

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    Stc 2 Human His
  • View Data Sheet

    Name :

    PBLD Human

    Description:

    Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant

    Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    Product # :

    PRO-010

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    Description

    PBLD Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PBLD solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

    • Synonyms

      Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    • 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 MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.

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    Pbld Human
  • View Data Sheet

    Name :

    PCID2 Human

    Description:

    PCI Domain Containing 2 Human Recombinant

    PCI Domain Containing 2, CSN12-Like Protein, PCI Domain-Containing Protein 2, F10, PCI domain-containing protein 2.

    Product # :

    PRO-2074

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PCID2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (80-399 a.a) and having a molecular mass of 39.3kDa. PCID2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PCID2 protein solution (1.0 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCI Domain Containing 2 (PCID2) is expressed in immature and early-stage B lymphocytes and regulates the expression of mitotic checkpoint protein MAD2. PCID2 is a component of the TREX-2 complex, transcription and export complex 2, this complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex, nuclear basket.

    • Synonyms

      PCI Domain Containing 2, CSN12-Like Protein, PCI Domain-Containing Protein 2, F10, PCI 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 MAYKCQTVIV QSFLRAFQAH KEENWALPVM YAVALDLRVF ANNADQQLVK KGKSKVGDML EKAAELLMSC FRVCASDTRA GIEDSKKWGM LFLVNQLFKI YFKINKLHLC KPLIRAIDSS NLKDDYSTAQ RVTYKYYVGR KAMFDSDFKQ AEEYLSFAFE HCHRSSQKNK RMILIYLLPV KMLLGHMPTV ELLKKYHLMQ FAEVTRAVSE GNLLLLHEAL AKHEAFFIRC GIFLILEKLK IITYRNLFKK VYLLLKTHQL SLDAFLVALK FMQVEDVDID EVQCILANLI YMGHVKGYIS HQHQKLVVSK QNPFPPLSTV C.

    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.

    Pcid2 Human
  • View Data Sheet

    Name :

    BTF3L4 Human

    Description:

    Basic Transcription Factor 3-Like 4 Human Recombinant

    Basic transcription factor 3-like 4, BTF3L4.

    Product # :

    PRO-1870

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    Description

    BTF3L4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 11.3kDa. BTF3L4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BTF3L4 protein solution (1mg/ml) containing 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

      BTF3L4 is a part of the NAC-beta family which contains 1 NAC-A/B (NAC-alpha/beta) domain and required for the initiation of transcription. BTF3L4 binds to polypeptide chains as they emerge from the ribosome and prevents their interaction with the SRP, which usually targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor which forms a stable complex with RNA polymerase II.

    • Synonyms

      Basic transcription factor 3-like 4, BTF3L4.

    • 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 MGSMNQEKLA KLQAQVRIGG KGTARRKKKV VHRTATADDK KLQSSLKKLA VNNIAGIEES WTVKHQNQKT LMRKMMMFQI L.

    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.

    Btf3L4 Human
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